SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_015798746.1 NCBI__GCF_000023265.1:WP_015798746.1 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)
73% identity, 100% coverage: 1:310/311 of query aligns to 1:310/310 of P9WP55

query
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P9WP55

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K44 (= K44) modified: N6-(pyridoxal phosphate)lysine
N74 (= N74) binding pyridoxal 5'-phosphate
GTGGT 178:182 (= GTGGT 178:182) binding pyridoxal 5'-phosphate
S266 (= S266) 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)
73% identity, 98% coverage: 1:306/311 of query aligns to 1:306/306 of 2q3dA

query
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2q3dA

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active site: K44 (= K44), S266 (= S266), P293 (= P293)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K44), T71 (= T71), S72 (= S72), N74 (= N74), T75 (= T75), Q144 (= Q144), V177 (= V177), G178 (= G178), T179 (= T179), G180 (= G180), T182 (= T182), G222 (= G222), I223 (= I223), S266 (= S266), P293 (= P293), D294 (≠ S294)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
73% identity, 96% coverage: 1:300/311 of query aligns to 1:300/300 of 3zeiA

query
sites
3zeiA

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active site: K44 (= K44), S266 (= S266), P293 (= P293)
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 (= T71), S72 (= S72), I126 (= I126), Q144 (= Q144), F145 (= F145), K215 (= K215), G222 (= G222), A225 (= A225), F227 (= F227)
binding pyridoxal-5'-phosphate: K44 (= K44), N74 (= N74), V177 (= V177), G178 (= G178), T179 (= T179), G180 (= G180), T182 (= T182), G222 (= G222), S266 (= S266), P293 (= P293), D294 (≠ S294)

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)
73% identity, 96% coverage: 1:300/311 of query aligns to 1:300/300 of 2q3cA

query
sites
2q3cA

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active site: K44 (= K44), S266 (= S266), P293 (= P293)
binding : T71 (= T71), S72 (= S72), G73 (= G73), T75 (= T75), M122 (= M122), Q144 (= Q144), K215 (= K215), G222 (= G222), A225 (= A225)

4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
62% identity, 100% coverage: 1:310/311 of query aligns to 1:313/318 of 4lmaA

query
sites
4lmaA

M

M

R

R

I

I

A

A

E

H

D

D

V

V

T

T

K

E

L

L

V

V

G

G

N

R

T

T

P

P

L

L

V

V

R

Q

L

L

N

N

R

R

V

I

-

P

-

Q

I

A

D

E

G

G

A

C

G

L

A

G

T

R

V

I

V

V

A

M

K

K

L

L

E

E

F

G

Y

M

N

N

P

P

A

A

N

A

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

T

A

H

M

M

I

I

D

N

A

S

A

A

E

E

R

K

E

A

G

G

R

L

L

I

K

N

P

P

G

E

S

T

T

T

I

V

-

L

V

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

M

M

V

T

A

A

R

K

G

G

Y

Y

R

R

C

L

I

I

L

L

T

T

M

M

P

P

E

E

T

T

M

M

S

S

R

L

E

E

R

R

M

A

L

M

L

L

R

K

A

A

F

Y

G

G

A

A

E

T

L

L

V

E

L

L

T

T

P

P

G

G

P

S

E

Q

G

G

M

M

G

K

G

G

A

A

I

I

A

L

R

R

A

A

E

Q

Q

Q

L

I

V

V

K

D

E

S

H

I

P

P

D

G

Y

A

V

Y

M

M

L

L

Q

Q

F

F

E

R

N

N

P

P

A

S

N

N

P

P

A

E

I

I

H

H

R

R

A

L

T

T

A

A

E

E

L

I

W

W

R

Q

D

D

T

T

D

E

G

G

A

Q

I

V

D

D

V

F

V

I

V

V

G

A

G

G

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

S

T

G

G

I

V

G

A

Q

E

A

V

L

I

K

K

P

S

R

R

R

K

P

P

S

S

L

F

Q

Q

L

V

I

V

A

A

V

V

E

E

P

P

A

F

A

N

S

S

P

P

V

V

L

I

S

S

G

G

Q

N

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

E

T

V

Y

L

D

R

A

T

T

D

V

L

V

I

D

D

E

E

V

V

V

I

Q

T

V

V

T

S

N

D

D

E

E

E

A

A

F

F

E

Q

M

F

A

G

R

R

M

L

A

A

R

K

E

E

G

G

L

L

V

S

G

G

I

I

S
|
S

S

S

G

G

A

A

A

N

V

L

A

C

A

A

R

I

R

Q

V

L

A

A

Q

Q

R

R

P

P

E

E

S

N

A

E

G

G

K

K

L

L

I

I

A

V

V

V

I

I

I

Q

P
|
P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

L

L

M

F

F

A

Q

D

N

L

I

A

E

D

E

active site: K46 (= K44), S269 (= S266)
binding pyridoxal-5'-phosphate: K46 (= K44), N77 (= N74), G181 (= G178), T182 (= T179), G183 (= G180), T185 (= T182), G225 (= G222), S269 (= S266), P296 (= P293)

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
65% identity, 99% coverage: 1:307/311 of query aligns to 1:310/310 of 4lmbA

query
sites
4lmbA

M

M

R

L

I

I

A

A

E

R

D

D

V

I

T

T

K

Q

L

L

V

V

G

G

N

R

T

T

P

P

L

L

V

V

R

Q

L

L

N

N

R

R

-

I

-

P

V

V

I

A

D

E

G

G

A

V

G

K

A

A

T

R

V

I

V

V

A

V

K

K

L

L

E

E

F

S

Y

M

N

N

P

P

A

A

N

A

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

V

A

S

M

M

I

V

D

E

A

D

A

A

E

E

R

A

E

A

G

G

R

L

L

I

K

H

P

P

G

D

S

K

T

T

I

I

-

L

V

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

M

M

V

V

A

A

R

K

G

G

Y

Y

R

R

C

L

I

V

L

L

T

T

M

M

P

P

E

E

T

T

M
|
M

S

S

R

L

E

E

R

R

M

A

L

M

L

L

R

K

A

A

F

Y

G

G

A

A

E

Q

L

L

V

E

L

L

T

T

P

P

G

G

P

S

E

Q

G

G

M
|
M

G

E

G

G

A

A

I

I

A

T

R

R

A

A

E

E

Q

E

L

I

V

V

K

E

E

N

H

T

P

P

D

N

Y

A

V

Y

M

S

L

L

Q

Q

Q
|
Q

F
|
F

E

R

N

N

P

P

A

A

N

N

P

P

A

K

I

I

H

H

R

R

A

E

T

T

A

A

E

E

L

I

W

W

R

A

D

D

T

T

D

D

G

G

A

L

I

V

D

D

V

I

V

V

V

I

G

G

V
|
V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

S

T

G

G

I

I

G

A

Q

E

A

T

L

I

K

K

P

P

R

R

P

P

S

Q

L

F

Q

Q

L

A

I

I

A

A

V

V

E

E

P

P

A

S

A

N

S

S

P

P

V

V

L

L

S

S

G

G

Q

Q

K

P

G

G

P

P

H

H

P

K

I

I

Q
|
Q

G
|
G

I
|
I

G

G

A
|
A

G

G

F

F

V

I

P

P

G

A

T

I

Y

F

D

R

A

P

T

E

V

L

V

I

D

D

E

E

V

V

V

I

Q

I

V

V

T

D

N

D

D

T

E

E

A

A

F

F

E

A

M

Y

A

A

R

R

M

L

A

A

R

R

E

Q

E

E

G

G

L

L

V

S

G

G

I

I

S
|
S

S

A

G

G

A

A

V

L

A

W

A

A

R

I

R

Q

V

V

A

G

Q

K

R

R

P

P

E

E

S

N

A

E

G

D

K

K

L

L

I

I

A

V

V

M

I

I

I

Q

P
|
P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

A

K

D

D

active site: K46 (= K44), S269 (= S266)
binding cysteine: K46 (= K44), T74 (= T71), S75 (= S72), N77 (= N74), T78 (= T75), M101 (= M98), M125 (= M122), M125 (= M122), Q147 (= Q144), F148 (= F145), Q224 (= Q221), G225 (= G222), G225 (= G222), I226 (= I223), A228 (= A225)
binding pyridoxal-5'-phosphate: K46 (= K44), N77 (= N74), V180 (= V177), G181 (= G178), T182 (= T179), G183 (= G180), T185 (= T182), G225 (= G222), S269 (= S266), P296 (= P293)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
59% identity, 99% coverage: 1:308/311 of query aligns to 11:319/323 of 4aecA

query
sites
4aecA

M

L

R

N

I

I

A

A

E

D

D

N

V

V

T

S

K

Q

L

L

V

I

G

G

N

K

T

T

P

P

L

M

V

V

R

Y

L

L

N

N

R

S

V

I

I

A

D

K

G

G

A

C

G

V

A

A

T

N

V

I

V

A

A

A

K

K

L

L

E

E

F

I

Y

M

N

E

P

P

A

C

N

C

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

V

Y

A

S

M

M

I

V

D

T

A

D

A

A

E

E

R

Q

E

K

G

G

R

F

L

I

K

S

P

P

G

G

-

K

S

S

T

V

I

L

V

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

M

F

V

I

A

A

A

S

R

R

G

G

Y

Y

R

R

C

L

I

I

L

L

T

T

M

M

P

P

E

A

T

S

M

M

S

S

R

M

E

E

R

R

M

V

L

L

R

K

A

A

F

F

G

G

A

A

E

E

L

L

V

V

L

L

T

T

P

D

G

P

P

A

E

K

G

G

M

M

G

T

G

G

A

A

I

V

A

Q

R

K

A

A

E

E

Q

E

L

I

V

L

K

K

E

N

H

T

P

P

D

D

Y

A

V

Y

M

M

L

L

Q

Q

F

F

E

D

N

N

P

P

A

A

N

N

P

P

A

K

I

I

H

H

R

Y

A

E

T

T

A

G

E

P

E

E

L

I

W

W

R

D

D

D

T

T

D

K

G

G

A

K

I

V

D

D

V

I

V

F

V

V

G

A

G

G

V
x
I

G
|
G

T
|
T

G
|
G

T
|
T

I

I

S

T

G

G

I

V

G

G

Q

R

A

F

L

I

K

K

P

E

R

K

R

N

P

P

S

K

L

T

Q

Q

L

V

I

I

A

G

V

V

E

E

P

P

A

T

A

E

S

S

P

D

V

I

L

L

S

S

G

G

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

K

T

N

Y

L

D

D

A

Q

T

K

V

I

V

M

D

D

E

E

V

V

V

I

Q

A

V

I

T

S

N

S

D

E

E

E

A

A

F

I

E

E

M

T

A

A

R

K

R

Q

M

L

A

A

R

L

E

K

E

E

G

G

L

L

L

M

V

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

R

I

R

K

V

V

A

A

Q

K

R

R

P

P

E

E

S

N

A

A

G

G

K

K

L

L

I

I

A

A

V

V

I

V

I

F

P
|
P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

P

L

L

F

F

A

Q

D

S

L

I

active site: K54 (= K44), S277 (= S266)
binding pyridoxal-5'-phosphate: K54 (= K44), N85 (= N74), I188 (≠ V177), G189 (= G178), T190 (= T179), G191 (= G180), G192 (= G181), T193 (= T182), G233 (= G222), S277 (= S266), P304 (= P293)

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)
59% identity, 99% coverage: 1:308/311 of query aligns to 73:381/392 of P47999

query
sites
P47999

M

L

R

N

I

I

A

A

E

D

D

N

V

A

T

A

K

Q

L

L

V

I

G

G

N

K

T

T

P

P

L

M

V

V

R

Y

L

L

N

N

R

N

V

V

I

V

D

K

G

G

A

C

G

V

A

A

T

S

V

V

V

A

A

A

K

K

L

L

E

E

F

I

Y

M

N

E

P

P

A

C

N

C

S

S

V

V

K

K

D

D

R

R

I

I

G

G

V

Y

A

S

M

M

I

I

D

T

A

D

A

A

E

E

R

E

E

K

G

G

R

L

L

I

K

T

P

P

G

G

-

K

S

S

T

V

I

L

V

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

M

F

V

I

A

A

A

S

R

K

G

G

Y

Y

R

K

C

L

I

I

L

L

T

T

M

M

P

P

E

A

T

S

M

M

S

S

R

L

E

E

R

R

M

V

L

L

R

R

A

A

F

F

G

G

A

A

E

E

L

L

V

V

L

L

T

T

P

E

G

P

P

A

E

K

G

G

M

M

G

T

G

G

A

A

I

I

A

Q

R

K

A

A

E

E

Q

E

L

I

V

L

K

K

E

K

H

T

P

P

D

N

Y

S

V

Y

M

M

L

L

Q

Q

F

F

E

D

N

N

P

P

A

A

N

N

P

P

A

K

I

I

H

H

R

Y

A

E

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

R

G

G

A

K

I

I

D

D

V

I

V

L

V

V

G

A

G

G

V

I

G

G

T

T

G

G

T

T

I

I

S

T

G

G

I

V

G

G

Q

R

A

F

L

I

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K

P

E

R

R

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K

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P

S

E

L

L

Q

K

L

V

I

I

A

G

V

V

E

E

P

P

A

T

A

E

S

S

P

A

V

I

L

L

S

S

G

G

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

V

V

P

P

G

K

T

N

Y

L

D

D

A

L

T

A

V

I

V

V

D

D

E

E

V

Y

V

I

Q

A

V

I

T

S

N

S

D

E

E

E

A

A

F

I

E

E

M

T

A

S

R

K

R

Q

M

L

A

A

R

L

E

Q

E

E

G

G

L

L

V

V

G

G

I

I

S

S

G

G

A

A

V

A

A

A

R

I

R

Q

V

V

A

A

Q

K

R

R

P

P

E

E

S

N

A

A

G

G

K

K

L

L

I

I

A

A

V

V

I

V

I

F

P

P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

Q

L

L

F

F

A

Q

D

S

L

I

Sites not aligning to the query:

61 modified: N-acetylalanine

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
60% identity, 99% coverage: 1:308/311 of query aligns to 2:309/310 of 5xoqA

query
sites
5xoqA

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binding : T72 (= T71), S73 (= S72), G74 (= G73), T76 (= T75), M123 (= M122), Q144 (= Q144), R218 (≠ P217), H219 (= H218), Q222 (= Q221), G223 (= G222), A226 (= A225)

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)
60% identity, 98% coverage: 2:305/311 of query aligns to 4:308/322 of P47998

query
sites
P47998

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K46 (= K44) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
T74 (= T71) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
S75 (= S72) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
N77 (= N74) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
T78 (= T75) mutation T->A,S: Reduction of cysteine synthase activity.
Q147 (= Q144) mutation Q->A,E: Strong reduction of cysteine synthase activity.
H157 (= H154) mutation H->Q,N: Slight reduction of cysteine synthase activity.
G162 (≠ A159) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (= GTGGT 178:182) binding pyridoxal 5'-phosphate
T182 (= T179) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T182) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ Q214) mutation to A: Impaired interaction with SAT1.
H221 (= H218) mutation to A: Impaired interaction with SAT1.
K222 (≠ P219) mutation to A: Impaired interaction with SAT1.
S269 (= S266) 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)
60% identity, 98% coverage: 2:305/311 of query aligns to 2:306/320 of 2isqA

query
sites
2isqA

R

R

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A

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active site: K44 (= K44), S267 (= S266)
binding pyridoxal-5'-phosphate: K44 (= K44), N75 (= N74), G177 (= G176), G179 (= G178), T180 (= T179), G181 (= G180), T183 (= T182), G223 (= G222), S267 (= S266), P294 (= P293)
binding : T72 (= T71), S73 (= S72), G74 (= G73), T76 (= T75), G122 (= G121), M123 (= M122), K124 (≠ G123), G217 (= G216), P218 (= P217), H219 (= H218), Q222 (= Q221), G223 (= G222)

7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
61% identity, 97% coverage: 3:305/311 of query aligns to 3:306/309 of 7n2tA

query
sites
7n2tA

I

I

A

A

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D

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N

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V

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A

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R
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R

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F

F

binding phosphate ion: R277 (= R276), R281 (= R280)

1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
60% identity, 98% coverage: 2:305/311 of query aligns to 2:306/320 of 1z7yA

query
sites
1z7yA

R

R

I

I

A

A

E

K

D

D

V

V

T

T

K

E

L

L

V

I

G

G

N

N

T

T

P

P

L

L

V

V

R

Y

L

L

N

N

R

N

V

V

I

A

D

E

G

G

A

C

G

V

A

G

T

R

V

V

V

A

A

A

K

K

L

L

E

E

F

M

Y

M

N

E

P

P

A

C

N

S

S

S

V

V

K
x
A

D

D

R

R

I

I

G

G

V

F

A

S

M

M

I

I

D

S

A

D

A

A

E

E

R

K

E

K

G

G

R

L

L

I

K

K

P

P

G

G

-

E

S

S

T

V

I

L

V

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

M

F

V

T

A

A

R

K

G

G

Y

Y

R

K

C

L

I

I

L

I

T

T

M

M

P

P

E

A

T

S

M

M

S

S

R

T

E

E

R

R

M

I

L

I

L

L

R

L

A

A

F

F

G

G

A

V

E

E

L

L

V

V

L

L

T

T

P

D

G

P

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

A

R

K

A

A

E

E

Q

E

L

I

V

L

K

A

E

K

H

T

P

P

D

N

Y

G

V

Y

M

M

L

L

Q

Q

Q
|
Q

F

F

E

E

N

N

P

P

A

A

N

N

P

P

A

K

I

I

H

H

R

Y

A

E

T

T

A

G

E

P

E

E

L

I

W

W

R

K

D

G

T

T

D

G

G

G

A

K

I

I

D

D

V

G

V

F

V

V

G

S

G

G

V
x
I

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

S

T

G

G

I

A

G

G

Q

K

A

Y

L

L

K

K

P

E

R

Q

R

N

P

A

S

N

L

V

Q

K

L

L

I

Y

A

G

V

V

E

E

P

P

A

V

A

E

S

S

P

A

V

I

L

L

S

S

G

G

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

S

T

V

Y

L

D

N

A

V

T

D

V

L

V

I

D

D

E

E

V

V

Q

Q

V

V

T

S

N

S

D

D

E

E

A

S

F

I

E

D

M

M

A

A

R

R

R

Q

M

L

A

A

R

L

E

K

E

E

G

G

L

L

V

V

G

G

I

I

S
|
S

S

S

G

G

A

A

V

A

A

A

R

I

R

K

V

L

A

A

Q

Q

R

R

P

P

E

E

S

N

A

A

G

G

K

K

L

L

I

F

A

V

V

A

I

I

I

F

P
|
P

S
|
S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

V

L

L

F

F

active site: A44 (≠ K44), S267 (= S266)
binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G73), N75 (= N74), T76 (= T75), Q145 (= Q144), I178 (≠ V177), G179 (= G178), T180 (= T179), G181 (= G180), T183 (= T182), G223 (= G222), S267 (= S266), P294 (= P293), S295 (= S294)

Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
55% identity, 99% coverage: 3:311/311 of query aligns to 7:316/341 of Q93244

query
sites
Q93244

I

I

A

G

E

E

D

N

V

A

T

A

K

A

L

L

V

I

G

G

N

N

T

T

P

P

L

M

V

V

R

Y

L

I

N

N

R

K

V

L

I

T

D

K

G

G

A

L

G

P

A

G

T

T

V

V

V

A

A

V

K

K

L

I

E

E

F

Y

Y

M

N

N

P

P

A

A

N

G

S

S

V

V

K

K

D

D

R

R

I

I

G

G

V

A

A

A

M

M

I

L

D

A

A

A

E

E

R

K

E

D

G

G

R

T

L

V

K

I

P

P

G

G

-

V

S

T

T

T

I

L

V

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

M

F

V

V

A
|
A

A

A

R

K

G

G

Y

Y

R

R

C

C

I

I

L

V

T

T

M

M

P

P

E

A

T

S

M

M

S

S

R

G

E

E

R

R

M

T

L

L

R

K

A

A

F

Y

G

G

A

S

E

E

L

V

V

V

L

L

T

T

P

D

G

P

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

D

R

M

A

A

E

N

Q

Q

L

L

V

K

K

E

E

N

H

I

P

P

D

G

Y
x
S

V

I

M

I

L

L

Q

A

Q

Q

F

F

E

D

N

N

P

P

A

N

N

N

P

P

A

L

I

V

H

H

R

Y

A

Q

T

T

A

G

E

P

E

E

L

I

W

W

R

R

D

Q

T

T

D

K

G

G

A

T

I

V

D

D

V

A

V

V

G

F

G
|
G

V

V

G
|
G

T

T

G

G

T

T

I

I

S

T

G

G

I

V

G

G

Q

R

A

Y

L

L

K

Q

P

E

R

Q

R

N

P

P

S

G

L

V

Q

R

L

V

I

F

A

A

V

V

E

E

P

P

A

E

S

S

P

A

V

I

L

L

S

S

G

G

G

R

Q

P

K

A

G

G

P

P

H

H

P

K

I

I

Q

Q

G

G

I

I

G
|
G

A

A

G

G

F

F

V

A

P

P

G

A

T

V

Y

L

D

D

A

T

T

K

V

I

V

Y

D

E

E

D

V

V

V

I

Q

R

V

I

T

H

N

S

D

D

E

E

A

A

F

I

E

V

M

M

A

A

R

Q

R
|
R

M

L

A

S

R

Y

E

E

G

G

L

L

V

G

G

G

I

I

S

S

S
|
S

G

G

A

A

A

N

V

V

A

A

R

L

R

Q

V

L

A

A

Q

A

R

R

P

P

E

E

S

M

A

A

G

G

K

K

L

L

I

I

A

V

V
x
T

I

C

I

L

P

P

S

S

F

C

G

G

E

E

R

R

Y

Y

L

M

S

T

T

S

P

P

L

L

F

Y

A

T

D

D

L

I

A

R

D

E

A

S

P75 (= P70) mutation to L: In n5537; severe loss of protein stability.
A88 (= A83) mutation to V: In n5522; severe loss of protein stability.
S144 (≠ Y139) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
G181 (= G176) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
G183 (= G178) mutation to R: In n5515; severe loss of protein stability.
G229 (= G224) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
R259 (= R254) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
S272 (= S267) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
T295 (≠ V290) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.

6z4nAAA structure of oass complexed with upar inhibitor (see paper)
57% identity, 99% coverage: 2:308/311 of query aligns to 4:316/321 of 6z4nAAA

query
sites
6z4nAAA

R

K

I

I

A

Y

E

E

D

D

V

N

T

S

K

L

L

T

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

N

N

R

R

V

I

I

G

D

N

G

G

A

-

G

-

A

-

T

R

V

I

V

L

A

A

K

K

L

V

E

E

F

S

Y

R

N

N

P

P

A

S

N

F

S

S

V

V

K
|
K

D

C

R

R

I

I

G

G

V

A

A

N

M

M

I

I

D

W

A

D

A

A

E

E

R

K

E

R

G

G

R

V

L

L

K

K

P

P

G

G

S

V

T

E

I

L

V

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

M

Y

V

V

A

A

R

R

G

G

Y

Y

R

K

C

L

I

T

L

L

T

T

M

M

P

P

E

E

T

T

M

M

S

S

R

I

E

E

R

R

M

K

L

L

R

K

A

A

F

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

G

G

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

Q

R

K

A

A

E

E

Q

E

L

I

V

V

K

A

E

S

H

D

P

P

D

Q

-

K

Y

Y

V

L

M

L

L

L

Q

Q

Q
|
Q

F
|
F

E

S

N

N

P

P

A

A

N

N

P

P

A

E

I

I

H

H

R

E

A

K

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

D

G

G

A

Q

I

V

D

D

V

V

V

F

V

I

G

S

G

G

V
|
V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

S

T

G

G

I

V

G

T

Q

R

A

Y

L

I

K

K

P

G

R

T

R

K

P

G

S

K

L

T

Q

D

L

L

I

I

-

T

-

V

A

A

V

V

E

E

P

P

A

T

A

D

S

S

P

P

V

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q
|
Q

G
|
G

I
|
I

G

G

A
|
A

G

G

F

F

V

I

P

P

G

G

T

N

Y

L

D

D

A

L

T

K

V

L

V

I

D

D

E

K

V

V

Q

G

V

I

T

T

N

N

D

E

E

E

A

A

F

I

E

S

M

T

A

A

R

R

M

L

A

M

R

E

E

E

G

G

L

I

L

L

V

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

R

L

R

K

V

L

A

Q

Q

E

R

D

P

E

E

S

S

F

A

T

G

N

K

K

L

N

I

I

A

V

V

V

I

I

I

L

P
|
P

S

S

F

S

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

A

A

D

D

L

L

binding pyridoxal-5'-phosphate: K43 (= K44), N73 (= N74), V177 (= V177), G178 (= G178), T179 (= T179), G180 (= G180), T182 (= T182), G230 (= G222), S274 (= S266), P301 (= P293)
binding (1~{S},2~{S})-1-[(4-methylphenyl)methyl]-2-phenyl-cyclopropane-1-carboxylic acid: K43 (= K44), T70 (= T71), G72 (= G73), N73 (= N74), T74 (= T75), Q144 (= Q144), F145 (= F145), Q229 (= Q221), G230 (= G222), I231 (= I223), A233 (= A225)

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)
57% identity, 99% coverage: 2:308/311 of query aligns to 3:315/323 of P0A1E3

query
sites
P0A1E3

R

K

I

I

A

Y

E

E

D

D

V

N

T

S

K

L

L

T

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

N

N

R

R

V

I

I

G

D

N

G

G

A

-

G

-

A

-

T

R

V

I

V

L

A

A

K

K

L

V

E

E

F

S

Y

R

N

N

P

P

A

S

N

F

S

S

V

V

K

K

D

C

R

R

I

I

G

G

V

A

A

N

M

M

I

I

D

W

A

D

A

A

E

E

R

K

E

R

G

G

R

V

L

L

K

K

P

P

G

G

S

V

T

E

I

L

V

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

M

Y

V

V

A

A

R

R

G

G

Y

Y

R

K

C

L

I

T

L

L

T

T

M

M

P

P

E

E

T

T

M

M

S

S

R

I

E

E

R

R

M

K

L

L

R

K

A

A

F

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

G

G

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

Q

R

K

A

A

E

E

Q

E

L

I

V

V

K

A

E

S

H

D

P

P

D

Q

-

K

Y

Y

V

L

M

L

L

L

Q

Q

F

F

E

S

N

N

P

P

A

A

N

N

P

P

A

E

I

I

H

H

R

E

A

K

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

D

G

G

A

Q

I

V

D

D

V

V

V

F

V

I

G

S

G

G

V

V

G

G

T

T

G

G

T

T

I

L

S

T

G

G

I

V

G

T

Q

R

A

Y

L

I

K

K

P

G

R

T

R

K

P

G

S

K

L

T

Q

D

L

L

I

I

-

T

-

V

A

A

V

V

E

E

P

P

A

T

A

D

S

S

P

P

V

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

G

T

N

Y

L

D

D

A

L

T

K

V

L

V

I

D

D

E

K

V

V

Q

G

V

I

T

T

N

N

D

E

E

E

A

A

F

I

E

S

M

T

A

A

R

R

M

L

A

M

R

E

E

E

G

G

L

I

L

L

V

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

R

L

R

K

V

L

A

Q

Q

E

R

D

P

E

E

S

S

F

A

T

G

N

K

K

L

N

I

I

A

V

V

V

I

I

I

L

P

P

S

S

F

S

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

A

A

D

D

L

L

N72 (= N74) binding pyridoxal 5'-phosphate
S273 (= S266) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

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, 99% coverage: 2:308/311 of query aligns to 3:315/323 of P0ABK5

query
sites
P0ABK5

R

K

I

I

A

F

E

E

D

D

V

N

T

S

K

L

L

T

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

N

N

R

R

V

I

I

G

D

N

G

G

A

-

G

-

A

-

T

R

V

I

V

L

A

A

K

K

L

V

E

E

F

S

Y

R

N

N

P

P

A

S

N

F

S

S

V

V

K
|
K

D

C

R

R

I

I

G

G

V

A

A

N

M

M

I

I

D

W

A

D

A

A

E

E

R

K

E

R

G

G

R

V

L

L

K

K

P

P

G

G

S

V

T

E

I

L

V

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

M

Y

V

V

A

A

R

R

G

G

Y

Y

R

K

C

L

I

T

L

L

T

T

M

M

P

P

E

E

T

T

M

M

S

S

R

I

E

E

R

R

M

K

L

L

R

K

A

A

F

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

G

G

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

Q

R

K

A

A

E

E

Q

E

L

I

V

V

K

A

E

S

H

N

P

P

D

E

-

K

Y

Y

V

L

M

L

L

L

Q

Q

F

F

E

S

N

N

P

P

A

A

N

N

P

P

A

E

I

I

H

H

R

E

A

K

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

D

G

G

A

Q

I

V

D

D

V

V

V

F

V

I

G

A

G

G

V

V

G

G

T

T

G

G

T

T

I

L

S

T

G

G

I

V

G

S

Q

R

A

Y

L

I

K

K

P

G

R

T

R

K

P

G

S

K

L

T

Q

D

L

L

I

I

-

S

-

V

A

A

V

V

E

E

P

P

A

T

A

D

S

S

P

P

V

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

A

T

N

Y

L

D

D

A

L

T

K

V

L

V

V

D

D

E

K

V

V

V

I

Q

G

V

I

T

T

N

N

D

E

E

E

A

A

F

I

E

S

M

T

A

A

R

R

M

L

A

M

R

E

E

E

G

G

L

I

L

L

V

A

G

G

I

I

S

S

G

G

A

A

V

V

A

A

R

L

R

K

V

L

A

Q

Q

E

R

D

P

E

E

S

S

F

A

T

G

N

K

K

L

N

I

I

A

V

V

V

I

I

I

L

P

P

S

S

F

S

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

A

A

D

D

L

L

K42 (= K44) 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

1d6sA Crystal structure of the k41a mutant of o-acetylserine sulfhydrylase complexed in external aldimine linkage with methionine (see paper)
56% identity, 99% coverage: 2:308/311 of query aligns to 2:314/322 of 1d6sA

query
sites
1d6sA

R

K

I

I

A

Y

E

E

D

D

V

N

T

S

K

L

L

T

V

I

G

G

N

H

T

T

P

P

L

L

V

V

R

R

L

L

N

N

R

R

V

I

I

G

D

N

G

G

A

-

G

-

A

-

T

R

V

I

V

L

A

A

K

K

L

V

E

E

F

S

Y

R

N

N

P

P

A

S

N

F

S

S

V

V

K
x
A

D

C

R

R

I

I

G

G

V

A

A

N

M

M

I

I

D

W

A

D

A

A

E

E

R

K

E

R

G

G

R

V

L

L

K

K

P

P

G

G

S

V

T

E

I

L

V

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

M

Y

V

V

A

A

R

R

G

G

Y

Y

R

K

C

L

I

T

L

L

T

T

M

M

P

P

E

E

T

T

M

M

S

S

R

I

E

E

R

R

M

K

L

L

R

K

A

A

F

L

G

G

A

A

E

N

L

L

V

V

L

L

T

T

P

E

G

G

P

A

E

K

G

G

M

M

G

K

G

G

A

A

I

I

A

Q

R

K

A

A

E

E

Q

E

L

I

V

V

K

A

E

S

H

D

P

P

D

Q

-

K

Y

Y

V

L

M

L

L

L

Q

Q

Q
|
Q

F
|
F

E

S

N

N

P

P

A

A

N

N

P

P

A

E

I

I

H

H

R

E

A

K

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

D

G

G

A

Q

I

V

D

D

V

V

V

F

V

I

G

S

G

G

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

S

T

G

G

I

V

G

T

Q

R

A

Y

L

I

K

K

P

G

R

T

R

K

P

G

S

K

L

T

Q

D

L

L

I

I

-

T

-

V

A

A

V

V

E

E

P

P

A

T

A

D

S

S

P

P

V

V

L

I

S

A

G

Q

G

A

-

L

-

A

-

G

-

E

-

I

Q

K

K

P

G

G

P

P

H

H

P

K

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

V

I

P

P

G

G

T

N

Y

L

D

D

A

L

T

K

V

L

V

I

D

D

E

K

V

V

Q

G

V

I

T

T

N

N

D

E

E

E

A

A

F

I

E

S

M

T

A

A

R

R

M

L

A

M

R

E

E

E

G

G

L

I

L

L

V

A

G

G

I

I

S
|
S

S

S

G

G

A

A

V

V

A

A

R

L

R

K

V

L

A

Q

Q

E

R

D

P

E

E

S

S

F

A

T

G

N

K

K

L

N

I

I

A

V

V

V

I

I

I

L

P
|
P

S

S

F

S

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

A

A

D

D

L

L

active site: A41 (≠ K44), G228 (= G222)
binding methionine: T68 (= T71), N69 (≠ S72), N71 (= N74), T72 (= T75), Q142 (= Q144), F143 (= F145), G176 (= G178), G228 (= G222)
binding pyridoxal-5'-phosphate: N71 (= N74), G176 (= G178), T177 (= T179), G178 (= G180), T180 (= T182), G228 (= G222), S272 (= S266), P299 (= P293)

8b9wA Cysteine synthase from trypanosoma theileri with plp bound (see paper)
54% identity, 98% coverage: 3:308/311 of query aligns to 9:314/329 of 8b9wA

query
sites
8b9wA

I

V

A

A

E

P

D

S

V

V

T

D

K

A

L

L

V

I

G

G

N

N

T

T

P

P

L

A

V

V

R

Y

L

L

N

-

R

R

V

N

I

M

D

N

G

K

A

T

G

A

A

A

T

T

V

I

V

V

A

L

K

K

L

L

E

E

F

S

Y

E

N

N

P

P

A

M

N

A

S

S

V

V

K
|
K

D

D

R

R

I

L

G

A

V

Y

A

A

M

I

I

Y

D

D

A

K

A

A

E

E

R

K

E

E

G

G

R

K

L

I

K

K

P

R

G

G

-

K

S

S

T

V

I

I

V

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

M

L

V

L

A

G

A

A

A

V

R

R

G

G

Y

Y

R

K

C

V

I

I

L

I

T

T

M

M

P

P

E

D

T

S

M

M

S

S

R

M

E

E

R

R

M

S

L

L

R

R

A

I

F

F

G

G

A

A

E

E

L

L

V

I

L

L

T

T

P

P

G

A

P

S

E

L

G

G

M

M

G

K

G

G

A

A

I

V

A

A

R

M

A

A

E

N

Q

R

L

I

V

V

K

S

E

N

H

N

P

P

D

D

Y

A

V

V

M

L

L

A

Q

D

Q

Q

F

F

E

C

N

T

P

K

A

Y

N

N

P

A

A

Q

I

I

H

H

R

E

A

E

T

T

A

G

E

P

E

E

L

I

W

W

R

R

D

Q

T

T

D

K

G

G

A

H

I

V

D

D

V

C

V

F

V

V

G

A

G

G

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

L

S

T

G

G

I

V

G

A

Q

R

A

F

L

L

K

K

P

S

R

V

R

G

P

C

S

N

L

A

Q

N

L

I

I

V

A

A

V

V

E

E

P

P

A

Q

A

E

S

S

P

P

V

V

L

L

S

S

G

G

Q

R

K

P

G

G

P

P

H

H

P

R

I

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

V

V

P

P

G

E

T

V

Y

L

D

D

A

R

T

E

V

L

V

V

D

D

E

E

V

I

Q

Q

V

V

T

S

N

S

D

D

E

K

A

A

F

I

E

E

M

T

A

A

R

Q

R

K

M

L

A

S

R

R

E

M

E

D

G

G

L

I

L

F

V

C

G

G

I

F

S
|
S

S

A

G

G

A

A

A

N

V

V

A

F

A

A

R

L

R

K

V

I

A

A

Q

E

R

R

P

P

E

E

S

M

A

A

G

G

K

K

L

T

I

I

A

V

V

T

I

V

I

I

P
|
P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

Y

A

A

D

S

L

V

binding pyridoxal-5'-phosphate: K49 (= K44), N80 (= N74), G184 (= G178), T185 (= T179), G186 (= G180), T188 (= T182), G228 (= G222), S272 (= S266), P299 (= P293)

3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
51% identity, 99% coverage: 2:308/311 of query aligns to 10:317/329 of 3vbeC

query
sites
3vbeC

R

N

I

I

A

K

E

K

D

H

V

V

T

S

K

Q

L

L

V

I

G

G

N

R

T

T

P

P

L

L

V

V

R

Y

L

L

N

N

R

K

V

V

I

T

D

E

G

G

A

C

G

G

A

A

T

Y

V

V

V

A

A

V

K

K

L

Q

E

E

F

M

Y

M

N

Q

P

P

A

T

N

A

S

S

V

I

K
|
K

D

D

R

R

I

P

G

A

V

Y

A

A

M

M

I

I

D

T

A

D

A

A

E

E

R

E

E

K

G

N

R

L

L

I

K

T

P

P

G

G

-

K

S

T

T

T

I

L

V

I

E

E

P

P

T

T

S
|
S

G

G

N
|
N

T

M

G

G

I

I

A

S

L

M

A

A

M

F

V

M

A

A

A

M

R

K

G

G

Y

Y

R

K

C

M

I

V

L

L

T

T

M

M

P

P

E

S

T

Y

M

T

S

S

R

L

E

E

R

R

M

V

L

T

L

M

R

R

A

A

F

F

G

G

A

A

E

E

L

L

V

I

L

L

T

T

P

D

G

P

P

A

E

K

G

G

M

M

G

G

A

T

I

V

A

K

R

K

A

A

E

Y

Q

E

L

L

V

L

K

E

E

N

H

T

P

P

D

N

Y

A

V

H

M

M

L

L

Q

Q

F

F

E

S

N

N

P

P

A

A

N

N

P

T

A

Q

I

V

H

H

R

F

A

E

T

T

A

G

E

P

E

E

L

I

W

W

R

E

D

D

T

T

D

N

G

G

A

Q

I

V

D

D

V

I

V

F

V

V

G
x
M

G

G

V

I

G
|
G

T
x
S

G
|
G

G

G

T
|
T

I

V

S

S

G

G

I

V

G

G

Q

Q

A

Y

L

L

K

K

P

S

R

K

R

N

P

P

S

N

L

V

Q

K

L

I

I

Y

A

G

V

V

E
|
E

P

P

A

S

A

E

S
|
S

P

N

V

V

L

L

S

N

G

G

Q

K

K

P

G

G

P

P

H

H

P

H

I

I

Q

T

G
|
G

I

N

G

G

A

V

G

G

F

F

V

K

P

P

G

D

T

I

Y

L

D

D

A

L

T

D

V

V

V

M

D

E

E

K

V

V

V

L

Q

E

V

V

T

S

N

S

D

E

E

D

A

A

F

V

E

N

M

M

A

A

R

R

R

V

M

L

A

A

R

L

E

K

E

E

G

G

L

L

L

M

V

V

G

G

I

I

S
|
S

S

S

G

G

A

A

A

N

V

T

A

V

A

A

R

L

R

R

V

L

A

A

Q

Q

R

L

P

P

E

E

S

N

A

K

G

G

K

K

L

L

I

I

A

V

V

T

I

V

I

H

P
|
P

S

S

F

F

G

G

E

E

R

R

Y

Y

L

L

S

S

T

S

P

V

L

L

F

F

A

Q

D

E

L

L

active site: K52 (= K44), S81 (= S72), E212 (= E203), S216 (= S207), S275 (= S266), P302 (= P293)
binding pyridoxal-5'-phosphate: K52 (= K44), N83 (= N74), M184 (≠ G175), G187 (= G178), S188 (≠ T179), G189 (= G180), T191 (= T182), G231 (= G222), S275 (= S266), P302 (= P293)

Query Sequence

>WP_015798746.1 NCBI__GCF_000023265.1:WP_015798746.1
MRIAEDVTKLVGNTPLVRLNRVIDGAGATVVAKLEFYNPANSVKDRIGVAMIDAAEREGR
LKPGSTIVEPTSGNTGIALAMVAAARGYRCILTMPETMSRERRMLLRAFGAELVLTPGPE
GMGGAIARAEQLVKEHPDYVMLQQFENPANPAIHRATTAEELWRDTDGAIDVVVGGVGTG
GTISGIGQALKPRRPSLQLIAVEPAASPVLSGGQKGPHPIQGIGAGFVPGTYDATVVDEV
VQVTNDEAFEMARRMAREEGLLVGISSGAAVAAARRVAQRPESAGKLIAVIIPSFGERYL
STPLFADLADA

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