SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3607478 FitnessBrowser__Dino:3607478 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

D2Z027 O-ureido-L-serine synthase; Cysteine synthase homolog DscD; O-acetylserine sulfhydrylase; EC 2.6.99.3; EC 2.5.1.47 from Streptomyces lavendulae (see paper)
49% identity, 91% coverage: 17:345/360 of query aligns to 4:312/324 of D2Z027

query
sites
D2Z027

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K43 (= K56) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
V74 (≠ T87) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
Y97 (≠ F110) mutation to F: KM for OAS is unchanged, KM for H(2)S is 0.073 mM.; mutation to M: KM for OAS is 330 mM, KM for H(2)S is 0.084.
S121 (≠ G134) mutation to A: KM for OAS is 140 mM, KM for H(2)S is 0.095 mM.; mutation to M: KM for OAS is 44 mM, KM for H(2)S is 0.20 mM.

3x43A Crystal structure of o-ureido-l-serine synthase (see paper)
49% identity, 91% coverage: 17:345/360 of query aligns to 3:311/316 of 3x43A

query
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3x43A

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active site: K42 (= K56), S264 (= S298)
binding pyridoxal-5'-phosphate: K42 (= K56), N72 (= N86), F175 (≠ Y189), G176 (= G190), T177 (= T191), T178 (≠ G192), T180 (= T194), G220 (= G250), S264 (= S298), P290 (= P324), D291 (= D325)

3x44A Crystal structure of o-ureido-l-serine-bound k43a mutant of o-ureido- l-serine synthase (see paper)
49% identity, 91% coverage: 17:345/360 of query aligns to 3:311/321 of 3x44A

query
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3x44A

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active site: A42 (≠ K56), S264 (= S298)
binding (E)-O-(carbamoylamino)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: T69 (= T83), S70 (= S84), N72 (= N86), V73 (≠ T87), S120 (≠ G134), Q141 (= Q155), F175 (≠ Y189), G176 (= G190), T177 (= T191), T178 (≠ G192), T180 (= T194), G220 (= G250), L221 (≠ W251), P223 (= P253), S264 (= S298), P290 (= P324), D291 (= D325)

P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 90% coverage: 18:341/360 of query aligns to 5:310/310 of P9WP55

query
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P9WP55

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F

K

E

G

P

P

H

H

P

P

I

I

Q

Q

G

G

W

I

T

G

P

A

D

G

F

F

I

V

P

P

K

P

V

V

L

L

Q

-

E

-

S

-

I

-

D

D

Q

Q

G

D

F

L

Y

V

D

D

A

E

L

I

P

T

V

V

A

G

G

N

A

E

D

D

G

A

I

L

A

N

W

V

A

A

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R

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L

A

A

A

R

E

E

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G

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L

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|
S

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S

G

G

S

A

T

A

F

T

A

V

I

A

S

A

H

L

E

Q

V

V

A

A

K

R

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

V

L

I

I

L

V

C

V

M

V

L

L

P

P

D

D

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E

E

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Y

L

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T

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L

F

F

E

A

G

D

I

V

V

A

E

D

K44 (= K56) modified: N6-(pyridoxal phosphate)lysine
N74 (= N86) binding
GTGGT 178:182 (= GTGGT 190:194) binding
S266 (= S298) binding

2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
43% identity, 89% coverage: 18:336/360 of query aligns to 5:305/306 of 2q3dA

query
sites
2q3dA

D

E

S

D

V

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D

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-

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E

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A

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E

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F

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N

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A

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K

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D

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T

G

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A

A

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C

A

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D

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E

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-

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x
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|
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|
T

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I

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G

G

L

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G

A

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V

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K

E

A

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E

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T

A

K

R

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I

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L

A

T

V

E

E

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P

A

A

N

-

A

-

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-

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-

S

-

G

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I

-

A

-

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-

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-

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-

D

-

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-

N

-

G

A

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A

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V

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S

G

A

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H

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|
G

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x
I

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G

F

F

I

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P

K

P

V

V

L

L

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-

E

-

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-

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-

D

D

Q

Q

G

D

F

L

Y

V

D

D

A

E

L

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P

T

V

V

A

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G

N

A

E

D

D

G

A

I

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A

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W

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A

A

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L

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A

A

R

E

E

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G

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|
S

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S

G

G

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A

T

A

F

T

A

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I

A

S

A

H

L

E

Q

V

V

A

A

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R

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

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L

I

I

L

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C

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M

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|
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|
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G

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Y

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S

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P

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L

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F

active site: K44 (= K56), S266 (= S298), P293 (= P324)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K56), T71 (= T83), S72 (= S84), N74 (= N86), T75 (= T87), Q144 (= Q155), V177 (≠ Y189), G178 (= G190), T179 (= T191), G180 (= G192), T182 (= T194), G222 (= G250), I223 (≠ W251), S266 (= S298), P293 (= P324), D294 (= D325)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
42% identity, 87% coverage: 18:331/360 of query aligns to 5:300/300 of 3zeiA

query
sites
3zeiA

D

E

S

D

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T

D

Q

T

L

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I

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G

N

R

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A

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E

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G

A

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-

A

E

D

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I

Y

V

V

A

K

K

A

L

E

E

F

F

N

N

P

P

A

A

A

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S

V

V

K
|
K

D

D

R

R

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I

A

G

L

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A

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M

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A

A

E

E

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A

A

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G

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T

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I

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T

S
|
S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

V

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C

A

A

Q

A

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Y

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C

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V

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L

T

T

M

M

A

P

E

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S

T

F

M

S

S

I

L

E

E

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R

K

M

L

L

M

L

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R

L

A

L

Y

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G

A

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L

V

I

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L

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T

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P

R

G

A

A

E

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G

G

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G

G

M

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x
I

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K

A

A

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E

E

L

L

A

A

E

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A

T

N

D

G

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-

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Y

F

F

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A

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Q

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|
F

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A

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A

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E

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I

H

H

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A

A

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E

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E

I

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R

D

D

F

T

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G

G

C

-

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D

Y

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I

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G

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x
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|
T

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|
G

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G

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A

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R

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I

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L

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E

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A

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-

A

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-

L

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-

S

-

G

-

I

-

A

-

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-

D

-

R

-

D

-

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-

N

-

G

A

A

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P

A

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V

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H

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S

G

A

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F
x
K

E

G

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H

H

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I

I

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G
|
G

W

I

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x
A

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|
F

I

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P

K

P

V

V

L

L

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-

E

-

S

-

I

-

D

D

Q

Q

G

D

F

L

Y

V

D

D

A

E

L

I

P

T

V

V

A

G

G

N

A

E

D

D

G

A

I

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A

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W

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A

A

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L

L

A

A

A

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E

E

G

G

I

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L

L

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G

G

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|
S

G

S

G

G

S

A

T

A

F

T

A

V

I

A

S

A

H

L

E

Q

V

V

A

A

K

R

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

V

L

I

I

L

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C

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M

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D

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G

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E

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Y

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L

active site: K44 (= K56), S266 (= S298), P293 (= P324)
binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (= T83), S72 (= S84), I126 (≠ Y138), Q144 (= Q155), F145 (= F156), K215 (≠ F243), G222 (= G250), A225 (≠ P253), F227 (= F255)
binding pyridoxal-5'-phosphate: K44 (= K56), N74 (= N86), V177 (≠ Y189), G178 (= G190), T179 (= T191), G180 (= G192), T182 (= T194), G222 (= G250), S266 (= S298), P293 (= P324), D294 (= D325)

2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
42% identity, 87% coverage: 18:331/360 of query aligns to 5:300/300 of 2q3cA

query
sites
2q3cA

D

E

S

D

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G

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-

A

E

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A

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K

A

L

E

E

F

F

N

N

P

P

A

A

A

N

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S

V

V

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|
K

D

D

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I

A

G

L

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A

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A

A

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A

A

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D

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I

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I

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E

E

A

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T

S
|
S

G
|
G

N

N

T
|
T

G

G

I

I

G

A

L

L

A

A

M

M

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C

A

A

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A

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G

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C

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M

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A

A

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x
M

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A

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I

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A

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K

A

A

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E

E

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L

L

A

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A

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G

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F

F

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A

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A

A

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N

A

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E

A

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I

H

H

E

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N

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T

A

A

Q

E

E

E

I

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R

D

D

F

T

E

D

G

G

C

-

K

K

L

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I

I

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V

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A

G

G

Y

V

G

G

T

T

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G

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I

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T

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G

L

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G

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V

V

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I

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K

E

A

R

R

K

P

P

E

S

T

A

K

R

I

F

I

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L

A

T

V

E

E

P

P

A

A

N

-

A

-

Q

-

L

-

G

-

S

-

G

-

I

-

A

-

Q

-

D

-

R

-

D

-

P

-

N

-

G

A

A

S

P

P

A

V

V

L

S

S

H

G

S

G

A

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F
x
K

E

G

P

P

H

H

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P

I

I

Q

Q

G
|
G

W

I

T

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x
A

D

G

F

F

I

V

P

P

K

P

V

V

L

L

Q

-

E

-

S

-

I

-

D

D

Q

Q

G

D

F

L

Y

V

D

D

A

E

L

I

P

T

V

V

A

G

G

N

A

E

D

D

G

A

I

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A

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W

V

A

A

R

R

L

L

A

A

A

R

E

E

G

G

I

L

L

L

T

V

G

G

I

I

S
|
S

G

S

G

G

S

A

T

A

F

T

A

V

I

A

S

A

H

L

E

Q

V

V

A

A

K

R

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

V

L

I

I

L

V

C

V

M

V

L

L

P
|
P

D

D

T

F

G

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K56), S266 (= S298), P293 (= P324)
binding : T71 (= T83), S72 (= S84), G73 (= G85), T75 (= T87), M122 (≠ G134), Q144 (= Q155), K215 (≠ F243), G222 (= G250), A225 (≠ P253)

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
43% identity, 88% coverage: 22:339/360 of query aligns to 10:309/310 of 5xoqA

query
sites
5xoqA

D

E

T

S

V

I

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G

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P

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A

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K

A

I

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E

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G

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R

N

N

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P

A

A

A

Y

S

S

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V

K

K

D

C

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T

S
|
S

G
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G

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N

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|
T

G

G

I

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A

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A

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F

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C

A

A

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A

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M

M

A

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E

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M

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M

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A

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K

D

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L

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L

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A

A

E

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K

G

G
x
M

F

K

G

G

M

A

Y

I

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K

K

A

A

V

E

E

E

L

L

A

A

E

A

A

Q

N

P

G

G

W

W

F

F

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I

A

P

S

Q

Q
|
Q

F

F

E

K

T

N

A

P

A

A

N

N

A

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E

A

M

I

H

H

E

V

N

K

T

T

A

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E

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I

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G

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D

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F

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E

E

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K

Q

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D

D

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binding : T72 (= T83), S73 (= S84), G74 (= G85), T76 (= T87), M123 (≠ G134), Q144 (= Q155), R218 (≠ A235), H219 (= H246), Q222 (= Q249), G223 (= G250), A226 (≠ P253)

P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
38% identity, 88% coverage: 15:332/360 of query aligns to 75:383/551 of P35520

query
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P35520

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P78 (≠ D18) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
G85 (= G25) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T27) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
L101 (vs. gap) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
K102 (≠ G39) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
C109 (≠ A46) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P51) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
K119 (= K56) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ N62) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
M126 (≠ I63) to V: in CBSD; loss of activity
E131 (= E68) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G76) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ V80) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E81) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G85) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N86) binding
L154 (= L91) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A92) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
C165 (≠ L102) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
M173 (≠ F110) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
E176 (= E113) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
V180 (≠ L117) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (= T128) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ A141) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (= A159) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N161) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
A231 (≠ M164) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ N167) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
GTGGT 256:260 (= GTGGT 190:194) binding
T257 (= T191) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (= T196) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
R266 (= R200) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (≠ R203) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ R206) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ T209) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
I278 (= I212) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
D281 (≠ E215) to N: in CBSD; loss of activity
A288 (= A227) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ S241) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
G305 (= G250) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (≠ T252) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
V320 (≠ Y269) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D270) to V: in CBSD; loss of activity
R336 (= R285) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
L338 (= L287) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
G347 (= G296) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S298) binding ; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
T353 (= T302) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ V318) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D325) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ E328) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586

Sites not aligning to the query:

18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
52 binding axial binding residue
58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
69 A → P: in dbSNP:rs17849313
384 K → E: in CBSD; severe form; dbSNP:rs121964967
422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
38% identity, 89% coverage: 15:335/360 of query aligns to 35:346/500 of 7qgtB

query
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7qgtB

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P
|
P

D
|
D

T

S

G

V

E

R

R

N

Y

Y

L

M

S

T

T

K

P

F

L

L

binding protoporphyrin ix containing fe: A186 (= A159), P189 (≠ A162), L190 (≠ E163), Y193 (≠ E166), R226 (= R200)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K56), T106 (= T83), S107 (= S84), N109 (= N86), T110 (= T87), Q182 (= Q155), G216 (= G190), T217 (= T191), G218 (= G192), T220 (= T194), G265 (= G250), S309 (= S298), P335 (= P324), D336 (= D325)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 10, 11, 12, 13, 14, 23, 24, 25

7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
38% identity, 89% coverage: 15:335/360 of query aligns to 35:346/500 of 7qgtA

query
sites
7qgtA

K

K

T

I

Y

L

D

P

S

D

V

I

L

L

D

K

T

K

V

I

G

G

N

D

T

T

P

P

V

M

I

V

R

R

I

I

N

N

N

K

L

I

A

G

P

K

E

K

-

F

-

G

-

L

G

K

V

C

E

E

L

L

Y

L

V

A

K

K

A

C

E

E

F

F

N

N

P

A

A

G

S

S

V

V

K
|
K

D

D

R

R

L

I

A

S

L

L

N

R

I

M

I

I

E

E

A

D

A

A

E

E

R

R

A

D

G

G

T

T

L

L

K

K

P

P

G

G

Q

D

T

T

V

I

E

E

A

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

M

L

V

A

C

A

A

A

Q

V

K

R

G

G

Y

Y

P

R

L

C

V

I

I

I

T

V

M

M

A

P

E

E

S

K

F

M

S

S

I

S

E

E

R

K

R

V

K

D

L

V

M

L

R

R

L

A

L

L

G

G

A

A

K

E

V

I

V

V

L

R

T

T

P

P

-

T

-

N

-

A

-

R

-

F

-

D

R

S

A

P

E

E

K

S

G

H

F

V

G

G

M

V

-

A

Y

W

R

R

K

L

A

K

V

N

E

E

L

I

A

P

E

N

A

S

N

H

G

-

W

-

F

-

L

I

A

L

S

D

Q

Q

F

Y

E

R

T

N

A
|
A

A

S

N

N

A
x
P

E
x
L

M

A

H

H

E
x
Y

N

D

T

T

A

A

Q

D

E

E

I

I

L

L

G

Q

D

Q

F

C

E

D

G

G

C

-

K

K

L

L

D

D

Y

M

I

L

V

V

T

A

G

S

Y

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

V

I

T

T

G

G

L

I

G

A

R
|
R

V

K

L

L

R

K

K

E

A

K

R

C

P

P

E

G

T

C

K

R

I

I

L

G

T

V

E

D

P

P

A

E

N

-

A

-

Q

-

L

-

G

G

S

S

G

I

I

L

A

A

Q

E

D

P

R

E

D

E

P

L

N

N

G

Q

A

T

P

E

A

Q

V

T

S

T

H

Y

S

E

A

-

F

-

E

-

P

-

H

-

P

-

I

V

Q

E

G
|
G

W

I

T

G

P

Y

D

D

F

F

I

I

P

P

K

T

V

V

L

L

Q

-

E

-

S

-

I

-

D

D

Q

R

G

T

F

V

Y

V

D

D

A

K

L

W

L

F

P

K

V

S

A

N

G

D

A

E

D

E

G

A

I

F

A

T

W

F

A

A

R

R

R

M

L

L

A

I

A

A

E

Q

E

E

G

G

I

L

L

L

T

C

G

G

I

G

S
|
S

G

A

G

G

S

S

T

T

F

V

A

A

I

V

S

A

H

V

E

K

V

A

A

A

K

Q

T

E

A

L

P

Q

E

E

G

G

S

Q

V

R

I

C

L

V

C

V

M

I

L

L

P
|
P

D
|
D

T

S

G

V

E

R

R

N

Y

Y

L

M

S

T

T

K

P

F

L

L

binding protoporphyrin ix containing fe: A186 (= A159), P189 (≠ A162), L190 (≠ E163), Y193 (≠ E166), R226 (= R200)
binding pyridoxal-5'-phosphate: K79 (= K56), N109 (= N86), G216 (= G190), T217 (= T191), G218 (= G192), T220 (= T194), G265 (= G250), S309 (= S298), P335 (= P324), D336 (= D325)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 11, 12, 13, 14, 18, 23, 24, 25

4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
38% identity, 89% coverage: 15:335/360 of query aligns to 33:342/486 of 4pcuA

query
sites
4pcuA

K

K

T

I

Y

L

D

P

S

D

V

I

L

L

D

K

T

K

V

I

G

G

N

D

T

T

P

P

V

M

I

V

R

R

I

I

N

N

N

K

L

I

A

G

P

K

E

K

-

F

-

G

-

L

G

K

V

C

E

E

L

L

Y

L

V

A

K

K

A

C

E

E

F

F

N

N

P

A

A

G

S

S

V

V

K
|
K

D

D

R

R

L

I

A

S

L

L

N

R

I

M

I

I

E

E

A

D

A

A

E

E

R

R

A

D

G

G

T

T

L

L

K

K

P

P

G

G

Q

D

T

T

V

I

E

E

A

P

T

T

S
|
S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

M

L

V

A

C

A

A

A

Q

V

K

R

G

G

Y

Y

P

R

L

C

V

I

I

I

T

V

M

M

A

P

E

E

S

K

F

M

S

S

I

S

E

E

R

K

R

V

K

D

L

V

M

L

R

R

L

A

L

L

G

G

A

A

K

E

V

I

V

V

L

R

T

T

-

P

-

A

-

R

-

F

-

D

-

S

P

P

R

S

A

S

E

H

K

V

G

G

F

V

G

A

M

-

Y

W

R

R

K

L

A

K

V

N

E

E

L

I

A

P

E

N

A

S

N

H

G

-

W

-

F

-

L

I

A

L

S

D

Q

Q

F

Y

E

R

T

N

A
|
A

A

S

N

N

A
x
P

E
x
L

M

A

H

H

E
x
Y

N

D

T

T

A

A

Q

D

E

E

I

I

L

L

G

Q

D

Q

F

C

E

D

G

G

C

-

K

K

L

L

D

D

Y

M

I

L

V

V

T

A

G

S

Y

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

V

I

T

T

G

G

L

I

G

A

R
|
R

V

K

L

L

R

K

K

E

A

K

R

C

P

P

E

G

T

C

K

R

I

I

L

G

T

V

E
x
D

P

P

A

E

N

-

A

-

Q

-

L

-

G

G

S

S

G

I

I

L

A

A

Q

E

D

P

R

E

D

E

P

L

N

N

G

Q

A

T

P

E

A

Q

V

T

S

T

H

Y

S

E

A

-

F

-

E

-

P

-

H

-

P

-

I

V

Q

E

G
|
G

W

I

T

G

P

Y

D

D

F

F

I

I

P

P

K
x
T

V

V

L

L

Q

-

E

-

S

-

I

-

D

D

Q

R

G

T

F

V

Y

V

D

D

A

K

L

W

L

F

P

K

V

S

A

N

G

D

A

E

D

E

G

A

I

F

A

T

W

F

A

A

R

R

R

M

L

L

A

I

A

A

E

Q

E

E

G

G

I

L

L

L

T

C

G

G

I

G

S
|
S

G

A

G

G

S

S

T

T

F

V

A

A

I

V

S

A

H

V

E

K

V

A

A

A

K

Q

T

E

A

L

P

Q

E

E

G

G

S

Q

V

R

I

C

L

V

C

V

M

I

L

L

P
|
P

D
|
D

T

S

G

V

E

R

R

N

Y

Y

L

M

S

T

T

K

P

F

L

L

active site: K77 (= K56), S105 (= S84), D237 (≠ E215), S305 (= S298)
binding protoporphyrin ix containing fe: A182 (= A159), P185 (≠ A162), L186 (≠ E163), Y189 (≠ E166), R222 (= R200), T269 (≠ K258)
binding pyridoxal-5'-phosphate: K77 (= K56), N107 (= N86), G212 (= G190), T213 (= T191), G214 (= G192), T216 (= T194), G261 (= G250), S305 (= S298), P331 (= P324), D332 (= D325)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479

4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
39% identity, 91% coverage: 15:341/360 of query aligns to 2:313/318 of 4lmaA

query
sites
4lmaA

K

R

T

I

Y

A

D

H

S

D

V

V

L

T

D

E

T

L

V

V

G

G

N

R

T

T

P

P

V

L

I

V

R

Q

I

L

N

N

N

R

L

I

-

P

A

Q

P

A

E

E

G

G

V

C

-

L

-

G

E

R

L

I

Y

V

V

M

K

K

A

L

E

E

F

G

F

M

N

N

P

P

A

A

S

S

V

V

K
|
K

D

D

R

R

L

I

A

G

L

T

N

H

I

M

I

I

E

N

A

S

A

A

E

E

R

K

A

A

G

G

T

L

L

I

K

N

P

P

G

E

Q

T

T

T

V

V

-

L

V

V

E

E

A

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

T

C

A

A

A

Q

A

K

K

G

G

Y

Y

P

R

L

L

V

I

I

L

T

T

M

M

A

P

E

E

S

T

F

M

S

S

I

L

E

E

R

R

K

A

L

M

M

L

R

K

L

A

L

Y

G

G

A

A

K

T

V

L

V

E

L

L

T

T

P

P

R

G

A

S

E

Q

K

G

G

M

F

K

G

G

M

A

Y

I

R

L

K

R

A

A

V

Q

E

Q

L

I

A

V

E

D

A

S

-

I

N

P

G

G

W

A

F

Y

L

M

A

L

S

Q

Q

Q

F

F

E

R

T

N

A

P

A

S

N

N

A

P

E

E

M

I

H

H

E

R

N

L

T

T

A

A

Q

E

E

E

I

I

L

W

G

Q

D

D

F

T

E

E

G

G

C

-

K

Q

L

V

D

D

Y

F

I

I

V

V

T

A

G

G

Y

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

V

I

T

T

G

G

L

V

G

A

R

E

V

V

L

I

R

K

K

S

A

R

R

K

P

P

E

S

T

F

K

Q

I

V

L

A

T

V

E

E

P

P

A

F

N

N

A

-

Q

-

L

-

G

-

S

-

G

-

I

-

A

-

Q

-

D

-

R

-

D

-

P

-

N

-

G

-

A

S

P

P

A

V

V

I

S

S

H

G

S

G

A

N

F

P

E

G

P

P

H

H

P

K

I

I

Q

Q

G
|
G

W

I

T

G

P

A

D

G

F

F

I

I

P

P

K

E

V

V

L

L

Q

R

E

T

S

D

I

L

D

-

Q

-

G

-

F

-

Y

I

D

D

A

E

L

V

L

I

P

T

V

V

A

S

G

D

A

E

D

E

G

A

I

F

A

Q

W

F

A

G

R

R

L

L

A

A

A

K

E

E

G

G

I

L

L

L

T

S

G

G

I

I

S
|
S

G

S

G

G

S

A

T

N

F

L

A

C

I

A

S

A

H

I

E

Q

V

L

A

A

K

Q

T

R

A

P

P

E

-

N

E

E

G

G

S

K

V

L

I

I

L

V

C

V

M

I

L

Q

P
|
P

D

S

T

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

L

L

M

F

F

E

Q

G

N

I

I

V

E

E

E

active site: K46 (= K56), S269 (= S298)
binding pyridoxal-5'-phosphate: K46 (= K56), N77 (= N86), G181 (= G190), T182 (= T191), G183 (= G192), T185 (= T194), G225 (= G250), S269 (= S298), P296 (= P324)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
39% identity, 94% coverage: 7:343/360 of query aligns to 2:323/323 of 4aecA

query
sites
4aecA

I

V

R

K

R

R

T

E

T

T

G

G

N

P

G

D

-

G

-

L

K

N

T

I

Y

A

D

D

S

N

V

V

L

S

D

Q

T

L

V

I

G

G

N

K

T

T

P

P

V

M

I

V

R

Y

I

L

N

N

N

S

L

I

A

A

P

K

E

G

G

C

V

V

-

A

E

N

L

I

Y

A

V

A

K

K

A

L

E

E

F

I

F

M

N

E

P

P

A

C

S

S

V

V

K
|
K

D

D

R

R

L

I

A

G

L

Y

N

S

I

M

I

V

E

T

A

D

A

A

E

E

R

Q

A

K

G

G

T

F

L

I

K

S

P

P

G

G

Q

K

T

S

V

V

-

L

V

V

E

E

A

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

M

F

V

I

C

A

A

A

Q

S

K

R

G

G

Y

Y

P

R

L

L

V

I

I

L

T

T

M

M

A

P

E

A

S

S

F

M

S

S

I

M

E

E

R

R

K

V

L

L

M

L

R

K

L

A

L

F

G

G

A

A

K

E

V

L

V

V

L

L

T

T

P

D

R

P

A

A

E

K

K

G

G

M

F

T

G

G

M

A

Y

V

R

Q

K

K

A

A

V

E

E

E

-

I

L

L

A

K

E

N

A

T

N

P

G

D

W

A

F

Y

L

M

A

L

S

Q

Q

Q

F

F

E

D

T

N

A

P

A

A

N

N

A

P

E

K

M

I

H

H

E

Y

N

E

T

T

A

G

Q

P

E

E

I

I

L

W

G

D

D

D

F

T

E

K

G

G

C

-

K

K

L

V

D

D

Y

I

I

F

V

V

T

A

G

G

Y
x
I

G
|
G

T
|
T

G
|
G

T
|
T

V

I

T

T

G

G

L

V

G

G

R

R

V

F

L

I

R

K

K

E

A

K

R

N

P

P

E

K

T

T

K

Q

I

V

I

I

L

G

T

V

E

E

P

P

A

T

N

E

A

S

Q

D

L

I

L

L

G

S

S

-

G

-

I

-

A

-

Q

-

D

-

R

-

D

-

P

-

N

G

G

G

A

K

P

P

A

G

V

-

S

-

H

-

S

-

A

-

F

-

E

-

P

P

H

H

P

K

I

I

Q

Q

G
|
G

W

I

T

G

P

A

D

G

F

F

I

I

P

P

K

K

V

-

L

-

Q

-

E

-

S

N

I

L

D

D

Q

Q

G

K

F

I

Y

M

D

D

A

E

L

V

L

I

P

A

V

I

A

S

G

S

A

E

D

E

G

A

I

I

A

E

W

T

A

A

R

K

R

Q

L

L

A

A

A

L

E

K

E

E

G

G

I

L

L

M

T

V

G

G

I

I

S
|
S

G

S

G

G

S

A

T

A

F

A

A

A

I

A

S

A

H

I

E

K

V

V

A

A

K

K

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

V

L

I

I

L

A

C

V

M

V

L

F

P
|
P

D

S

T

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

P

L

L

F

F

E

Q

G

S

I

I

V

R

E

E

D

E

M

V

active site: K54 (= K56), S277 (= S298)
binding pyridoxal-5'-phosphate: K54 (= K56), N85 (= N86), I188 (≠ Y189), G189 (= G190), T190 (= T191), G191 (= G192), G192 (= G193), T193 (= T194), G233 (= G250), S277 (= S298), P304 (= P324)

P47999 Cysteine synthase, chloroplastic/chromoplastic; At.OAS.7-4; Beta-substituted Ala synthase 2;1; ARAth-Bsas2;1; CSase B; AtCS-B; CS-B; O-acetylserine (thiol)-lyase; O-acetylserine sulfhydrylase; OAS-TL B; cpACS1; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
40% identity, 91% coverage: 18:345/360 of query aligns to 77:387/392 of P47999

query
sites
P47999

D

D

S

N

V

A

L

A

D

Q

T

L

V

I

G

G

N

K

T

T

P

P

V

M

I

V

R

Y

I

L

N

N

L

V

A

V

P

K

E

G

G

C

V

V

-

A

E

S

L

V

Y

A

V

A

K

K

A

L

E

E

F

I

F

M

N

E

P

P

A

C

S

S

V

V

K

K

D

D

R

R

L

I

A

G

L

Y

N

S

I

M

I

I

E

T

A

D

A

A

E

E

R

E

A

K

G

G

T

L

L

I

K

T

P

P

G

G

Q

K

T

S

V

V

-

L

V

V

E

E

A

S

T

T

S

S

G

G

N

N

T

T

G

G

I

I

G

G

L

L

A

A

M

F

V

I

C

A

A

A

Q

S

K

K

G

G

Y

Y

P

K

L

L

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I

I

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T

M

M

A

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E

A

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M

S

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E

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V

L

L

M

L

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R

L

A

L

F

G

G

A

A

K

E

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L

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V

L

L

T

T

P

E

R

P

A

A

E

K

K

G

G

M

F

T

G

G

M

A

Y

I

R

Q

K

K

A

A

V

E

E

E

-

I

L

L

A

K

E

K

A

T

N

P

G

N

W

S

F

Y

L

M

A

L

S

Q

Q

Q

F

F

E

D

T

N

A

P

A

A

N

N

A

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K

M

I

H

H

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Y

N

E

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T

A

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Q

P

E

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I

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G

E

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D

F

T

E

R

G

G

C

-

K

K

L

I

D

D

Y

I

I

L

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V

T

A

G

G

Y

I

G

G

T

T

G

G

T

T

V

I

T

T

G

G

L

V

G

G

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R

V

F

L

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K

E

A

R

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K

P

P

E

E

T

L

K

K

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V

I

I

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T

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E

E

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P

A

T

N

E

A

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Q

A

L

I

L

L

G

S

S

G

G

G

I

-

A

-

Q

-

D

-

R

-

D

K

P

P

N

G

G

-

A

-

P

-

A

-

V

-

S

-

H

-

S

-

A

-

F

-

E

-

P

P

H

H

P

K

I

I

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Q

G

G

W

I

T

G

P

A

D

G

F

F

I

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P

P

K

K

V

-

L

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-

E

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S

N

I

L

D

D

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L

G

A

F

I

Y

V

D

D

A

E

L

Y

L

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P

A

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I

A

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G

S

A

E

D

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G

A

I

I

A

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T

A

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R

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L

L

A

A

A

L

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Q

E

E

G

G

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V

G

G

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I

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S

G

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G

G

S

A

T

A

F

A

A

A

I

A

S

A

H

I

E

Q

V

V

A

A

K

K

T

R

A

-

P

P

E

E

-

N

-

A

G

G

S

K

V

L

I

I

L

A

C

V

M

V

L

F

P

P

D

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T

F

G

G

E

E

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R

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Y

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T

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N

E

E

Q

Sites not aligning to the query:

61 modified: N-acetylalanine

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
39% identity, 87% coverage: 24:336/360 of query aligns to 7:301/302 of 2efyA

query
sites
2efyA

V

I

G

G

N

K

T

T

P

P

V

V

I

V

R

R

I

L

N

A

N

K

L

V

A

V

-

E

P

P

E

D

G

M

V

A

E

E

L

V

Y

W

V

V

K

K

A

L

E

E

F

G

F

L

N

N

P

P

A

G

S

S

V

I

K
|
K

D

D

R

R

L

P

A

A

L

W

N

Y

I

M

I

I

E

K

A

D

A

A

E

E

R

E

A

R

G

G

T

I

L

L

K

R

P

P

G

G

-

S

-

G

Q

Q

T

V

V

I

V

V

E

E

A

P

T
|
T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

M

V

I

C

A

A

A

Q

S

K

R

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G

Y

Y

P

R

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L

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I

I

L

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T

M

M

A

P

E

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Q

F

M

S

S

I

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E

E

R

R

R

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K

R

L

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M

L

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K

L

A

L

F

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G

A

A

K

E

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V

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L

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T

P

D

R

P

A

E

E

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K

R

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M

F

L

G

A

M

A

Y

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K

E

A

A

V

L

E

R

L

L

A

K

E

E

A

E

N

L

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G

W

A

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F

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A

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D

Q
|
Q

F

F

E

K

T

N

A

P

A

A

N

N

A

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M

A

H

H

E

Y

N

E

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A

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Q

P

E

E

I

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G

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D

A

F

L

E

E

G

G

C

-

K

R

L

I

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D

Y

A

I

F

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V

T
x
Y

G

G

Y

S

G
|
G

T
|
T

G
|
G

G

G

T
|
T

V

I

T

T

G

G

L

V

G

G

R

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V

Y

L

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R

K

K

E

A

R

R

I

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P

E

H

T

V

K

K

I

V

I

I

L

A

T

V

E
|
E

P

P

A

A

N

R

A
x
S

Q

N

L

V

L

L

G

S

S

G

G

G

I

-

A

-

Q

-

D

-

R

-

D

-

P

-

N

-

G

-

A

-

P

-

A

-

V

-

S

-

H

-

S

-

A

K

F

M

E

G

P

Q

H

H

P

G

I

F

Q

Q

G
|
G

W
x
M

T

G

P
|
P

D

G

F

F

I

I

P

P

K

-

V

-

L

-

Q

-

E

E

S

N

I

L

D

D

Q

L

G

S

F

L

Y

L

D

D

A

G

L

V

L

I

P

Q

V

V

A

W

G

E

A

E

D

D

G

A

I

F

A

P

W

L

A

A

R

R

L

L

A

A

A

R

E

E

G

G

I

L

L

F

T

L

G

G

I

M

S
|
S

G

S

G

G

S

G

T

I

F

V

A

W

I

A

S

A

H

L

E

Q

V

V

A

A

K

R

T

E

A

L

P

G

E

P

G

G

S

K

V

R

I

V

L

A

C

C

M

I

L

S

P
|
P

D
|
D

T

G

G

G

E

W

R

K

Y

Y

L

L

S

S

T

T

P

P

L

L

F

Y

active site: K40 (= K56), S70 (= S84), E200 (= E215), S204 (≠ A219), S263 (= S298)
binding 5-oxohexanoic acid: T69 (= T83), G71 (= G85), T73 (= T87), Q141 (= Q155), G175 (= G190), G219 (= G250), M220 (≠ W251), P222 (= P253)
binding pyridoxal-5'-phosphate: K40 (= K56), N72 (= N86), Y172 (≠ T187), G175 (= G190), T176 (= T191), G177 (= G192), T179 (= T194), G219 (= G250), S263 (= S298), P289 (= P324), D290 (= D325)

2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
39% identity, 87% coverage: 24:336/360 of query aligns to 7:301/302 of 2ecqA

query
sites
2ecqA

V

I

G

G

N

K

T

T

P

P

V

V

I

V

R

R

I

L

N

A

N

K

L

V

A

V

-

E

P

P

E

D

G

M

V

A

E

E

L

V

Y

W

V

V

K

K

A

L

E

E

F

G

F

L

N

N

P

P

A

G

S

S

V

I

K
|
K

D

D

R

R

L

P

A

A

L

W

N

Y

I

M

I

I

E

K

A

D

A

A

E

E

R

E

A

R

G

G

T

I

L

L

K

R

P

P

G

G

-

S

-

G

Q

Q

T

V

V

I

V

V

E

E

A

P

T

T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

M

V

I

C

A

A

A

Q

S

K

R

G

G

Y

Y

P

R

L

L

V

I

I

L

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T

M

M

A

P

E

A

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Q

F

M

S

S

I

E

E

E

R

R

R

K

K

R

L

V

M

L

R

K

L

A

L

F

G

G

A

A

K

E

V

L

V

V

L

L

T

T

P

D

R

P

A

E

E

R

K

R

G

M

F

L

G

A

M

A

Y

R

R

E

K

E

A

A

V

L

E

R

L

L

A

K

E

E

A

E

N

L

G

G

W

A

F

F

L

M

A

P

S

D

Q
|
Q

F

F

E

K

T

N

A

P

A

A

N

N

A

V

E

R

M

A

H

H

E

Y

N

E

T

T

A

G

Q

P

E

E

I

L

L

Y

G

E

D

A

F

L

E

E

G

G

C

-

K

R

L

I

D

D

Y

A

I

F

V

V

T
x
Y

G
|
G

Y

S

G
|
G

T
|
T

G

G

T
|
T

V

I

T

T

G

G

L

V

G

G

R

R

V

Y

L

L

R

K

K

E

A

R

R

I

P

P

E

H

T

V

K

K

I

V

I

I

L

A

T

V

E
|
E

P

P

A

A

N

R

A
x
S

Q

N

L

V

L

L

G

S

S

G

G

G

I

-

A

-

Q

-

D

-

R

-

D

-

P

-

N

-

G

-

A

-

P

-

A

-

V

-

S

-

H

-

S

-

A

K

F

M

E

G

P

Q

H

H

P

G

I

F

Q

Q

G
|
G

W

M

T

G

P

P

D

G

F

F

I

I

P

P

K

-

V

-

L

-

Q

-

E

E

S

N

I

L

D

D

Q

L

G

S

F

L

Y

L

D

D

A

G

L

V

L

I

P

Q

V

V

A

W

G

E

A

E

D

D

G

A

I

F

A

P

W

L

A

A

R

R

L

L

A

A

A

R

E

E

G

G

I

L

L

F

T

L

G

G

I

M

S
|
S

G

S

G

G

S

G

T

I

F

V

A

W

I

A

S

A

H

L

E

Q

V

V

A

A

K

R

T

E

A

L

P

G

E

P

G

G

S

K

V

R

I

V

L

A

C

C

M

I

L

S

P
|
P

D

D

T

G

G

G

E

W

R

K

Y

Y

L

L

S

S

T

T

P

P

L

L

F

Y

active site: K40 (= K56), S70 (= S84), E200 (= E215), S204 (≠ A219), S263 (= S298)
binding (3s)-3-hydroxybutanoic acid: K40 (= K56), G71 (= G85), T73 (= T87), Q141 (= Q155), G219 (= G250)
binding pyridoxal-5'-phosphate: K40 (= K56), N72 (= N86), Y172 (≠ T187), G173 (= G188), G175 (= G190), T176 (= T191), T179 (= T194), G219 (= G250), S263 (= S298), P289 (= P324)

2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
39% identity, 87% coverage: 24:336/360 of query aligns to 7:301/302 of 2ecoA

query
sites
2ecoA

V

I

G

G

N

K

T

T

P

P

V

V

I

V

R

R

I

L

N

A

N

K

L

V

A

V

-

E

P

P

E

D

G

M

V

A

E

E

L

V

Y

W

V

V

K

K

A

L

E

E

F

G

F

L

N

N

P

P

A

G

S

S

V

I

K
|
K

D

D

R

R

L

P

A

A

L

W

N

Y

I

M

I

I

E

K

A

D

A

A

E

E

R

E

A

R

G

G

T

I

L

L

K

R

P

P

G

G

-

S

-

G

Q

Q

T

V

V

I

V

V

E

E

A

P

T
|
T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

M

V

I

C

A

A

A

Q

S

K

R

G

G

Y

Y

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R

L

L

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I

I

L

T

T

M

M

A

P

E

A

S

Q

F

M

S

S

I

E

E

E

R

R

R

K

K

R

L

V

M

L

R

K

L

A

L

F

G

G

A

A

K

E

V

L

V

V

L

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E

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x
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-

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active site: K40 (= K56), S70 (= S84), E200 (= E215), S204 (≠ A219), S263 (= S298)
binding 4-methyl valeric acid: K40 (= K56), T69 (= T83), G71 (= G85), T73 (= T87), Q141 (= Q155), G175 (= G190), T176 (= T191), G219 (= G250)
binding pyridoxal-5'-phosphate: K40 (= K56), N72 (= N86), Y172 (≠ T187), G175 (= G190), T176 (= T191), T179 (= T194), G219 (= G250), S263 (= S298), P289 (= P324), D290 (= D325)

5xemA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-lanthionine-plp schiff base
39% identity, 88% coverage: 18:333/360 of query aligns to 4:302/302 of 5xemA

query
sites
5xemA

D

N

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S

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I

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G

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K

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N

binding (2R)-2-azanyl-3-[(2R)-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-propanoic acid: K42 (= K56), T69 (= T83), S70 (= S84), N72 (= N86), T73 (= T87), M120 (≠ G134), Q142 (= Q155), G176 (= G190), T177 (= T191), G220 (= G250), M221 (≠ W251), G222 (≠ T252), S224 (≠ D254)
binding calcium ion: L300 (= L331), S301 (= S332), N302 (≠ T333)
binding pyridoxal-5'-phosphate: K42 (= K56), N72 (= N86), T175 (≠ Y189), G176 (= G190), T177 (= T191), G178 (= G192), S180 (≠ T194), G220 (= G250), S266 (= S298), T293 (≠ P324), D294 (= D325)

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
40% identity, 88% coverage: 20:337/360 of query aligns to 7:309/310 of 4lmbA

query
sites
4lmbA

V

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K

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T

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A

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N

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I

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G

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S

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A

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K

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A

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P

E

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N

E

E

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K

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I

I

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M

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P

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K

active site: K46 (= K56), S269 (= S298)
binding cysteine: K46 (= K56), T74 (= T83), S75 (= S84), N77 (= N86), T78 (= T87), M101 (≠ F110), M125 (≠ G134), M125 (≠ G134), Q147 (= Q155), F148 (= F156), Q224 (= Q249), G225 (= G250), G225 (= G250), I226 (≠ W251), A228 (≠ P253)
binding pyridoxal-5'-phosphate: K46 (= K56), N77 (= N86), V180 (≠ Y189), G181 (= G190), T182 (= T191), G183 (= G192), T185 (= T194), G225 (= G250), S269 (= S298), P296 (= P324)

Query Sequence

>3607478 FitnessBrowser__Dino:3607478
MTATPPIRRTTGNGKTYDSVLDTVGNTPVIRINNLAPEGVELYVKAEFFNPAASVKDRLA
LNIIEAAERAGTLKPGQTVVEATSGNTGIGLAMVCAQKGYPLVITMAESFSIERRKLMRL
LGAKVVLTPRAEKGFGMYRKAVELAEANGWFLASQFETAANAEMHENTTAQEILGDFEGC
KLDYIVTGYGTGGTVTGLGRVLRKARPETKIILTEPANAQLLGSGIAQDRDPNGAPAVSH
SAFEPHPIQGWTPDFIPKVLQESIDQGFYDALLPVAGADGIAWARRLAAEEGILTGISGG
STFAISHEVAKTAPEGSVILCMLPDTGERYLSTPLFEGIVEDMNEDERAISASTPGYQMP

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SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory