SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_020174433.1 NCBI__GCF_000385335.1:WP_020174433.1 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)

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)
62% identity, 93% coverage: 22:327/330 of query aligns to 3:305/310 of P9WP55

query
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P9WP55

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K44 (= K65) modified: N6-(pyridoxal phosphate)lysine
N74 (= N96) binding pyridoxal 5'-phosphate
GTGGT 178:182 (= GTGGT 200:204) binding pyridoxal 5'-phosphate
S266 (= S288) binding pyridoxal 5'-phosphate

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)
62% identity, 93% coverage: 22:327/330 of query aligns to 3:305/306 of 2q3dA

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active site: K44 (= K65), S266 (= S288), P293 (= P315)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K65), T71 (= T93), S72 (= S94), N74 (= N96), T75 (= T97), Q144 (= Q166), V177 (= V199), G178 (= G200), T179 (= T201), G180 (= G202), T182 (= T204), G222 (= G244), I223 (= I245), S266 (= S288), P293 (= P315), D294 (≠ S316)

4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
59% identity, 94% coverage: 21:330/330 of query aligns to 2:311/318 of 4lmaA

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active site: K46 (= K65), S269 (= S288)
binding pyridoxal-5'-phosphate: K46 (= K65), N77 (= N96), G181 (= G200), T182 (= T201), G183 (= G202), T185 (= T204), G225 (= G244), S269 (= S288), P296 (= P315)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
61% identity, 91% coverage: 22:322/330 of query aligns to 3:300/300 of 3zeiA

query
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active site: K44 (= K65), S266 (= S288), P293 (= P315)
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 (= T93), S72 (= S94), I126 (≠ V148), Q144 (= Q166), F145 (= F167), K215 (≠ P237), G222 (= G244), A225 (= A247), F227 (= F249)
binding pyridoxal-5'-phosphate: K44 (= K65), N74 (= N96), V177 (= V199), G178 (= G200), T179 (= T201), G180 (= G202), T182 (= T204), G222 (= G244), S266 (= S288), P293 (= P315), D294 (≠ S316)

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)
61% identity, 91% coverage: 22:322/330 of query aligns to 3:300/300 of 2q3cA

query
sites
2q3cA

I

I

Y

A

D

E

S

D

I

I

T

T

D

Q

T

L

I

I

G

G

N

R

T

T

P

P

I

L

V

V

R

R

L

L

N

R

K

R

I

V

A

T

A

-

E

-

K

D

G

G

V

A

K

V

A

A

N

D

L

I

L

V

A

A

K

K

L

L

E

E

F

F

N

N

P

P

I

A

A

N

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

V

H

A

M

M

I

L

T

Q

V

A

L

A

E

E

E

Q

T

A

G

G

K

L

I

I

K

K

P

P

G

D

V

-

T

T

T

I

L

I

I

L

E

E

P

P

T
|
T

S
|
S

G
|
G

N

N

T
|
T

G

G

I

I

A

A

L

L

A

A

F

M

V

V

A

C

A

A

R

R

G

G

Y

Y

K

R

L

C

I

V

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

L

E

E

R

R

K

M

M

L

L

L

A

R

L

A

L

Y

G

G

A

A

E

E

L

L

V

I

L

L

T

T

P

P

A

G

P

A

Q

D

G

G

M
|
M

K

S

G

G

A

A

V

I

A

A

K

K

A

A

E

E

L

L

S

A

A

K

A

T

T

D

P

Q

D

R

S

Y

V

F

V

V

P

P

R

Q

Q
|
Q

F

F

D

E

N

N

P

P

A

A

N

N

P

P

E

A

I

I

H

H

R

R

L

V

T

T

A

A

E

E

I

V

W

W

N

R

D

D

T

T

N

D

G

G

E

K

I

V

D

D

A

I

F

V

V

V

A

A

G

G

V

V

G

G

T

T

G

G

T

T

I

I

T

T

G

G

V

V

A

A

Q

Q

V

V

L

I

K

K

P

E

R

R

K

K

P

P

G

S

I

A

K

R

I

F

V

V

A

A

I

V

E

E

P

P

E

A

D

A

S

S

P

P

I

V

L

L

S

S

G

G

Q

Q

P
x
K

G

G

P

P

H

H

K

P

I

I

Q

Q

G
|
G

I

I

G

G

A
|
A

G

G

F

F

I

V

P

P

S

P

I

V

L

L

D

D

R

Q

S

D

L

L

I

V

D

D

E

E

V

I

T

T

V

V

G

G

N

N

Q

E

T

D

A

A

F

L

D

N

T

V

A

A

R

R

L

R

L

L

A

A

R

R

L

E

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

T

A

V

A

A

C

L

E

Q

I

V

G

A

S

R

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

I

V

V

L

V

I

V

I

L

P
|
P

S

D

F

F

A

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K65), S266 (= S288), P293 (= P315)
binding : T71 (= T93), S72 (= S94), G73 (= G95), T75 (= T97), M122 (= M144), Q144 (= Q166), K215 (≠ P237), G222 (= G244), A225 (= A247)

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
61% identity, 93% coverage: 22:328/330 of query aligns to 3:309/310 of 4lmbA

query
sites
4lmbA

I

I

Y

A

D

R

S

D

I

I

T

T

D

Q

T

L

I

V

G

G

N

R

T

T

P

P

I

L

V

V

R

Q

L

L

N

N

K

R

I

I

A

P

A

V

E

A

K

E

G

G

V

V

K

K

A

A

N

R

L

I

L

V

A

V

K

K

L

L

E

E

F

S

F

M

N

N

P

P

I

A

A

A

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

V

H

S

M

M

I

V

T

E

V

D

L

A

E

E

E

A

T

A

G

G

K

L

I

I

K

H

P

P

G

D

V

K

T

T

T

I

L

L

I

V

E

E

P

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

I

A

A

L

L

A

A

F

M

V

V

A

A

R

K

G

G

Y

Y

K

R

L

L

I

V

L

L

V

T

M

M

P

P

E

E

S

T

M
|
M

S

S

I

L

E

E

R

R

K

A

M

M

L

L

A

K

L

A

L

Y

G

G

A

A

E

Q

L

L

V

E

L

L

T

T

P

P

A

G

P

S

Q

Q

G

G

M
|
M

K

E

G

G

A

A

V

I

A

T

K

R

A

A

E

E

L

I

S

V

A

E

A

N

T

T

P

P

D

N

S

A

V

Y

V

S

P

L

R

Q

Q
|
Q

F
|
F

D

R

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

R

L

E

T

T

A

A

E

E

I

I

W

W

N

A

D

D

T

T

N

D

G

G

E

L

I

V

D

D

A

I

F

V

V

I

A

G

G

G

V
|
V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

T

T

G

G

V

I

A

A

Q

E

V

T

L

I

K

K

P

P

R

R

K

R

P

P

G

Q

I

F

K

Q

I

A

V

I

A

A

I

V

E

E

P

P

E

S

D

N

S

S

P

P

I

V

L

L

S

S

G

G

Q

Q

P

P

G

G

P

P

H

H

K

K

I

I

Q
|
Q

G
|
G

I
|
I

G

G

A
|
A

G

G

F

F

I

I

P

P

S

A

I

I

L

F

D

R

R

P

S

E

L

L

I

I

D

D

E

E

V

V

V

I

T

I

V

V

G

D

N

D

Q

T

T

E

A

A

F

F

D

A

T

Y

A

A

R

R

L

R

L

L

A

A

R

R

L

Q

E

E

G

G

I

L

P

L

A

S

G

G

I

I

S
|
S

S

A

G

G

A

A

V

L

A

W

A

A

C

I

E

Q

I

V

G

G

S

K

R

R

P

P

E

E

F

N

A

E

G

D

K

K

N

L

I

I

V

V

L

M

I

I

I

Q

P
|
P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

K

active site: K46 (= K65), S269 (= S288)
binding cysteine: K46 (= K65), T74 (= T93), S75 (= S94), N77 (= N96), T78 (= T97), M101 (= M120), M125 (= M144), M125 (= M144), Q147 (= Q166), F148 (= F167), Q224 (= Q243), G225 (= G244), G225 (= G244), I226 (= I245), A228 (= A247)
binding pyridoxal-5'-phosphate: K46 (= K65), N77 (= N96), V180 (= V199), G181 (= G200), T182 (= T201), G183 (= G202), T185 (= T204), G225 (= G244), S269 (= S288), P296 (= P315)

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
60% identity, 94% coverage: 22:330/330 of query aligns to 4:309/310 of 5xoqA

query
sites
5xoqA

I

I

Y

F

D

K

S

D

I

N

T

S

D

E

T

S

I

I

G

G

N

R

T

T

P

P

I

L

V

V

R

Q

L

I

N

N

K

R

I

L

A

T

A

A

E

-

K

-

G

G

V

L

K

S

A

S

N

R

L

V

L

L

A

A

K

K

L

I

E

E

F

G

F

R

N

N

P

P

I

A

A

Y

S

S

V

V

K

K

D

C

R

R

I

I

G

G

V

A

H

A

M

M

I

I

T

W

V

D

L

A

E

E

E

Q

T

S

G

G

K

K

I

L

K

K

P

P

G

G

V

M

T

H

T

-

L

V

I

V

E

E

P

P

T
|
T

S
|
S

G
|
G

N

N

T
|
T

G

G

I

I

A

A

L

L

A

A

F

F

V

V

A

C

A

A

R

R

G

G

Y

Y

K

K

L

L

I

T

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

I

E

E

R

R

K

M

M

M

L

L

A

K

L

S

L

F

G

G

A

A

E

D

L

L

V

V

L

L

T

T

P

P

A

G

P

A

Q

D

G

G

M
|
M

K

K

G

G

A

A

V

I

A

S

K

K

A

A

E

E

L

L

S

-

A

A

T

Q

P

P

D

G

S

W

V

F

V

I

P

P

R

Q

Q
|
Q

F

F

D

K

N

N

P

P

A

A

N

N

P

P

E

A

I

I

H

H

R

V

L

K

T

T

A

G

E

P

E

E

I

I

W

W

N

N

D

D

T

T

N

E

G

G

E

Q

I

V

D

D

A

V

F

F

V

V

A

A

G

G

V

V

G

G

T

T

G

G

T

T

I

I

T

T

G

G

V

V

A

A

Q

R

V

F

L

L

K

K

-

H

P

E

R

K

K

K

P

H

G

P

I

V

K

H

I

V

V

V

A

A

I

V

E

E

P

P

E

A

D

A

S

S

P

P

I

V

L

L

S

A

G

G

Q

P

P

A

G

G

P
x
R

H
|
H

K

K

I

I

Q
|
Q

G
|
G

I

I

G

G

A
|
A

G

G

F

F

I

V

P

P

S

D

I

T

L

F

D

D

R

R

S

S

L

V

I

V

D

D

E

E

V

I

V

L

T

S

V

V

G

T

N

D

Q

D

T

E

A

A

F

I

D

E

T

T

A

A

R

R

L

K

L

L

A

A

R

M

L

E

E

E

G

G

I

I

P

S

A

C

G

G

I

I

S

S

S

C

G

G

A

A

V

M

A

A

A

G

A

A

C

L

E

K

I

V

G

A

S

A

R

R

P

P

E

E

F

F

A

A

G

G

K

K

N

T

I

I

V

V

L

T

I

V

I

L

P

P

S

D

F

A

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

E

G

N

L

L

binding : T72 (= T93), S73 (= S94), G74 (= G95), T76 (= T97), M123 (= M144), Q144 (= Q166), R218 (≠ P239), H219 (= H240), Q222 (= Q243), G223 (= G244), A226 (= A247)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
58% identity, 94% coverage: 22:330/330 of query aligns to 13:319/323 of 4aecA

query
sites
4aecA

I

I

Y

A

D

D

S

N

I

V

T

S

D

Q

T

L

I

I

G

G

N

K

T

T

P

P

I

M

V

V

R

Y

L

L

N

N

K

S

I

I

A

A

A

-

E

-

K

K

G

G

V

C

K

V

A

A

N

N

L

I

L

A

A

A

K

K

L

L

E

E

F

I

F

M

N

E

P

P

I

C

A

C

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

Y

H

S

M

M

I

V

T

T

V

D

L

A

E

E

E

Q

T

K

G

G

K

F

I

I

K

S

P

P

G

G

V

K

T

S

T

V

L

L

I

V

E

E

P

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

G

L

L

A

A

F

F

V

I

A

A

A

S

R

R

G

G

Y

Y

K

R

L

L

I

I

L

L

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

M

E

E

R

R

K

V

M

L

L

L

A

K

L

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

T

T

P

D

A

P

P

A

Q

K

G

G

M

M

K

T

G

G

A

A

V

V

A

Q

K

K

A

A

E

E

L

I

S

L

A

K

A

N

T

T

P

P

D

D

S

A

V

Y

V

M

P

L

R

Q

Q

Q

F

F

D

D

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

Y

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

D

D

D

T

T

N

K

G

G

E

K

I

V

D

D

A

I

F

F

V

V

A

A

G

G

V
x
I

G
|
G

T
|
T

G
|
G

T
|
T

I

I

T

T

G

G

V

V

A

G

Q

R

V

F

L

I

K

K

P

E

R

K

K

N

P

P

G

K

I

T

K

Q

I

V

V

I

A

G

I

V

E

E

P

P

E

T

D

E

S

S

P

D

I

I

L

L

S

S

G

G

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

K

I

N

L

L

D

D

R

Q

S

K

L

I

I

M

D

D

E

E

V

V

V

I

T

A

V

I

G

S

N

S

Q

E

T

E

A

A

F

I

D

E

T

T

A

A

R

K

L

Q

L

L

A

A

R

L

L

K

E

E

G

G

I

L

P

M

A

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

C

I

E

K

I

V

G

A

S

K

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

I

V

A

L

V

I

V

I

F

P
|
P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

P

L

L

F

F

E

Q

G

S

L

I

active site: K54 (= K65), S277 (= S288)
binding pyridoxal-5'-phosphate: K54 (= K65), N85 (= N96), I188 (≠ V199), G189 (= G200), T190 (= T201), G191 (= G202), G192 (= G203), T193 (= T204), G233 (= G244), S277 (= S288), P304 (= P315)

7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
59% identity, 94% coverage: 22:330/330 of query aligns to 3:309/309 of 7n2tA

query
sites
7n2tA

I

I

Y

A

D

K

S

D

I

V

T

T

D

E

T

L

I

I

G

G

N

N

T

T

P

P

I

L

V

V

R

Y

L

L

N

N

K

R

I

V

A

V

A

-

E

-

K

D

G

G

V

C

K

V

A

A

N

R

L

V

L

A

A

A

K

K

L

L

E

E

F

M

N

E

P

P

I

C

A

S

S

S

V

V

K

K

D

D

R

R

I

I

G

G

V

Y

H

S

M

M

I

I

T

S

V

D

L

A

E

E

E

N

T

K

G

G

K

L

I

I

K

T

P

P

G

G

V

E

T

S

T

V

L

L

I

I

E

E

P

P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

G

L

L

A

A

F

F

V

I

A

A

R

K

G

G

Y

Y

K

R

L

L

I

I

L

I

V

C

M

M

P

P

E

A

S

S

M

M

S

S

I

L

E

E

R

R

K

T

M

I

L

L

A

R

L

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

T

T

P

D

A

P

P

A

Q

R

G

G

M

M

K

K

G

G

A

A

V

V

A

Q

K

K

A

A

E

E

L

I

S

K

A

A

A

K

T

T

P

P

D

N

S

S

V

Y

V

I

P

L

R

Q

Q

Q

F

F

D

E

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

Y

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

R

D

G

T

S

N

G

G

G

E

K

I

I

D

D

A

A

F

L

V

V

A

S

G

G

V

I

G

G

T

T

G

G

T

T

I

V

T

T

G

G

V

A

A

G

Q

K

V

Y

L

L

K

K

P

E

R

Q

K

N

P

P

G

N

I

I

K

K

I

L

V

Y

A

G

I

V

E

E

P

P

E

V

D

E

S

S

P

A

I

I

L

L

S

S

G

G

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

G

I

V

L

L

D

D

R

V

S

N

L

L

I

L

D

D

E

E

V

V

V

I

T

Q

V

V

G

S

N

S

Q

E

T

E

A

S

F

I

D

E

T

T

A

A

R

K

L

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S

S

G

G

A

A

V

A

A

A

C

I

E
x
R

I

I

G

A

S

K

R
|
R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

I

V

V

L

A

I

V

I

F

P

P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

V

L

L

F

F

E

E

G

S

L

V

binding phosphate ion: R277 (≠ E298), R281 (= R302)

P47998 Cysteine synthase 1; At.OAS.5-8; Beta-substituted Ala synthase 1;1; ARAth-Bsas1;1; CSase A; AtCS-A; Cys-3A; O-acetylserine (thiol)-lyase 1; OAS-TL A; O-acetylserine sulfhydrylase; Protein ONSET OF LEAF DEATH 3; EC 2.5.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
59% identity, 93% coverage: 21:328/330 of query aligns to 4:309/322 of P47998

query
sites
P47998

R

R

I

I

Y

A

D

K

S

D

I

V

T

T

D

E

T

L

I

I

G

G

N

N

T

T

P

P

I

L

V

V

R

Y

L

L

N

N

K

N

I

V

A

A

A

-

E

-

K

E

G

G

V

C

K

V

A

G

N

R

L

V

L

A

A

A

K

K

L

L

E

E

F

M

N

E

P

P

I

C

A

S

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

F

H

S

M

M

I

I

T

S

V

D

L

A

E

E

E

K

T

K

G

G

K

L

I

I

K

K

P

P

G

G

V

E

T

S

T

V

L

L

I

I

E

E

P

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

V

A

G

L

L

A

A

F

F

V

T

A

A

R

K

G

G

Y

Y

K

K

L

L

I

I

L

I

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

T

E

E

R

R

K

I

M

I

L

L

A

L

L

A

L

F

G

G

A

V

E

E

L

L

V

V

L

L

T

T

P

D

A

P

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

A

K

K

A

A

E

E

L

I

S

L

A

A

A

K

T

T

P

P

D

N

S

G

V

Y

V

M

P

L

R

Q

Q
|
Q

F

F

D

E

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H
|
H

R

Y

L

E

T

T

A
x
G

E

P

E

E

I

I

W

W

N

K

D

G

T

T

N

G

G

G

E

K

I

I

D

D

A

G

F

F

V

V

A

S

G

G

V

I

G
|
G

T
|
T

G
|
G

T
|
T

I

I

T

T

G

G

V

A

A

G

Q

K

V

Y

L

L

K

K

P

E

R

Q

K

N

P

A

G

N

I

V

K

K

I

L

V

Y

A

G

I

V

E

E

P

P

E

V

D

E

S

S

P

A

I

I

L

L

S

S

G

G

Q
x
K

P

P

G

G

P

P

H
|
H

K
|
K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

S

I

V

L

L

D

N

R

V

S

D

L

L

I

I

D

D

E

E

V

V

T

Q

V

V

G

S

N

S

Q

D

T

E

A

S

F

I

D

D

T

M

A

A

R

R

L

Q

L

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

C

I

E

K

I

L

G

A

S

Q

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

F

V

V

L

A

I

I

I

F

P

P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

V

L

L

F

F

E

D

K46 (= K65) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
T74 (= T93) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
S75 (= S94) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
N77 (= N96) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
T78 (= T97) mutation T->A,S: Reduction of cysteine synthase activity.
Q147 (= Q166) mutation Q->A,E: Strong reduction of cysteine synthase activity.
H157 (= H176) mutation H->Q,N: Slight reduction of cysteine synthase activity.
G162 (≠ A181) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (= GTGGT 200:204) binding pyridoxal 5'-phosphate
T182 (= T201) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T204) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ Q236) mutation to A: Impaired interaction with SAT1.
H221 (= H240) mutation to A: Impaired interaction with SAT1.
K222 (= K241) mutation to A: Impaired interaction with SAT1.
S269 (= S288) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.

2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
59% identity, 93% coverage: 21:328/330 of query aligns to 2:307/320 of 2isqA

query
sites
2isqA

R

R

I

I

Y

A

D

K

S

D

I

V

T

T

D

E

T

L

I

I

G

G

N

N

T

T

P

P

I

L

V

V

R

Y

L

L

N

N

K

N

I

V

A

A

A

-

E

-

K

E

G

G

V

C

K

V

A

G

N

R

L

V

L

A

A

A

K

K

L

L

E

E

F

M

N

E

P

P

I

C

A

S

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

F

H

S

M

M

I

I

T

S

V

D

L

A

E

E

E

K

T

K

G

G

K

L

I

I

K

K

P

P

G

G

V

E

T

S

T

V

L

L

I

I

E

E

P

P

T
|
T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

V

A

G

L

L

A

A

F

F

V

T

A

A

R

K

G

G

Y

Y

K

K

L

L

I

I

L

I

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

T

E

E

R

R

K

I

M

I

L

L

A

L

L

A

L

F

G

G

A

V

E

E

L

L

V

V

L

L

T

T

P

D

A

P

P

A

Q

K

G
|
G

M
|
M

K
|
K

G

G

A

A

V

I

A

A

K

K

A

A

E

E

L

I

S

L

A

A

A

K

T

T

P

P

D

N

S

G

V

Y

V

M

P

L

R

Q

Q

Q

F

F

D

E

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

Y

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

K

D

G

T

T

N

G

G

G

E

K

I

I

D

D

A

G

F

F

V

V

A

S

G
|
G

V

I

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

T

T

G

G

V

A

A

G

Q

K

V

Y

L

L

K

K

P

E

R

Q

K

N

P

A

G

N

I

V

K

K

I

L

V

Y

A

G

I

V

E

E

P

P

E

V

D

E

S

S

P

A

I

I

L

L

S

S

G

G

Q

K

P

P

G
|
G

P
|
P

H
|
H

K

K

I

I

Q
|
Q

G
|
G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

S

I

V

L

L

D

N

R

V

S

D

L

L

I

I

D

D

E

E

V

V

T

Q

V

V

G

S

N

S

Q

D

T

E

A

S

F

I

D

D

T

M

A

A

R

R

L

Q

L

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

C

I

E

K

I

L

G

A

S

Q

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

F

V

V

L

A

I

I

I

F

P
|
P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

V

L

L

F

F

E

D

active site: K44 (= K65), S267 (= S288)
binding pyridoxal-5'-phosphate: K44 (= K65), N75 (= N96), G177 (= G198), G179 (= G200), T180 (= T201), G181 (= G202), T183 (= T204), G223 (= G244), S267 (= S288), P294 (= P315)
binding : T72 (= T93), S73 (= S94), G74 (= G95), T76 (= T97), G122 (= G143), M123 (= M144), K124 (= K145), G217 (= G238), P218 (= P239), H219 (= H240), Q222 (= Q243), G223 (= G244)

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)
57% identity, 94% coverage: 22:330/330 of query aligns to 75:381/392 of P47999

query
sites
P47999

I

I

Y

A

D

D

S

N

I

A

T

A

D

Q

T

L

I

I

G

G

N

K

T

T

P

P

I

M

V

V

R

Y

L

L

N

N

K

N

I

V

A

V

A

-

E

-

K

K

G

G

V

C

K

V

A

A

N

S

L

V

L

A

A

A

K

K

L

L

E

E

F

I

F

M

N

E

P

P

I

C

A

C

S

S

V

V

K

K

D

D

R

R

I

I

G

G

V

Y

H

S

M

M

I

I

T

T

V

D

L

A

E

E

T

K

G

G

K

L

I

I

K

T

P

P

G

G

V

K

T

S

T

V

L

L

I

V

E

E

P

S

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

G

L

L

A

A

F

F

V

I

A

A

A

S

R

K

G

G

Y

Y

K

K

L

L

I

I

L

L

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

L

E

E

R

R

K

V

M

L

L

L

A

R

L

A

L

F

G

G

A

A

E

E

L

L

V

V

L

L

T

T

P

E

A

P

P

A

Q

K

G

G

M

M

K

T

G

G

A

A

V

I

A

Q

K

K

A

A

E

E

L

I

S

L

A

K

T

T

P

P

D

N

S

S

V

Y

V

M

P

L

R

Q

Q

Q

F

F

D

D

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

Y

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

D

T

T

N

R

G

G

E

K

I

I

D

D

A

I

F

L

V

V

A

A

G

G

V

I

G

G

T

T

G

G

T

T

I

I

T

T

G

G

V

V

A

G

Q

R

V

F

L

I

K

K

P

E

R

R

K

K

P

P

G

E

I

L

K

K

I

V

V

I

A

G

I

V

E

E

P

P

E

T

D

E

S

S

P

A

I

I

L

L

S

S

G

G

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

I

V

P

P

S

K

I

N

L

L

D

D

R

L

S

A

L

I

I

V

D

D

E

E

V

Y

V

I

T

A

V

I

G

S

N

S

Q

E

T

E

A

A

F

I

D

E

T

T

A

S

R

K

L

Q

L

L

A

A

R

L

L

Q

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S

S

G

G

A

A

V

A

A

A

C

I

E

Q

I

V

G

A

S

K

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

I

V

A

L

V

I

V

I

F

P

P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

Q

L

L

F

F

E

Q

G

S

L

I

Sites not aligning to the query:

61 modified: N-acetylalanine

1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
59% identity, 93% coverage: 21:328/330 of query aligns to 2:307/320 of 1z7yA

query
sites
1z7yA

R

R

I

I

Y

A

D

K

S

D

I

V

T

T

D

E

T

L

I

I

G

G

N

N

T

T

P

P

I

L

V

V

R

Y

L

L

N

N

K

N

I

V

A

A

A

-

E

-

K

E

G

G

V

C

K

V

A

G

N

R

L

V

L

A

A

A

K

K

L

L

E

E

F

M

N

E

P

P

I

C

A

S

S

S

V

V

K
x
A

D

D

R

R

I

I

G

G

V

F

H

S

M

M

I

I

T

S

V

D

L

A

E

E

E

K

T

K

G

G

K

L

I

I

K

K

P

P

G

G

V

E

T

S

T

V

L

L

I

I

E

E

P

P

T

T

S

S

G
|
G

N
|
N

T
|
T

G

G

I

V

A

G

L

L

A

A

F

F

V

T

A

A

R

K

G

G

Y

Y

K

K

L

L

I

I

L

I

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

T

E

E

R

R

K

I

M

I

L

L

A

L

L

A

L

F

G

G

A

V

E

E

L

L

V

V

L

L

T

T

P

D

A

P

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

A

K

K

A

A

E

E

L

I

S

L

A

A

A

K

T

T

P

P

D

N

S

G

V

Y

V

M

P

L

R

Q

Q
|
Q

F

F

D

E

N

N

P

P

A

A

N

N

P

P

E

K

I

I

H

H

R

Y

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

K

D

G

T

T

N

G

G

G

E

K

I

I

D

D

A

G

F

F

V

V

A

S

G

G

V
x
I

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

T

T

G

G

V

A

A

G

Q

K

V

Y

L

L

K

K

P

E

R

Q

K

N

P

A

G

N

I

V

K

K

I

L

V

Y

A

G

I

V

E

E

P

P

E

V

D

E

S

S

P

A

I

I

L

L

S

S

G

G

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

S

I

V

L

L

D

N

R

V

S

D

L

L

I

I

D

D

E

E

V

V

T

Q

V

V

G

S

N

S

Q

D

T

E

A

S

F

I

D

D

T

M

A

A

R

R

L

Q

L

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

A

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

C

I

E

K

I

L

G

A

S

Q

R

R

P

P

E

E

F

N

A

A

G

G

K

K

N

L

I

F

V

V

L

A

I

I

I

F

P
|
P

S
|
S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

V

L

L

F

F

E

D

active site: A44 (≠ K65), S267 (= S288)
binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G95), N75 (= N96), T76 (= T97), Q145 (= Q166), I178 (≠ V199), G179 (= G200), T180 (= T201), G181 (= G202), T183 (= T204), G223 (= G244), S267 (= S288), P294 (= P315), S295 (= S316)

P0ABK5 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; S-carboxymethylcysteine synthase; Sulfate starvation-induced protein 5; SSI5; EC 2.5.1.47; EC 4.5.1.5 from Escherichia coli (strain K12) (see 5 papers)
57% identity, 94% coverage: 21:330/330 of query aligns to 3:315/323 of P0ABK5

query
sites
P0ABK5

R

K

I

I

Y

F

D

E

S

D

I

N

T

S

D

L

T

T

I

I

G

G

N

H

T

T

P

P

I

L

V

V

R

R

L

L

N

N

K

R

I

I

A

G

A

-

E

-

K

-

G

-

V

-

K

N

A

G

N

R

L

I

L

L

A

A

K

K

L

V

E

E

F

S

F

R

N

N

P

P

I

S

A

F

S

S

V

V

K
|
K

D

C

R

R

I

I

G

G

V

A

H

N

M

M

I

I

T

W

V

D

L

A

E

E

E

K

T

R

G

G

K

V

I

L

K

K

P

P

G

G

V

V

T

E

T

-

L

L

I

V

E

E

P

P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

A

L

L

A

A

F

Y

V

V

A

A

R

R

G

G

Y

Y

K

K

L

L

I

T

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

I

E

E

R

R

K

K

M

L

L

L

A

K

L

A

L

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

A

G

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

Q

K

K

A

A

E

E

L

I

S

V

A

A

A

S

T

N

P

P

D

E

S

K

-

Y

V

L

P

L

R

Q

Q

Q

F

F

D

S

N

N

P

P

A

A

N

N

P

P

E

E

I

I

H

H

R

E

L

K

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

D

T

T

N

D

G

G

E

Q

I

V

D

D

A

V

F

F

V

I

A

A

G

G

V

V

G

G

T

T

G

G

T

T

I

L

T

T

G

G

V

V

A

S

Q

R

V

Y

L

I

K

K

P

G

R

T

K

K

P

G

G

K

I

T

K

D

I

L

-

I

-

S

V

V

A

A

I

V

E

E

P

P

E

T

D

D

S

S

P

P

I

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

A

I

N

L

L

D

D

R

L

S

K

L

L

I

V

D

D

E

K

V

V

V

I

T

G

V

I

G

T

N

N

Q

E

T

E

A

A

F

I

D

S

T

T

A

A

R

R

L

R

L

L

A

M

R

E

L

E

E

E

G

G

I

I

P

L

A

A

G

G

I

I

S

S

G

G

A

A

V

V

A

A

C

L

E

K

I

L

G

Q

S

E

R

D

P

E

E

S

F

F

A

T

G

N

K

K

N

N

I

I

V

V

L

V

I

I

I

L

P

P

S

S

F

S

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

A

G

D

L

L

K42 (= K65) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Still stimulates tRNase activity of CdiA-CT in vitro and in vivo.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P0A1E3 Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine sulfhydrylase A; EC 2.5.1.47 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
58% identity, 94% coverage: 21:330/330 of query aligns to 3:315/323 of P0A1E3

query
sites
P0A1E3

R

K

I

I

Y

Y

D

E

S

D

I

N

T

S

D

L

T

T

I

I

G

G

N

H

T

T

P

P

I

L

V

V

R

R

L

L

N

N

K

R

I

I

A

G

A

-

E

-

K

-

G

-

V

-

K

N

A

G

N

R

L

I

L

L

A

A

K

K

L

V

E

E

F

S

F

R

N

N

P

P

I

S

A

F

S

S

V

V

K

K

D

C

R

R

I

I

G

G

V

A

H

N

M

M

I

I

T

W

V

D

L

A

E

E

E

K

T

R

G

G

K

V

I

L

K

K

P

P

G

G

V

V

T

E

T

-

L

L

I

V

E

E

P

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

A

L

L

A

A

F

Y

V

V

A

A

R

R

G

G

Y

Y

K

K

L

L

I

T

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

I

E

E

R

R

K

K

M

L

L

L

A

K

L

A

L

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

A

G

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

Q

K

K

A

A

E

E

L

I

S

V

A

A

A

S

T

D

P

P

D

Q

S

K

-

Y

V

L

P

L

R

Q

Q

Q

F

F

D

S

N

N

P

P

A

A

N

N

P

P

E

E

I

I

H

H

R

E

L

K

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

D

T

T

N

D

G

G

E

Q

I

V

D

D

A

V

F

F

V

I

A

S

G

G

V

V

G

G

T

T

G

G

T

T

I

L

T

T

G

G

V

V

A

T

Q

R

V

Y

L

I

K

K

P

G

R

T

K

K

P

G

G

K

I

T

K

D

I

L

-

I

-

T

V

V

A

A

I

V

E

E

P

P

E

T

D

D

S

S

P

P

I

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

G

I

N

L

L

D

D

R

L

S

K

L

L

I

I

D

D

E

K

V

V

T

G

V

I

G

T

N

N

Q

E

T

E

A

A

F

I

D

S

T

T

A

A

R

R

L

R

L

L

A

M

R

E

L

E

E

E

G

G

I

I

P

L

A

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

C

L

E

K

I

L

G

Q

S

E

R

D

P

E

E

S

F

F

A

T

G

N

K

K

N

N

I

I

V

V

L

V

I

I

I

L

P

P

S

S

F

S

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

A

G

D

L

L

N72 (= N96) binding pyridoxal 5'-phosphate
S273 (= S288) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

6z4nAAA structure of oass complexed with upar inhibitor (see paper)
58% identity, 94% coverage: 21:330/330 of query aligns to 4:316/321 of 6z4nAAA

query
sites
6z4nAAA

R

K

I

I

Y

Y

D

E

S

D

I

N

T

S

D

L

T

T

I

I

G

G

N

H

T

T

P

P

I

L

V

V

R

R

L

L

N

N

K

R

I

I

A

G

A

-

E

-

K

-

G

-

V

-

K

N

A

G

N

R

L

I

L

L

A

A

K

K

L

V

E

E

F

S

F

R

N

N

P

P

I

S

A

F

S

S

V

V

K
|
K

D

C

R

R

I

I

G

G

V

A

H

N

M

M

I

I

T

W

V

D

L

A

E

E

E

K

T

R

G

G

K

V

I

L

K

K

P

P

G

G

V

V

T

E

T

-

L

L

I

V

E

E

P

P

T
|
T

S

S

G
|
G

N
|
N

T
|
T

G

G

I

I

A

A

L

L

A

A

F

Y

V

V

A

A

R

R

G

G

Y

Y

K

K

L

L

I

T

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

I

E

E

R

R

K

K

M

L

L

L

A

K

L

A

L

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

A

G

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

Q

K

K

A

A

E

E

L

I

S

V

A

A

A

S

T

D

P

P

D

Q

S

K

-

Y

V

L

P

L

R

Q

Q
|
Q

F
|
F

D

S

N

N

P

P

A

A

N

N

P

P

E

E

I

I

H

H

R

E

L

K

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

D

T

T

N

D

G

G

E

Q

I

V

D

D

A

V

F

F

V

I

A

S

G

G

V
|
V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

T

T

G

G

V

V

A

T

Q

R

V

Y

L

I

K

K

P

G

R

T

K

K

P

G

G

K

I

T

K

D

I

L

-

I

-

T

V

V

A

A

I

V

E

E

P

P

E

T

D

D

S

S

P

P

I

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q
|
Q

G
|
G

I
|
I

G

G

A
|
A

G

G

F

F

I

I

P

P

S

G

I

N

L

L

D

D

R

L

S

K

L

L

I

I

D

D

E

K

V

V

T

G

V

I

G

T

N

N

Q

E

T

E

A

A

F

I

D

S

T

T

A

A

R

R

L

R

L

L

A

M

R

E

L

E

E

E

G

G

I

I

P

L

A

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

C

L

E

K

I

L

G

Q

S

E

R

D

P

E

E

S

F

F

A

T

G

N

K

K

N

N

I

I

V

V

L

V

I

I

I

L

P
|
P

S

S

F

S

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

A

G

D

L

L

binding pyridoxal-5'-phosphate: K43 (= K65), N73 (= N96), V177 (= V199), G178 (= G200), T179 (= T201), G180 (= G202), T182 (= T204), G230 (= G244), S274 (= S288), P301 (= P315)
binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K65), T70 (= T93), G72 (= G95), N73 (= N96), T74 (= T97), Q144 (= Q166), F145 (= F167), Q229 (= Q243), G230 (= G244), I231 (= I245), A233 (= A247)

8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
55% identity, 92% coverage: 25:327/330 of query aligns to 12:311/329 of 8b9wA

query
sites
8b9wA

S

S

I

V

T

D

D

A

T

L

I

I

G

G

N

N

T

T

P

P

I

A

V

V

R

Y

L

L

N

R

K

N

I

M

A

-

E

-

K

N

G

K

V

T

K

A

A

A

N

T

L

I

L

V

A

L

K

K

L

L

E

E

F

S

F

E

N

N

P

P

I

M

A

A

S

S

V

V

K
|
K

D

D

R

R

I

L

G

A

V

Y

H

A

M

I

I

Y

T

D

V

K

L

A

E

E

E

K

T

E

G

G

K

K

I

I

K

K

P

R

G

G

V

K

T

S

T

V

L

I

I

V

E

E

P

A

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

A

A

L

L

A

A

F

L

V

L

A

G

A

A

A

V

R

R

G

G

Y

Y

K

K

L

V

I

I

L

I

V

T

M

M

P

P

E

D

S

S

M

M

S

S

I

M

E

E

R

R

K

S

M

L

L

L

A

R

L

I

L

F

G

G

A

A

E

E

L

L

V

I

L

L

T

T

P

P

A

A

P

S

Q

L

G

G

M

M

K

K

G

G

A

A

V

V

A

A

K

M

A

A

E

N

E

R

L

I

S

V

A

S

A

N

T

N

P

P

D

D

S

A

V

V

V

L

P

A

R

D

Q

Q

F

F

D

C

N

T

P

K

A

Y

N

N

P

A

E

Q

I

I

H

H

R

E

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

R

D

Q

T

T

N

K

G

G

E

H

I

V

D

D

A

C

F

F

V

V

A

A

G

G

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

T

T

G

G

V

V

A

A

Q

R

V

F

L

L

K

K

P

S

R

V

K

G

P

C

G

N

I

A

K

N

I

I

V

V

A

A

I

V

E

E

P

P

E

Q

D

E

S

S

P

P

I

V

L

L

S

S

G

G

Q

R

P

P

G

G

P

P

H

H

K

R

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

I

V

P

P

S

E

I

V

L

L

D

D

R

R

S

E

L

L

I

V

D

D

E

E

V

I

T

Q

V

V

G

S

N

S

Q

D

T

K

A

A

F

I

D

E

T

T

A

A

R

Q

L

K

L

L

A

S

R

R

L

M

E

D

G

G

I

I

P

F

A

C

G

G

I

F

S
|
S

S

A

G

G

A

A

A

N

V

V

A

F

A

A

C

L

E

K

I

I

G

A

S

E

R

R

P

P

E

E

F

M

A

A

G

G

K

K

N

T

I

I

V

V

L

T

I

V

I

I

P
|
P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

Y

binding pyridoxal-5'-phosphate: K49 (= K65), N80 (= N96), G184 (= G200), T185 (= T201), G186 (= G202), T188 (= T204), G228 (= G244), S272 (= S288), P299 (= P315)

1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
57% identity, 94% coverage: 21:330/330 of query aligns to 2:314/322 of 1d6sA

query
sites
1d6sA

R

K

I

I

Y

Y

D

E

S

D

I

N

T

S

D

L

T

T

I

I

G

G

N

H

T

T

P

P

I

L

V

V

R

R

L

L

N

N

K

R

I

I

A

G

A

-

E

-

K

-

G

-

V

-

K

N

A

G

N

R

L

I

L

L

A

A

K

K

L

V

E

E

F

S

F

R

N

N

P

P

I

S

A

F

S

S

V

V

K
x
A

D

C

R

R

I

I

G

G

V

A

H

N

M

M

I

I

T

W

V

D

L

A

E

E

E

K

T

R

G

G

K

V

I

L

K

K

P

P

G

G

V

V

T

E

T

-

L

L

I

V

E

E

P

P

T
|
T

S
x
N

G

G

N
|
N

T
|
T

G

G

I

I

A

A

L

L

A

A

F

Y

V

V

A

A

R

R

G

G

Y

Y

K

K

L

L

I

T

L

L

V

T

M

M

P

P

E

E

S

T

M

M

S

S

I

I

E

E

R

R

K

K

M

L

L

L

A

K

L

A

L

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

A

G

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

Q

K

K

A

A

E

E

L

I

S

V

A

A

A

S

T

D

P

P

D

Q

S

K

-

Y

V

L

P

L

R

Q

Q
|
Q

F
|
F

D

S

N

N

P

P

A

A

N

N

P

P

E

E

I

I

H

H

R

E

L

K

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

D

T

T

N

D

G

G

E

Q

I

V

D

D

A

V

F

F

V

I

A

S

G

G

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

T

T

G

G

V

V

A

T

Q

R

V

Y

L

I

K

K

P

G

R

T

K

K

P

G

G

K

I

T

K

D

I

L

-

I

-

T

V

V

A

A

I

V

E

E

P

P

E

T

D

D

S

S

P

P

I

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

P

P

G

G

P

P

H

H

K

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

I

I

P

P

S

G

I

N

L

L

D

D

R

L

S

K

L

L

I

I

D

D

E

K

V

V

T

G

V

I

G

T

N

N

Q

E

T

E

A

A

F

I

D

S

T

T

A

A

R

R

L

R

L

L

A

M

R

E

L

E

E

E

G

G

I

I

P

L

A

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

C

L

E

K

I

L

G

Q

S

E

R

D

P

E

E

S

F

F

A

T

G

N

K

K

N

N

I

I

V

V

L

V

I

I

I

L

P
|
P

S

S

F

S

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

A

L

L

F

F

E

A

G

D

L

L

active site: A41 (≠ K65), G228 (= G244)
binding methionine: T68 (= T93), N69 (≠ S94), N71 (= N96), T72 (= T97), Q142 (= Q166), F143 (= F167), G176 (= G200), G228 (= G244)
binding pyridoxal-5'-phosphate: N71 (= N96), G176 (= G200), T177 (= T201), G178 (= G202), T180 (= T204), G228 (= G244), S272 (= S288), P299 (= P315)

3t4pA Crystal structure of o-acetyl serine sulfhydrylase from leishmania donovani in complex with designed tetrapeptide (see paper)
53% identity, 94% coverage: 22:330/330 of query aligns to 10:315/319 of 3t4pA

query
sites
3t4pA

I

V

Y

A

D

Q

S

S

I

I

T

D

D

Q

T

L

I

I

G

G

N

Q

T

T

P

P

I

A

V

L

R

Y

L

L

N

N

K

K

I

L

A

-

E

-

K

N

G

N

V

T

K

K

A

A

N

K

L

V

A

L

K

K

L

M

E

E

F

C

F

E

N

N

P

P

I

M

A

A

S

S

V

V

K
|
K

D

D

R

R

I

L

G

G

V

F

H

A

M

I

I

Y

T

D

V

K

L

A

E

E

E

K

T

E

G

G

K

K

I

L

K

I

P

P

G

G

V

K

T

S

T

I

L

V

I

V

E

E

P

S

T
x
S

S
|
S

G
|
G

N

N

T
|
T

G

G

I

V

A

S

L

L

A

A

F

H

V

L

A

G

A

A

A

I

R

R

G

G

Y

Y

K

K

L

V

I

I

L

I

V

T

M

M

P

P

E

E

S

S

M

M

S

S

I

L

E

E

R

R

K

C

M

L

L

L

A

R

L

I

L

F

G

G

A

A

E

E

L

V

V

I

L

L

T

T

P

P

A

A

P

A

Q

L

G

G

M
|
M

K

K

G

G

A

A

V

V

A

A

K

M

A

A

E

K

L

I

S

V

A

A

T

N

P

P

D

N

S

A

V

V

V

L

P

A

R

D

Q
|
Q

F
|
F

D

A

N

T

P

K

A

Y

N

N

P

A

E

L

I

I

H

H

R

E

L

E

T

T

A

G

E

P

E

E

I

I

W

W

N

E

D

Q

T

T

N

N

G

H

E

N

I

V

D

D

A

C

F

F

V

I

A

A

G

G

V

V

G

G

T

T

G

G

T

T

I

L

T

T

G

G

V

V

A

A

Q

R

V

A

L

L

K

K

P

K

R

M

K

G

P

S

G

H

I

A

K

R

I

I

V

V

A

A

I

V

E

E

P

P

E

T

D

E

S

S

P

P

I

V

L

L

S

S

G

G

Q

K

P

P

G
|
G

P
|
P

H
|
H

K

K

I

I

Q

Q

G
|
G

I

I

G
|
G

A
x
P

G

G

F

F

I

V

P

P

S

D

I

V

L

L

D

D

R

R

S

S

L

L

I

I

D

D

E

E

V

V

V

L

T

C

V

V

G

A

N

G

Q

D

T

D

A

A

F

I

D

E

T

T

A

A

R

L

L

K

L

L

A

T

R

R

L

S

E

D

G

G

I

V

P

F

A

C

G

G

I

F

S
|
S

S

G

G

G

A

A

A

N

V

V

A

Y

A

A

C

L

E

K

I

I

G

A

S

E

R

R

P

P

E

E

F

M

A

E

G

G

K

K

N

T

I

I

V

V

L

T

I

V

I

I

P

P

S

S

F

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

A

T

L

L

F

Y

E

R

G

S

L

V

active site: K50 (= K65), S273 (= S288)
binding : S78 (≠ T93), S79 (= S94), G80 (= G95), T82 (= T97), M129 (= M144), Q151 (= Q166), F152 (= F167), G223 (= G238), P224 (= P239), H225 (= H240), G229 (= G244), G231 (= G246), P232 (≠ A247)

Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
52% identity, 94% coverage: 19:327/330 of query aligns to 4:310/341 of Q93244

query
sites
Q93244

R

R

G

N

R

S

I

I

Y

G

D

E

S

N

I

A

T

A

D

A

T

L

I

I

G

G

N

N

T

T

P

P

I

M

V

V

R

Y

L

I

N

N

K

K

I

L

A

T

A

-

E

-

K

K

G

G

V

L

K

P

A

G

N

T

L

V

L

A

A

V

K

K

L

I

E

E

F

Y

F

M

N

N

P

P

I

A

A

G

S

S

V

V

K

K

D

D

R

R

I

I

G

G

V

A

H

A

M

M

I

L

T

A

V

A

L

A

E

E

E

K

T

D

G

G

K

T

I

V

K

I

P

P

G

G

V

V

T

T

L

L

I

I

E

E

P
|
P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

A

A

L

L

A

A

F

F

V

V

A
|
A

A

A

R

K

G

G

Y

Y

K

R

L

C

I

I

L

V

V

T

M

M

P

P

E

A

S

S

M

M

S

S

I

G

E

E

R

R

K

T

M

L

L

L

A

K

L

A

L

Y

G

G

A

S

E

E

L

V

V

V

L

L

T

T

P

D

A

P

P

A

Q

K

G

G

M

M

K

K

G

G

A

A

V

I

A

D

K

M

A

A

E

N

E

Q

L

L

S

K

A

E

A

N

T

I

P

P

D

G

S
|
S

V

I

P

L

R

A

Q

Q

F

F

D

D

N

N

P

P

A

N

N

N

P

P

E

L

I

V

H

H

R

Y

L

Q

T

T

A

G

E

P

E

E

I

I

W

W

N

R

D

Q

T

T

N

K

G

G

E

T

I

V

D

D

A

A

F

V

V

V

A

F

G
|
G

V

V

G
|
G

T

T

G

G

T

T

I

I

T

T

G

G

V

V

A

G

Q

R

V

Y

L

L

K

Q

P

E

R

Q

K

N

P

P

G

G

I

V

K

R

I

V

V

F

A

A

I

V

E

E

P

P

E

E

D

E

S

S

P

A

I

I

L

L

S

S

G

G

G

R

Q

P

P

A

G

G

P

P

H

H

K

K

I

I

Q

Q

G

G

I

I

G
|
G

A

A

G

G

F

F

I

A

P

P

S

A

I

V

L

L

D

D

R

T

S

K

L

I

I

Y

D

E

E

D

V

V

V

I

T

R

V

I

G

H

N

S

Q

D

T

E

A

A

F

I

D

V

T

M

A

A

R

Q

L
x
R

L

L

A

S

R

Y

L

E

E

E

G

G

I

L

P

L

A

G

G

G

I

I

S

S

S
|
S

G

G

A

A

A

N

V

V

A

A

C

L

E

Q

I

L

G

A

S

A

R

R

P

P

E

E

F

M

A

A

G

G

K

K

N

L

I

I

V

V

L
x
T

I

C

I

L

P

P

S

S

F

C

A

G

E

E

R

R

Y

Y

L

M

S

T

T

S

A

P

L

L

F

Y

P75 (= P92) mutation to L: In n5537; severe loss of protein stability.
A88 (= A105) mutation to V: In n5522; severe loss of protein stability.
S144 (= S161) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
G181 (= G198) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
G183 (= G200) mutation to R: In n5515; severe loss of protein stability.
G229 (= G246) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
R259 (≠ L276) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
S272 (= S289) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
T295 (≠ L312) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.

Query Sequence

>WP_020174433.1 NCBI__GCF_000385335.1:WP_020174433.1
MAQAALKAESPATTQVPGRGRIYDSITDTIGNTPIVRLNKIAAEKGVKANLLAKLEFFNP
IASVKDRIGVHMITVLEETGKIKPGVTTLIEPTSGNTGIALAFVAAARGYKLILVMPESM
SIERRKMLALLGAELVLTPAPQGMKGAVAKAEELSAATPDSVVPRQFDNPANPEIHRLTT
AEEIWNDTNGEIDAFVAGVGTGGTITGVAQVLKPRKPGIKIVAIEPEDSPILSGGQPGPH
KIQGIGAGFIPSILDRSLIDEVVTVGNQTAFDTARLLARLEGIPAGISSGAAVAAACEIG
SRPEFAGKNIVLIIPSFAERYLSTALFEGL

Or try a new SitesBLAST search

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