SitesBLAST

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)
59% identity, 95% coverage: 14:324/326 of query aligns to 3:310/310 of P9WP55

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P9WP55

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K44 (= K57) modified: N6-(pyridoxal phosphate)lysine
N74 (= N88) binding pyridoxal 5'-phosphate
GTGGT 178:182 (= GTGGT 192:196) binding pyridoxal 5'-phosphate
S266 (= S280) binding pyridoxal 5'-phosphate

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
57% identity, 94% coverage: 14:320/326 of query aligns to 3:309/310 of 4lmbA

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4lmbA

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active site: K46 (= K57), S269 (= S280)
binding cysteine: K46 (= K57), T74 (= T85), S75 (= S86), N77 (= N88), T78 (= T89), M101 (= M112), M125 (= M136), M125 (= M136), Q147 (= Q158), F148 (= F159), Q224 (= Q235), G225 (= G236), G225 (= G236), I226 (= I237), A228 (= A239)
binding pyridoxal-5'-phosphate: K46 (= K57), N77 (= N88), V180 (= V191), G181 (= G192), T182 (= T193), G183 (= G194), T185 (= T196), G225 (= G236), S269 (= S280), P296 (≠ A307)

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)
59% identity, 94% coverage: 14:319/326 of query aligns to 3:305/306 of 2q3dA

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2q3dA

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active site: K44 (= K57), S266 (= S280), P293 (≠ A307)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K57), T71 (= T85), S72 (= S86), N74 (= N88), T75 (= T89), Q144 (= Q158), V177 (= V191), G178 (= G192), T179 (= T193), G180 (= G194), T182 (= T196), G222 (= G236), I223 (= I237), S266 (= S280), P293 (≠ A307), D294 (≠ S308)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
53% identity, 98% coverage: 9:326/326 of query aligns to 8:323/323 of 4aecA

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4aecA

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L

I

D

R

D

E

E

E

A

V

active site: K54 (= K57), S277 (= S280)
binding pyridoxal-5'-phosphate: K54 (= K57), N85 (= N88), I188 (≠ V191), G189 (= G192), T190 (= T193), G191 (= G194), G192 (= G195), T193 (= T196), G233 (= G236), S277 (= S280), P304 (≠ A307)

2isqA Crystal structure of o-acetylserine sulfhydrylase from arabidopsis thaliana in complex with c-terminal peptide from arabidopsis serine acetyltransferase (see paper)
54% identity, 96% coverage: 13:326/326 of query aligns to 2:313/320 of 2isqA

query
sites
2isqA

R

R

I

I

Y

A

D

K

D

D

F

V

V

T

A

E

T

L

I

I

G

G

E

N

T

T

P

P

L

L

V

V

R

Y

L

L

S

N

R

N

L

V

G

A

A

E

E

-

A

-

G

G

L

C

A

V

A

G

E

R

L

V

L

A

A

A

K

K

L

L

E

E

M

M

F

M

N

E

P

P

L

C

S

S

V

V

K
|
K

D

D

R

R

I

I

A

G

L

F

A

S

M

M

I

I

E

S

A

D

A

A

E

E

A

K

E

K

G

G

R

L

I

I

T

K

P

P

G

G

R

E

S

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

G

G

L

L

A

A

F

F

I

T

A

A

R

K

G

G

Y

Y

R

K

L

L

I

I

L

I

T

T

M

M

P

P

A

A

N

S

M

M

S

S

A

T

E

E

R

R

K

I

L

I

F

L

A

L

F

A

Y

F

G

G

A

V

R

E

V

L

E

V

L

L

T

T

D

D

P

P

A

A

A

K

G
|
G

M
|
M

R
x
K

G

G

A

A

I

I

D

A

R

K

A

A

E

E

A

E

L

I

L

L

E

A

E

K

I

T

P

P

D

N

S

G

F

Y

T

M

P

L

A

Q

Q

Q

F

F

S

E

N

N

P

P

A

A

N

N

P

P

R

K

A

I

H

H

R

Y

L

E

R

T

T

T

A

G

E

P

E

E

I

I

W

W

R

K

D

G

T

T

G

G

S

K

V

I

D

D

G

G

L

F

I

V

A

S

G
|
G

V

I

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

T

T

G

G

I

A

A

G

G

K

V

Y

L

L

K

K

E

E

R

Q

R

N

P

A

G

N

F

V

R

K

A

L

Y

Y

A

G

V

V

E

E

P

P

A

V

G

E

S

S

P

A

V

I

L

L

S

S

G

G

A

K

P

P

G
|
G

P
|
P

H
|
H

G

K

L

I

Q
|
Q

G
|
G

I

I

G

G

A

A

G

G

F

F

L

I

P

P

D

S

T

V

L

L

D

N

A

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T

D

L

L

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I

D

D

E

E

T

V

L

V

Q

Q

V

V

T

S

D

S

D

D

E

E

A

S

L

I

A

D

M

M

S

A

R

R

R

Q

V

L

A

A

R

L

L

K

E

E

G

G

I

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P

L

C

V

G

G

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I

S
|
S

S

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G

G

A

A

L

A

S

A

A

A

V

I

Q

K

V

L

A

A

A

Q

R

R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

F

V

V

V

A

I

I

L

F

A
x
P

S

S

G

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

V

L

L

F

F

E

D

G

A

L

T

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R

D

K

E

E

A

A

active site: K44 (= K57), S267 (= S280)
binding pyridoxal-5'-phosphate: K44 (= K57), N75 (= N88), G177 (= G190), G179 (= G192), T180 (= T193), G181 (= G194), T183 (= T196), G223 (= G236), S267 (= S280), P294 (≠ A307)
binding : T72 (= T85), S73 (= S86), G74 (= G87), T76 (= T89), G122 (= G135), M123 (= M136), K124 (≠ R137), G217 (= G230), P218 (= P231), H219 (= H232), Q222 (= Q235), G223 (= G236)

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)
54% identity, 96% coverage: 13:326/326 of query aligns to 4:315/322 of P47998

query
sites
P47998

R

R

I

I

Y

A

D

K

D

D

F

V

V

T

A

E

T

L

I

I

G

G

E

N

T

T

P

P

L

L

V

V

R

Y

L

L

S

N

R

N

L

V

G

A

A

E

E

-

A

-

G

G

L

C

A

V

A

G

E

R

L

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L

A

A

A

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K

L

L

E

E

M

M

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M

N

E

P

P

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C

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S

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V

K
|
K

D

D

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R

I

I

A

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M

I

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S

A

D

A

A

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E

A

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E

K

G

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R

L

I

I

T

K

P

P

G

G

R

E

S

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

G

G

L

L

A

A

F

F

I

T

A

A

R

K

G

G

Y

Y

R

K

L

L

I

I

L

I

T

T

M

M

P

P

A

A

N

S

M

M

S

S

A

T

E

E

R

R

K

I

L

I

F

L

A

L

F

A

Y

F

G

G

A

V

R

E

V

L

E

V

L

L

T

T

D

D

P

P

A

A

A

K

G

G

M

M

R

K

G

G

A

A

I

I

D

A

R

K

A

A

E

E

A

E

L

I

L

L

E

A

E

K

I

T

P

P

D

N

S

G

F

Y

T

M

P

L

A

Q

Q
|
Q

F

F

S

E

N

N

P

P

A

A

N

N

P

P

R

K

A

I

H
|
H

R

Y

L

E

R

T

T

T

A
x
G

E

P

E

E

I

I

W

W

R

K

D

G

T

T

G

G

S

K

V

I

D

D

G

G

L

F

I

V

A

S

G

G

V

I

G
|
G

T
|
T

G
|
G

T
|
T

L

I

T

T

G

G

I

A

A

G

G

K

V

Y

L

L

K

K

E

E

R

Q

R

N

P

A

G

N

F

V

R

K

A

L

Y

Y

A

G

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V

E

E

P

P

A

V

G

E

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S

P

A

V

I

L

L

S

S

G

G

A
x
K

P

P

G

G

P

P

H
|
H

G
x
K

L

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

L

I

P

P

D

S

T

V

L

L

D

N

A

V

T

D

L

L

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I

D

D

E

E

T

V

L

V

Q

Q

V

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T

S

D

S

D

D

E

E

A

S

L

I

A

D

M

M

S

A

R

R

R

Q

V

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

C

V

G

G

I

I

S
|
S

S

S

G

G

A

A

L

A

S

A

A

A

V

I

Q

K

V

L

A

A

A

Q

R

R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

F

V

V

V

A

I

I

L

F

A

P

S

S

G

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

V

L

L

F

F

E

D

G

A

L

T

D

R

D

K

E

E

A

A

K46 (= K57) modified: N6-(pyridoxal phosphate)lysine; mutation to A: No cysteine synthase activity.
T74 (= T85) mutation to A: Strong reduction of cysteine synthase activity.; mutation to S: Reduction of cysteine synthase activity.
S75 (= S86) mutation S->A,N,T: Strong reduction of cysteine synthase activity.
N77 (= N88) binding pyridoxal 5'-phosphate; mutation to A: Reduction of cysteine synthase activity.; mutation to D: Strong reduction of cysteine synthase activity.
T78 (= T89) mutation T->A,S: Reduction of cysteine synthase activity.
Q147 (= Q158) mutation Q->A,E: Strong reduction of cysteine synthase activity.
H157 (= H168) mutation H->Q,N: Slight reduction of cysteine synthase activity.
G162 (≠ A173) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (= GTGGT 192:196) binding pyridoxal 5'-phosphate
T182 (= T193) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T196) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ A228) mutation to A: Impaired interaction with SAT1.
H221 (= H232) mutation to A: Impaired interaction with SAT1.
K222 (≠ G233) mutation to A: Impaired interaction with SAT1.
S269 (= S280) binding pyridoxal 5'-phosphate; mutation to A: Strong reduction of cysteine synthase activity.; mutation to T: Reduction of cysteine synthase activity.

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)
53% identity, 97% coverage: 10:326/326 of query aligns to 71:385/392 of P47999

query
sites
P47999

E

E

G

G

G

L

R

N

I

I

Y

A

D

D

D

N

F

A

V

A

A

Q

T

L

I

I

G

G

E

K

T

T

P

P

L

M

V

V

R

Y

L

L

S

N

R

N

L

V

G

V

A

K

E

-

A

-

G

G

L

C

A

V

A

A

E

S

L

V

L

A

A

A

K

K

L

L

E

E

M

I

F

M

N

E

P

P

L

C

S

C

S

S

V

V

K

K

D

D

R

R

I

I

A

G

L

Y

A

S

M

M

I

I

E

T

A

D

A

A

E

E

A

E

E

K

G

G

R

L

I

I

T

T

P

P

G

G

R

K

S

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

G

G

L

L

A

A

F

F

I

I

A

A

A

S

R

K

G

G

Y

Y

R

K

L

L

I

I

L

L

T

T

M

M

P

P

A

A

N

S

M

M

S

S

A

L

E

E

R

R

K

V

L

L

F

L

A

R

F

A

Y

F

G

G

A

A

R

E

V

L

E

V

L

L

T

T

D

E

P

P

A

A

A

K

G

G

M

M

R

T

G

G

A

A

I

I

D

Q

R

K

A

A

E

E

A

E

L

I

L

L

E

K

I

T

P

P

D

N

S

S

F

Y

T

M

P

L

A

Q

Q

Q

F

F

S

D

N

N

P

P

A

A

N

N

P

P

R

K

A

I

H

H

R

Y

L

E

R

T

T

T

A

G

E

P

E

E

I

I

W

W

R

E

D

D

T

T

G

R

G

G

S

K

V

I

D

D

G

I

L

L

I

V

A

A

G

G

V

I

G

G

T

T

G

G

T

T

L

I

T

T

G

G

I

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A

G

G

R

V

F

L

I

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K

E

E

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R

R

K

P

P

G

E

F

L

R

K

A

V

Y

I

A

G

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V

E

E

P

P

A

T

G

E

S

S

P

A

V

I

L

L

S

S

G

G

A

K

P

P

G

G

P

P

H

H

G

K

L

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

L

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P

P

D

K

T

N

L

L

D

D

A

L

T

A

L

I

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V

D

D

E

E

T

Y

L

I

Q

A

V

I

T

S

D

S

D

E

E

E

A

A

L

I

A

E

M

T

S

S

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K

R

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V

L

A

A

R

L

L

Q

E

E

G

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I

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P

L

C

V

G

G

I

I

S

S

G

G

A

A

L

A

S

A

A

A

V

I

Q

Q

V

V

A

A

A

K

R

R

P

P

E

E

L

N

A

A

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G

Q

K

R

L

L

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A

V

V

I

V

L

F

A

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S

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F

A

G

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E

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R

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Y

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T

P

Q

L

L

F

F

E

Q

G

S

L

I

D

R

D

E

E

E

A

C

Sites not aligning to the query:

61 modified: N-acetylalanine

1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
53% identity, 96% coverage: 13:326/326 of query aligns to 2:313/320 of 1z7yA

query
sites
1z7yA

R

R

I

I

Y

A

D

K

D

D

F

V

V

T

A

E

T

L

I

I

G

G

E

N

T

T

P

P

L

L

V

V

R

Y

L

L

S

N

R

N

L

V

G

A

A

E

E

-

A

-

G

G

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C

A

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A

G

E

R

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L

A

A

A

K

K

L

L

E

E

M

M

F

M

N

E

P

P

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C

S

S

V

V

K
x
A

D

D

R

R

I

I

A

G

L

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A

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M

M

I

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S

A

D

A

A

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E

A

K

E

K

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L

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K

P

P

G

G

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E

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S

T

V

L

L

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I

E

E

P

P

T

T

S

S

G
|
G

N
|
N

T
|
T

G

G

I

V

G

G

L

L

A

A

F

F

I

T

A

A

R

K

G

G

Y

Y

R

K

L

L

I

I

L

I

T

T

M

M

P

P

A

A

N

S

M

M

S

S

A

T

E

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R

R

K

I

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L

A

L

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A

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F

G

G

A

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R

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V

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V

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T

T

D

D

P

P

A

A

A

K

G

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M

R

K

G

G

A

A

I

I

D

A

R

K

A

A

E

E

A

E

L

I

L

L

E

A

E

K

I

T

P

P

D

N

S

G

F

Y

T

M

P

L

A

Q

Q
|
Q

F

F

S

E

N

N

P

P

A

A

N

N

P

P

R

K

A

I

H

H

R

Y

L

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R

T

T

T

A

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E

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I

I

W

W

R

K

D

G

T

T

G

G

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K

V

I

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D

G

G

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A

S

G

G

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x
I

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

T

T

G

G

I

A

A

G

G

K

V

Y

L

L

K

K

E

E

R

Q

R

N

P

A

G

N

F

V

R

K

A

L

Y

Y

A

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V

E

E

P

P

A

V

G

E

S

S

P

A

V

I

L

L

S

S

G

G

A

K

P

P

G

G

P

P

H

H

G

K

L

I

Q

Q

G
|
G

I

I

G

G

A

A

G

G

F

F

L

I

P

P

D

S

T

V

L

L

D

N

A

V

T

D

L

L

V

I

D

D

E

E

T

V

L

V

Q

Q

V

V

T

S

D

S

D

D

E

E

A

S

L

I

A

D

M

M

S

A

R

R

R

Q

V

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

C

V

G

G

I

I

S
|
S

S

S

G

G

A

A

L

A

S

A

A

A

V

I

Q

K

V

L

A

A

A

Q

R

R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

F

V

V

V

A

I

I

L

F

A
x
P

S
|
S

G

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

V

L

L

F

F

E

D

G

A

L

T

D

R

D

K

E

E

A

A

active site: A44 (≠ K57), S267 (= S280)
binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G87), N75 (= N88), T76 (= T89), Q145 (= Q158), I178 (≠ V191), G179 (= G192), T180 (= T193), G181 (= G194), T183 (= T196), G223 (= G236), S267 (= S280), P294 (≠ A307), S295 (= S308)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
58% identity, 92% coverage: 14:314/326 of query aligns to 3:300/300 of 3zeiA

query
sites
3zeiA

I

I

Y

A

D

E

D

D

F

I

V

T

A

Q

T

L

I

I

G

G

E

R

T

T

P

P

L

L

V

V

R

R

L

L

S

R

R

R

L

V

G

-

A

-

E

T

A

D

G

G

L

A

A

V

A

A

E

D

L

I

L

V

A

A

K

K

L

L

E

E

M

F

F

F

N

N

P

P

L

A

S

N

S

S

V

V

K
|
K

D

D

R

R

I

I

A

G

L

V

A

A

M

M

I

L

E

Q

A

A

E

E

A

Q

E

A

G

G

R

L

I

I

T

K

P

P

G

D

R

-

S

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

G

A

L

L

A

A

F

M

I

V

A

C

A

A

R

R

G

G

Y

Y

R

R

L

C

I

V

L

L

T

T

M

M

P

P

A

E

N

T

M

M

S

S

A

L

E

E

R

R

K

M

L

L

F

L

A

R

F

A

Y

Y

G

G

A

A

R

E

V

L

E

I

L

L

T

T

D

P

P

G

A

A

A

D

G

G

M

M

R

S

G

G

A

A

I
|
I

D

A

R

K

A

A

E

E

A

E

L

L

L

A

E

K

E

T

I

D

P

Q

D

R

S

Y

F

F

T

V

P

P

A

Q

Q
|
Q

F
|
F

S

E

N

N

P

P

A

A

N

N

P

P

R

A

A

I

H

H

R

R

L

V

R

T

T

T

A

A

E

E

I

V

W

W

R

R

D

D

T

T

G

D

G

G

S

K

V

V

D

D

G

I

L

V

I

V

A

A

G

G

V
|
V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

L

I

T

T

G

G

I

V

A

A

G

Q

V

V

L

I

K

K

E

E

R

R

R

K

P

P

G

S

F

A

R

R

A

F

Y

V

A

A

V

V

E

E

P

P

A

A

G

A

S

S

P

P

V

V

L

L

S

S

G

G

A

Q

P
x
K

G

G

P

P

H

H

G

P

L

I

Q

Q

G
|
G

I

I

G

G

A
|
A

G

G

F
|
F

L

V

P

P

D

P

T

V

L

L

D

D

A

Q

T

D

L

L

V

V

D

D

E

E

T

I

L

I

Q

T

V

V

T

G

D

N

D

E

E

D

A

A

L

L

A

N

M

V

S

A

R

R

V

L

A

A

R

R

L

E

E

E

G

G

I

L

P

L

C

V

G

G

I

I

S
|
S

S

S

G

G

A

A

L

T

S

V

A

A

V

L

Q

Q

V

V

A

A

A

R

R

R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

I

V

V

I

V

L

L

A
x
P

S
x
D

G

F

A

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K57), S266 (= S280), P293 (≠ A307)
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 (= T85), S72 (= S86), I126 (= I140), Q144 (= Q158), F145 (= F159), K215 (≠ P229), G222 (= G236), A225 (= A239), F227 (= F241)
binding pyridoxal-5'-phosphate: K44 (= K57), N74 (= N88), V177 (= V191), G178 (= G192), T179 (= T193), G180 (= G194), T182 (= T196), G222 (= G236), S266 (= S280), P293 (≠ A307), D294 (≠ S308)

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)
58% identity, 92% coverage: 14:314/326 of query aligns to 3:300/300 of 2q3cA

query
sites
2q3cA

I

I

Y

A

D

E

D

D

F

I

V

T

A

Q

T

L

I

I

G

G

E

R

T

T

P

P

L

L

V

V

R

R

L

L

S

R

R

R

L

V

G

-

A

-

E

T

A

D

G

G

L

A

A

V

A

A

E

D

L

I

L

V

A

A

K

K

L

L

E

E

M

F

F

F

N

N

P

P

L

A

S

N

S

S

V

V

K
|
K

D

D

R

R

I

I

A

G

L

V

A

A

M

M

I

L

E

Q

A

A

E

E

A

Q

E

A

G

G

R

L

I

I

T

K

P

P

G

D

R

-

S

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

G

A

L

L

A

A

F

M

I

V

A

C

A

A

R

R

G

G

Y

Y

R

R

L

C

I

V

L

L

T

T

M

M

P

P

A

E

N

T

M

M

S

S

A

L

E

E

R

R

K

M

L

L

F

L

A

R

F

A

Y

Y

G

G

A

A

R

E

V

L

E

I

L

L

T

T

D

P

P

G

A

A

A

D

G

G

M
|
M

R

S

G

G

A

A

I

I

D

A

R

K

A

A

E

E

A

E

L

L

L

A

E

K

E

T

I

D

P

Q

D

R

S

Y

F

F

T

V

P

P

A

Q

Q
|
Q

F

F

S

E

N

N

P

P

A

A

N

N

P

P

R

A

A

I

H

H

R

R

L

V

R

T

T

T

A

A

E

E

I

V

W

W

R

R

D

D

T

T

G

D

G

G

S

K

V

V

D

D

G

I

L

V

I

V

A

A

G

G

V

V

G

G

T

T

G

G

T

T

L

I

T

T

G

G

I

V

A

A

G

Q

V

V

L

I

K

K

E

E

R

R

R

K

P

P

G

S

F

A

R

R

A

F

Y

V

A

A

V

V

E

E

P

P

A

A

G

A

S

S

P

P

V

V

L

L

S

S

G

G

A

Q

P
x
K

G

G

P

P

H

H

G

P

L

I

Q

Q

G
|
G

I

I

G

G

A
|
A

G

G

F

F

L

V

P

P

D

P

T

V

L

L

D

D

A

Q

T

D

L

L

V

V

D

D

E

E

T

I

L

I

Q

T

V

V

T

G

D

N

D

E

E

D

A

A

L

L

A

N

M

V

S

A

R

R

V

L

A

A

R

R

L

E

E

E

G

G

I

L

P

L

C

V

G

G

I

I

S
|
S

S

S

G

G

A

A

L

T

S

V

A

A

V

L

Q

Q

V

V

A

A

A

R

R

R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

I

V

V

I

V

L

L

A
x
P

S

D

G

F

A

G

E

E

R

R

Y

Y

L

L

active site: K44 (= K57), S266 (= S280), P293 (≠ A307)
binding : T71 (= T85), S72 (= S86), G73 (= G87), T75 (= T89), M122 (= M136), Q144 (= Q158), K215 (≠ P229), G222 (= G236), A225 (= A239)

7n2tA O-acetylserine sulfhydrylase from citrullus vulgaris in the internal aldimine state, with citrate bound (see paper)
55% identity, 95% coverage: 14:322/326 of query aligns to 3:309/309 of 7n2tA

query
sites
7n2tA

I

I

Y

A

D

K

D

D

F

V

V

T

A

E

T

L

I

I

G

G

E

N

T

T

P

P

L

L

V

V

R

Y

L

L

S

N

R

R

L

V

G

-

A

-

E

V

A

D

G

G

L

C

A

V

A

A

E

R

L

V

L

A

A

A

K

K

L

L

E

E

M

M

F

M

N

E

P

P

L

C

S

S

V

V

K

K

D

D

R

R

I

I

A

G

L

Y

A

S

M

M

I

I

E

S

A

D

A

A

E

E

A

N

E

K

G

G

R

L

I

I

T

T

P

P

G

G

R

E

S

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

G

G

L

L

A

A

F

F

I

I

A

A

R

K

G

G

Y

Y

R

R

L

L

I

I

L

I

T

C

M

M

P

P

A

A

N

S

M

M

S

S

A

L

E

E

R

R

K

T

L

I

F

L

A

R

F

A

Y

F

G

G

A

A

R

E

V

L

E

V

L

L

T

T

D

D

P

P

A

A

A

R

G

G

M

M

R

K

G

G

A

A

I

V

D

Q

R

K

A

A

E

E

A

E

L

I

L

K

E

A

E

K

I

T

P

P

D

N

S

S

F

Y

T

I

P

L

A

Q

Q

Q

F

F

S

E

N

N

P

P

A

A

N

N

P

P

R

K

A

I

H

H

R

Y

L

E

R

T

T

T

A

G

E

P

E

E

I

I

W

W

R

R

D

G

T

S

G

G

S

K

V

I

D

D

G

A

L

L

I

V

A

S

G

G

V

I

G

G

T

T

G

G

T

T

L

V

T

T

G

G

I

A

A

G

G

K

V

Y

L

L

K

K

E

E

R

Q

R

N

P

P

G

N

F

I

R

K

A

L

Y

Y

A

G

V

V

E

E

P

P

A

V

G

E

S

S

P

A

V

I

L

L

S

S

G

G

A

K

P

P

G

G

P

P

H

H

G

K

L

I

Q

Q

G

G

I

I

G

G

A

A

G

G

F

F

L

I

P

P

D

G

T

V

L

L

D

D

A

V

T

N

L

L

V

L

D

D

E

E

T

V

L

I

Q

Q

V

V

T

S

D

S

D

E

E

E

A

S

L

I

A

E

M

T

S

A

R

K

R

L

V

L

A

A

R

L

L

K

E

E

G

G

I

L

P

L

C

V

G

G

I

I

S

S

G

G

A

A

L

A

S

A

A

A

V

I

Q
x
R

V

I

A

A

A

K

R
|
R

P

P

E

E

L

N

A

A

G

G

Q

K

R

L

L

I

V

V

V

A

I

V

L

F

A

P

S

S

G

F

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

V

L

L

F

F

E

E

G

S

L

V

binding phosphate ion: R277 (≠ Q290), R281 (= R294)

Q93244 Cysteine synthase 1; O-acetylserine (thiol)-lyase 1; OAS-TL; EC 2.5.1.47 from Caenorhabditis elegans (see 2 papers)
52% identity, 96% coverage: 14:326/326 of query aligns to 7:317/341 of Q93244

query
sites
Q93244

I

I

Y

G

D

E

D

N

F

A

V

A

A

A

T

L

I

I

G

G

E

N

T

T

P

P

L

M

V

V

R

Y

L

I

S

N

R

K

L

L

G

-

A

-

E

T

A

K

G

G

L

L

A

P

A

G

E

T

L

V

L

A

A

V

K

K

L

I

E

E

M

Y

F

M

N

N

P

P

L

A

S

G

S

S

V

V

K

K

D

D

R

R

I

I

A

G

L

A

A

A

M

M

I

L

E

A

A

A

E

E

A

K

E

D

G

G

R

T

I

V

T

I

P

P

G

G

R

V

S

T

T

T

L

L

I

I

E

E

P
|
P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

G

A

L

L

A

A

F

F

I

V

A
|
A

A

A

R

K

G

G

Y

Y

R

R

L

C

I

I

L

V

T

T

M

M

P

P

A

A

N

S

M

M

S

S

A

G

E

E

R

R

K

T

L

L

F

L

A

K

F

A

Y

Y

G

G

A

S

R

E

V

V

E

V

L

L

T

T

D

D

P

P

A

A

A

K

G

G

M

M

R

K

G

G

A

A

I

I

D

D

R

M

A

A

E

N

A

Q

L

L

L

K

E

E

E

N

I

I

P

P

D

G

S
|
S

F

I

T

I

P

L

A

A

Q

Q

F

F

S

D

N

N

P

P

A

N

N

N

P

P

R

L

A

V

H

H

R

Y

L

Q

R

T

T

T

A

G

E

P

E

E

I

I

W

W

R

R

D

Q

T

T

G

K

G

G

S

T

V

V

D

D

G

A

L

V

I

V

A

F

G
|
G

V

V

G
|
G

T

T

G

G

T

T

L

I

T

T

G

G

I

V

A

G

G

R

V

Y

L

L

K

Q

E

E

R

Q

R

N

P

P

G

G

F

V

R

R

A

V

Y

F

A

A

V

V

E

E

P

P

A

E

G

E

S

S

P

A

V

I

L

L

S

S

G

G

G

R

A

P

P

A

G

G

P

P

H

H

G

K

L

I

Q

Q

G

G

I

I

G
|
G

A

A

G

G

F

F

L

A

P

P

D

A

T

V

L

L

D

D

A

T

T

K

L

I

V

Y

D

E

E

D

T

V

L

I

Q

R

V

I

T

H

D

S

D

D

E

E

A

A

L

I

A

V

M

M

S

A

R

Q

R
|
R

V

L

A

S

R

Y

L

E

E

E

G

G

I

L

P

L

C

G

G

G

I

I

S

S

S
|
S

G

G

A

A

A

N

L

V

S

A

A

A

V

L

Q

Q

V

L

A

A

R

R

P

P

E

E

L

M

A

A

G

G

Q

K

R

L

L

I

V

V

V
x
T

I

C

L

L

A

P

S

S

G

C

A

G

E

E

R

R

Y

Y

L

M

S

T

T

S

P

P

L

L

F

Y

E

T

G

D

L

I

D

R

D

E

E

S

A

A

P75 (= P84) mutation to L: In n5537; severe loss of protein stability.
A88 (= A97) mutation to V: In n5522; severe loss of protein stability.
S144 (= S153) mutation to F: In mr26; susceptible to high levels of hydrogen sulfide.
G181 (= G190) mutation to E: In n5521 and mr23; severe loss of protein stability. Susceptible to high levels of hydrogen sulfide.
G183 (= G192) mutation to R: In n5515; severe loss of protein stability.
G229 (= G238) mutation to E: In mr33; susceptible to high levels of hydrogen sulfide.
R259 (= R268) mutation to K: In n5519; no loss of protein stability. No effect on enzyme activity.
S272 (= S281) mutation to F: In mr29; susceptible to high levels of hydrogen sulfide.
T295 (≠ V304) mutation to I: In mr39; susceptible to high levels of hydrogen sulfide.

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
56% identity, 95% coverage: 14:322/326 of query aligns to 4:309/310 of 5xoqA

query
sites
5xoqA

I

I

Y

F

D

K

D

D

F

N

V

S

A

E

T

S

I

I

G

G

E

R

T

T

P

P

L

L

V

V

R

Q

L

I

S

N

R

R

L

L

G

-

A

-

E

T

A

A

G

G

L

L

A

S

E

R

L

V

L

L

A

A

K

K

L

I

E

E

M

G

F

R

N

N

P

P

L

A

S

Y

S

S

V

V

K

K

D

C

R

R

I

I

A

G

L

A

A

A

M

M

I

I

E

W

A

D

A

A

E

E

A

Q

E

S

G

G

R

K

I

L

T

K

P

P

G

G

R

M

S

H

T

-

L

V

I

V

E

E

P

P

T
|
T

S
|
S

G
|
G

N

N

T
|
T

G

G

I

I

G

A

L

L

A

A

F

F

I

V

A

C

A

A

R

R

G

G

Y

Y

R

K

L

L

I

T

L

L

T

T

M

M

P

P

A

E

N

T

M

M

S

S

A

I

E

E

R

R

K

M

L

M

F

L

A

K

F

S

Y

F

G

G

A

A

R

D

V

L

E

V

L

L

T

T

D

P

P

G

A

A

A

D

G

G

M
|
M

R

K

G

G

A

A

I

I

D

S

R

K

A

A

E

E

A

E

L

L

L

A

E

A

E

Q

I

-

P

P

D

G

S

W

F

F

T

I

P

P

A

Q

Q
|
Q

F

F

S

K

N

N

P

P

A

A

N

N

P

P

R

A

A

I

H

H

R

V

L

K

R

T

T

T

A

G

E

P

E

E

I

I

W

W

R

N

D

D

T

T

G

E

G

G

S

Q

V

V

D

D

G

V

L

F

I

V

A

A

G

G

V

V

G

G

T

T

G

G

T

T

L

I

T

T

G

G

I

V

A

A

G

R

V

F

L

L

K

K

-

H

E

E

R

K

P

H

G

P

F

V

R

H

A

V

Y

V

A

A

V

V

E

E

P

P

A

A

G

A

S

S

P

P

V

V

L

L

S

A

G

G

A

P

P

A

G

G

P
x
R

H
|
H

G

K

L

I

Q
|
Q

G
|
G

I

I

G

G

A
|
A

G

G

F

F

L

V

P

P

D

D

T

T

L

F

D

D

A

R

T

S

L

V

V

V

D

D

E

E

T

I

L

L

Q

S

V

V

T

T

D

D

E

E

A

A

L

I

A

E

M

T

S

A

R

R

R

K

V

L

A

A

R

M

L

E

E

E

G

G

I

I

P

S

C

C

G

G

I

I

S

S

S

C

G

G

A

A

L

M

S

A

A

G

A

A

V

L

Q

K

V

V

A

A

R

R

P

P

E

E

L

F

A

A

G

G

Q

K

R

T

L

I

V

V

V

T

I

V

L

L

A

P

S

D

G

A

A

G

E

E

R

R

Y

Y

L

L

S

S

T

T

P

A

L

L

F

F

E

E

G

N

L

L

binding : T72 (= T85), S73 (= S86), G74 (= G87), T76 (= T89), M123 (= M136), Q144 (= Q158), R218 (≠ P231), H219 (= H232), Q222 (= Q235), G223 (= G236), A226 (= A239)

8b9yC Cysteine synthase from trypanosoma cruzi with plp and oas (see paper)
51% identity, 94% coverage: 20:325/326 of query aligns to 16:318/330 of 8b9yC

query
sites
8b9yC

A

A

T

L

I

I

G

G

E

E

T

T