SitesBLAST

G85 (= G12) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T14) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
L101 (≠ R26) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
K102 (≠ E27) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
C109 (≠ L34) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P39) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
K119 (= K44) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ Y50) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
M126 (= M51) to V: in CBSD; loss of activity
E131 (= E56) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G64) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ V68) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E69) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G73) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N74) binding pyridoxal 5'-phosphate
L154 (≠ I79) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A80) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
C165 (≠ V90) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
M173 (≠ F98) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
E176 (= E101) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
V180 (≠ L105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (= T116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ L133) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ E148) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N150) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
A231 (= A153) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ L156) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
GTGGT 256:260 (≠ GSGGT 178:182) binding pyridoxal 5'-phosphate
T257 (≠ S179) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (= T184) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
R266 (≠ Q188) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K191) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ N194) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ I197) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
I278 (= I200) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
D281 (= D203) to N: in CBSD; loss of activity
A288 (≠ G210) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ G218) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
G305 (= G221) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G223) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
V320 (= V236) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D237) to V: in CBSD; loss of activity
R336 (= R252) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
L338 (= L254) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
G347 (= G263) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S265) binding pyridoxal 5'-phosphate; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
T353 (≠ A269) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (vs. gap) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D291) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ D294) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
K384 (= K299) to E: in CBSD; severe form; dbSNP:rs121964967

Sites not aligning to the query:

18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
52 binding axial binding residue
58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
69 A → P: in dbSNP:rs17849313
78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
45% identity, 97% coverage: 6:299/303 of query aligns to 39:344/500 of 7qgtB

query
sites
7qgtB

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binding protoporphyrin ix containing fe: A186 (≠ E148), P189 (= P151), L190 (≠ K152), Y193 (= Y155), R226 (≠ Q188)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (≠ A72), N109 (= N74), T110 (= T75), Q182 (= Q144), G216 (= G178), T217 (≠ S179), G218 (= G180), T220 (= T182), G265 (= G221), S309 (= S265), P335 (= P290), D336 (= D291)

Sites not aligning to the query:

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

8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
45% identity, 97% coverage: 6:299/303 of query aligns to 38:343/507 of 8s5hA

query
sites
8s5hA

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binding protoporphyrin ix containing fe: A185 (≠ E148), Y192 (= Y155), R225 (≠ Q188)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 10, 11, 17, 22, 23, 24

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)
44% identity, 100% coverage: 1:302/303 of query aligns to 1:305/310 of P9WP55

query
sites
P9WP55

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N

N

P

P

K

A

A

I

H

H

Y

R

L

V

T

T

G

A

P

E

E

E

I

V

Y

W

M

R

D

D

M

T

E

D

G

G

N

K

I

V

D

D

Y

I

L

V

V

V

A

A

G

G

A

V

G
|
G

S
x
T

G
|
G

T
|
T

F

I

T

T

G

G

V

V

A

A

Q

Q

Y

V

L

I

K

K

E

E

K

R

N

K

K

P

N

S

I

A

K

R

S

F

I

V

L

A

V

V

D

E

P

P

E

A

G

A

S

S

-

P

T

V

M

L

G

S

G

G

T

Q

E

K

G

G

C

P

Y

H

G

P

I

I

E

Q

G

G

I

I

G

G

N

A

N

G

F

F

I

V

P

P

E

P

T

V

M

L

D

D

M

Q

G

D

L

L

V

V

D

D

K

E

I

I

K

T

V

V

N

G

D

N

E

E

E

D

A

A

F

L

H

N

M

V

V

A

R

R

K

R

L

L

A

A

E

R

K

E

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

T

V

V

G

A

A

A

L

L

K

Q

L

V

A

A

Q

R

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

V

F

L

P

P

D

D

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

P

I

L

Y

F

K44 (= K44) modified: N6-(pyridoxal phosphate)lysine
N74 (= N74) binding pyridoxal 5'-phosphate
GTGGT 178:182 (≠ GSGGT 178:182) binding pyridoxal 5'-phosphate
S266 (= S265) 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)
44% identity, 100% coverage: 1:302/303 of query aligns to 1:305/306 of 2q3dA

query
sites
2q3dA

M

M

V

S

Y

I

Y

A

N

E

D

D

I

I

K

T

E

Q

M

L

V

I

G

G

N

R

T

T

P

P

I

L

L

V

K

R

L

L

N

R

L

V

N

T

V

D

K

G

R

A

E

V

I

A

G

D

I

I

F

V

A

A

K

K

L

L

E

E

S

F

F

F

N

N

P

P

G

A

G

N

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

V

Y

A

M

M

I

L

D

Q

S

A

A

A

E

E

K

Q

K

A

G

G

L

L

L

I

N

K

K

P

G

D

Y

T

T

I

I

I

V

L

E

E

A

P

T
|
T

A
x
S

G

G

N
|
N

T
|
T

G

G

L

I

G

A

I

L

A

A

L

M

G

V

A

C

L

A

N

A

R

R

G

G

Y

Y

K

R

V

C

I

V

F

L

V

T

V

M

P

P

E

E

K

T

F

M

S

S

Q

L

E

E

K

R

Q

R

I

M

L

L

M

L

K

R

A

A

L

Y

G

G

A

A

E

E

I

L

I

I

N

L

T

T

P

P

K

G

E

A

E

D

G

G

M

M

L

S

G

G

A

A

I

I

E

A

K

K

S

A

Q

E

E

E

L

L

L

A

R

K

D

T

I

D

P

Q

N

R

S

Y

I

F

S

V

L

P

K

Q

Q
|
Q

F

F

E

E

N

N

E

P

D

A

N

N

P

P

K

A

A

I

H

H

Y

R

L

V

T

T

G

A

P

E

E

E

I

V

Y

W

M

R

D

D

M

T

E

D

G

G

N

K

I

V

D

D

Y

I

L

V

V

V

A

A

G

G

A
x
V

G
|
G

S
x
T

G
|
G

G

G

T
|
T

F

I

T

T

G

G

V

V

A

A

Q

Q

Y

V

L

I

K

K

E

E

K

R

N

K

K

P

N

S

I

A

K

R

S

F

I

V

L

A

V

V

D

E

P

P

E

A

G

A

S

S

-

P

T

V

M

L

G

S

G

G

T

Q

E

K

G

G

C

P

Y

H

G

P

I

I

E

Q

G
|
G

I
|
I

G

G

N

A

N

G

F

F

I

V

P

P

E

P

T

V

M

L

D

D

M

Q

G

D

L

L

V

V

D

D

K

E

I

I

K

T

V

V

N

G

D

N

E

E

E

D

A

A

F

L

H

N

M

V

V

A

R

R

K

R

L

L

A

A

E

R

K

E

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

T

V

V

G

A

A

A

L

L

K

Q

L

V

A

A

Q

R

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

V

F

L

P
|
P

D
|
D

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

P

I

L

Y

F

active site: K44 (= K44), S266 (= S265), P293 (= P290)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K44), T71 (= T71), S72 (≠ A72), N74 (= N74), T75 (= T75), Q144 (= Q144), V177 (≠ A177), G178 (= G178), T179 (≠ S179), G180 (= G180), T182 (= T182), G222 (= G221), I223 (= I222), S266 (= S265), P293 (= P290), D294 (= D291)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
44% identity, 98% coverage: 1:297/303 of query aligns to 1:300/300 of 3zeiA

query
sites
3zeiA

M

M

V

S

Y

I

Y

A

N

E

D

D

I

I

K

T

E

Q

M

L

V

I

G

G

N

R

T

T

P

P

I

L

L

V

K

R

L

L

N

R

L

V

N

T

V

D

K

G

R

A

E

V

I

A

G

D

I

I

F

V

A

A

K

K

L

L

E

E

S

F

F

F

N

N

P

P

G

A

G

N

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

V

Y

A

M

M

I

L

D

Q

S

A

A

A

E

E

K

Q

K

A

G

G

L

L

L

I

N

K

K

P

G

D

Y

T

T

I

I

I

V

L

E

E

A

P

T
|
T

A
x
S

G

G

N
|
N

T

T

G

G

L

I

G

A

I

L

A

A

L

M

G

V

A

C

L

A

N

A

R

R

G

G

Y

Y

K

R

V

C

I

V

F

L

V

T

V

M

P

P

E

E

K

T

F

M

S

S

Q

L

E

E

K

R

Q

R

I

M

L

L

M

L

K

R

A

A

L

Y

G

G

A

A

E

E

I

L

I

I

N

L

T

T

P

P

K

G

E

A

E

D

G

G

M

M

L

S

G

G

A

A

I
|
I

E

A

K

K

S

A

Q

E

E

E

L

L

L

A

R

K

D

T

I

D

P

Q

N

R

S

Y

I

F

S

V

L

P

K

Q

Q
|
Q

F
|
F

E

E

N

N

E

P

D

A

N

N

P

P

K

A

A

I

H

H

Y

R

L

V

T

T

G

A

P

E

E

E

I

V

Y

W

M

R

D

D

M

T

E

D

G

G

N

K

I

V

D

D

Y

I

L

V

V

V

A

A

G

G

A
x
V

G
|
G

S
x
T

G
|
G

G

G

T
|
T

F

I

T

T

G

G

V

V

A

A

Q

Q

Y

V

L

I

K

K

E

E

K

R

N

K

K

P

N

S

I

A

K

R

S

F

I

V

L

A

V

V

D

E

P

P

E

A

G

A

S

S

-

P

T

V

M

L

G

S

G

G

T

Q

E
x
K

G

G

C

P

Y

H

G

P

I

I

E

Q

G
|
G

I

I

G

G

N
x
A

N

G

F
|
F

I

V

P

P

E

P

T

V

M

L

D

D

M

Q

G

D

L

L

V

V

D

D

K

E

I

I

K

T

V

V

N

G

D

N

E

E

E

D

A

A

F

L

H

N

M

V

V

A

R

R

K

R

L

L

A

A

E

R

K

E

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

T

V

V

G

A

A

A

L

L

K

Q

L

V

A

A

Q

R

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

V

F

L

P
|
P

D
|
D

R

F

G

G

D

E

R

R

Y

Y

F

L

active site: K44 (= K44), S266 (= S265), P293 (= P290)
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 (≠ A72), I126 (= I126), Q144 (= Q144), F145 (= F145), K215 (≠ E214), G222 (= G221), A225 (≠ N224), F227 (= F226)
binding pyridoxal-5'-phosphate: K44 (= K44), N74 (= N74), V177 (≠ A177), G178 (= G178), T179 (≠ S179), G180 (= G180), T182 (= T182), G222 (= G221), S266 (= S265), P293 (= P290), D294 (= D291)

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)
44% identity, 98% coverage: 1:297/303 of query aligns to 1:300/300 of 2q3cA

query
sites
2q3cA

M

M

V

S

Y

I

Y

A

N

E

D

D

I

I

K

T

E

Q

M

L

V

I

G

G

N

R

T

T

P

P

I

L

L

V

K

R

L

L

N

R

L

V

N

T

V

D

K

G

R

A

E

V

I

A

G

D

I

I

F

V

A

A

K

K

L

L

E

E

S

F

F

F

N

N

P

P

G

A

G

N

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

V

Y

A

M

M

I

L

D

Q

S

A

A

A

E

E

K

Q

K

A

G

G

L

L

L

I

N

K

K

P

G

D

Y

T

T

I

I

I

V

L

E

E

A

P

T
|
T

A
x
S

G
|
G

N

N

T
|
T

G

G

L

I

G

A

I

L

A

A

L

M

G

V

A

C

L

A

N

A

R

R

G

G

Y

Y

K

R

V

C

I

V

F

L

V

T

V

M

P

P

E

E

K

T

F

M

S

S

Q

L

E

E

K

R

Q

R

I

M

L

L

M

L

K

R

A

A

L

Y

G

G

A

A

E

E

I

L

I

I

N

L

T

T

P

P

K

G

E

A

E

D

G

G

M
|
M

L

S

G

G

A

A

I

I

E

A

K

K

S

A

Q

E

E

E

L

L

L

A

R

K

D

T

I

D

P

Q

N

R

S

Y

I

F

S

V

L

P

K

Q

Q
|
Q

F

F

E

E

N

N

E

P

D

A

N

N

P

P

K

A

A

I

H

H

Y

R

L

V

T

T

G

A

P

E

E

E

I

V

Y

W

M

R

D

D

M

T

E

D

G

G

N

K

I

V

D

D

Y

I

L

V

V

V

A

A

G

G

A

V

G

G

S

T

G

G

T

T

F

I

T

T

G

G

V

V

A

A

Q

Q

Y

V

L

I

K

K

E

E

K

R

N

K

K

P

N

S

I

A

K

R

S

F

I

V

L

A

V

V

D

E

P

P

E

A

G

A

S

S

-

P

T

V

M

L

G

S

G

G

T

Q

E
x
K

G

G

C

P

Y

H

G

P

I

I

E

Q

G
|
G

I

I

G

G

N
x
A

N

G

F

F

I

V

P

P

E

P

T

V

M

L

D

D

M

Q

G

D

L

L

V

V

D

D

K

E

I

I

K

T

V

V

N

G

D

N

E

E

E

D

A

A

F

L

H

N

M

V

V

A

R

R

K

R

L

L

A

A

E

R

K

E

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

T

V

V

G

A

A

A

L

L

K

Q

L

V

A

A

Q

R

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

V

F

L

P
|
P

D

D

R

F

G

G

D

E

R

R

Y

Y

F

L

active site: K44 (= K44), S266 (= S265), P293 (= P290)
binding : T71 (= T71), S72 (≠ A72), G73 (= G73), T75 (= T75), M122 (= M122), Q144 (= Q144), K215 (≠ E214), G222 (= G221), A225 (≠ N224)

4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
45% identity, 100% coverage: 1:303/303 of query aligns to 1:309/318 of 4lmaA

query
sites
4lmaA

M

M

V

R

Y

I

Y

A

N

H

D

D

I

V

K

T

E

E

M

L

V

V

G

G

N

R

T

T

P

P

I

L

L

V

K

Q

L

L

N

N

N

R

L

I

-

P

N

Q

V

A

K

E

R

G

E

C

I

L

G

G

-

R

I

I

F

V

A

M

K

K

L

L

E

E

S

G

F

M

N

N

P

P

G

A

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

T

Y

H

M

M

I

I

D

N

S

S

A

A

E

E

K

K

K

A

G

G

L

L

L

I

N

N

K

P

G

E

Y

T

T

T

I

V

-

L

V

V

E

E

A

P

T

T

A

S

G

G

N
|
N

T

T

G

G

L

I

G

A

I

L

A

A

L

M

G

T

A

A

L

A

N

A

R

K

G

G

Y

Y

K

R

V

L

I

I

F

L

V

T

V

M

P

P

E

E

K

T

F

M

S

S

Q

L

E

E

K

R

Q

R

I

A

L

M

M

L

K

K

A

A

L

Y

G

G

A

A

E

T

I

L

I

E

N

L

T

T

P

P

K

G

E

S

E

Q

G

G

M

M

L

K

G

G

A

A

I

I

E

L

K

R

S

A

Q

Q

E

Q

L

I

L

V

R

D

D

S

I

I

P

P

N

G

S

A

I

Y

S

M

L

L

K

Q

Q

Q

F

F

E

R

N

N

E

P

D

S

N

N

P

P

K

E

A

I

H

H

Y

R

L

L

T

T

G

A

P

E

E

E

I

I

Y

W

M

Q

D

D

M

T

E

E

G

G

N

Q

I

V

D

D

Y

F

L

I

V

V

A

A

G

G

A

V

G
|
G

S
x
T

G
|
G

G

G

T
|
T

F

I

T

T

G

G

V

V

A

A

Q

E

Y

V

L

I

K

K

E

S

K

R

N

K

K

P

N

S

I

F

K

Q

S

V

I

V

L

A

V

V

D

E

P

P

E

F

G

N

S

S

-

P

T

V

M

I

G

S

G

G

T

N

E

P

G

G

C

P

Y

H

G

K

I

I

E

Q

G
|
G

I

I

G

G

N

A

N

G

F

F

I

I

P

P

E

E

T

V

M

L

D

R

M

T

G

D

L

L

V

I

D

D

K

E

I

V

I

I

K

T

V

V

N

S

D

D

E

E

A

A

F

F

H

Q

M

F

V

G

R

R

K

R

L

L

A

A

E

K

K

E

E

E

G

G

L

L

I

L

V

S

G

G

S

I

S
|
S

S

S

G

G

A

A

A

N

L

L

V

C

G

A

A

A

L

I

K

Q

L

L

A

A

Q

Q

S

R

I

P

D

E

K

N

G

E

N

G

-

K

-

L

I

I

V

V

V

I

F

Q

P
|
P

D

S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

L

I

M

Y

F

H

Q

active site: K46 (= K44), S269 (= S265)
binding pyridoxal-5'-phosphate: K46 (= K44), N77 (= N74), G181 (= G178), T182 (≠ S179), G183 (= G180), T185 (= T182), G225 (= G221), S269 (= S265), P296 (= P290)

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)
45% identity, 99% coverage: 5:303/303 of query aligns to 77:379/392 of P47999

query
sites
P47999

N

D

D

N

I

A

K

A

E

Q

M

L

V

I

G

G

N

K

T

T

P

P

I

M

L

V

K

Y

L

L

N

N

L

V

N

V

V

K

K

G

R

C

E

V

I

A

G

S

I

V

F

A

A

A

K

K

L

L

E

E

S

I

F

M

N

E

P

P

G

C

S

S

V

V

K

K

D

D

R

R

I

I

G

G

L

Y

Y

S

M

M

I

I

D

T

S

D

A

A

E

E

K

E

K

K

G

G

L

L

L

I

N

T

K

P

G

G

Y

K

T

S

I

V

-

L

V

V

E

E

A

S

T

T

A

S

G

G

N

N

T

T

G

G

L

I

G

G

I

L

A

A

L

F

G

I

A

A

L

A

N

S

R

K

G

G

Y

Y

K

K

V

L

I

I

F

L

V

T

V

M

P

P

E

A

K

S

F

M

S

S

Q

L

E

E

K

R

Q

R

I

V

L

L

M

L

K

R

A

A

L

F

G

G

A

A

E

E

I

L

I

V

N

L

T

T

P

E

K

P

E

A

E

K

G

G

M

M

L

T

G

G

A

A

I

I

E

Q

K

K

S

A

Q

E

E

E

L

I

L

L

R

K

D

K

I

T

P

P

N

N

S

S

I

Y

S

M

L

L

K

Q

Q

Q

F

F

E

D

N

N

E

P

D

A

N

N

P

P

K

K

A

I

H

H

Y

Y

L

E

T

T

G

G

P

P

E

E

I

I

Y

W

M

E

D

D

M

T

E

R

G

G

N

K

I

I

D

D

Y

I

L

L

V

V

A

A

G

G

A

I

G

G

S

T

G

G

T

T

F

I

T

T

G

G

V

V

A

G

Q

R

Y

F

L

I

K

K

E

E

K

R

N

K

K

P

N

E

I

L

K

K

S

V

I

I

L

G

V

V

D

E

P

P

-

T

E

E

G

S

S

A

T

I

M

L

G

S

G

G

T

K

E

P

G

G

C

P

Y

H

G

K

I

I

E

Q

G

G

I

I

G

G

N

A

N

G

F

F

I

V

P

P

E

K

T

N

M

L

D

D

M

L

G

A

L

I

V

V

D

D

K

E

I

Y

I

I

K

A

V

I

N

S

D

S

E

E

A

A

F

I

H

E

M

T

V

S

R

K

K

Q

L

L

A

A

E

L

K

Q

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S

S

G

G

A

A

L

A

V

A

G

A

A

A

L

I

K

Q

L

V

A

A

Q

K

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

A

V

V

F

F

P

P

D

S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

Q

I

L

Y

F

H

Q

Sites not aligning to the query:

61 modified: N-acetylalanine

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)
46% identity, 98% coverage: 6:302/303 of query aligns to 8:308/322 of P47998

query
sites
P47998

D

D

I

V

K

T

E

E

M

L

V

I

G

G

N

N

T

T

P

P

I

L

L

V

K

Y

L

L

N

N

L

V

N

A

V

E

K

G

R

C

E

V

I

G

G

R

I

V

F

A

A

A

K

K

L

L

E

E

S

M

F

M

N

E

P

P

G

C

G

S

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

F

Y

S

M

M

I

I

D

S

S

D

A

A

E

E

K

K

G

G

L

L

L

I

N

K

K

P

G

G

Y

E

T

S

I

V

-

L

V

I

E

E

A

P

T
|
T

A
x
S

G

G

N
|
N

T
|
T

G

G

L

V

G

G

I

L

A

A

L

F

G

T

A

A

L

A

N

A

R

K

G

G

Y

Y

K

K

V

L

I

I

F

I

V

T

V

M

P

P

E

A

K

S

F

M

S

S

Q

T

E

E

K

R

Q

R

I

I

L

I

M

L

K

L

A

A

L

F

G

G

A

V

E

E

I

L

I

V

N

L

T

T

P

D

K

P

E

A

E

K

G

G

M

M

L

K

G

G

A

A

I

I

E

A

K

K

S

A

Q

E

E

E

L

I

L

L

R

A

D

K

I

T

P

P

N

N

S

G

I

Y

S

M

L

L

K

Q

Q
|
Q

F

F

E

E

N

N

E

P

D

A

N

N

P

P

K

K

A

I

H
|
H

Y

Y

L

E

T

T

G
|
G

P

P

E

E

I

I

Y

W

M

K

D

G

M

T

E

G

G

G

N

K

I

I

D

D

Y

G

L

F

V

V

A

S

G

G

A

I

G
|
G

S
x
T

G
|
G

T
|
T

F

I

T

T

G

G

V

A

A

G

Q

K

Y

Y

L

L

K

K

E

E

K

Q

N

N

K

A

N

N

I

V

K

K

S

L

I

Y

L

G

V

V

D

E

P

P

-

V

E

E

G

S

S

A

T

I

M

L

G

S

G

G

T
x
K

E

P

G

G

C

P

Y
x
H

G
x
K

I

I

E

Q

G

G

I

I

G

G

N

A

N

G

F

F

I

I

P

P

E

S

T

V

M

L

D

N

M

V

G

D

L

L

V

I

D

D

K

E

I

V

K

Q

V

V

N

S

D

S

E

D

E

E

A

S

F

I

H

D

M

M

V

A

R

R

K

Q

L

L

A

A

E

L

K

K

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

A

V

A

G

A

A

A

L

I

K

K

L

L

A

A

Q

Q

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

F

V

V

V

A

V

I

F

F

P

P

D

S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

V

I

L

Y

F

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 (≠ A72) 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 (= G159) mutation to E: In old3-1; displays a early leaf death phenotype. Abolishes cysteine synthase activity.
GTGGT 181:185 (≠ GSGGT 178:182) binding pyridoxal 5'-phosphate
T182 (≠ S179) mutation T->A,S: Slight reduction of cysteine synthase activity.
T185 (= T182) mutation T->A,S: Strong reduction of cysteine synthase activity.
K217 (≠ T213) mutation to A: Impaired interaction with SAT1.
H221 (≠ Y217) mutation to A: Impaired interaction with SAT1.
K222 (≠ G218) mutation to A: Impaired interaction with SAT1.
S269 (= S265) 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)
46% identity, 98% coverage: 6:302/303 of query aligns to 6:306/320 of 2isqA

query
sites
2isqA

D

D

I

V

K

T

E

E

M

L

V

I

G

G

N

N

T

T

P

P

I

L

L

V

K

Y

L

L

N

N

L

V

N

A

V

E

K

G

R

C

E

V

I

G

G

R

I

V

F

A

A

A

K

K

L

L

E

E

S

M

F

M

N

E

P

P

G

C

G

S

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

F

Y

S

M

M

I

I

D

S

S

D

A

A

E

E

K

K

G

G

L

L

L

I

N

K

K

P

G

G

Y

E

T

S

I

V

-

L

V

I

E

E

A

P

T
|
T

A
x
S

G
|
G

N
|
N

T
|
T

G

G

L

V

G

G

I

L

A

A

L

F

G

T

A

A

L

A

N

A

R

K

G

G

Y

Y

K

K

V

L

I

I

F

I

V

T

V

M

P

P

E

A

K

S

F

M

S

S

Q

T

E

E

K

R

Q

R

I

I

L

I

M

L

K

L

A

A

L

F

G

G

A

V

E

E

I

L

I

V

N

L

T

T

P

D

K

P

E

A

E

K

G
|
G

M
|
M

L
x
K

G

G

A

A

I

I

E

A

K

K

S

A

Q

E

E

E

L

I

L

L

R

A

D

K

I

T

P

P

N

N

S

G

I

Y

S

M

L

L

K

Q

Q

Q

F

F

E

E

N

N

E

P

D

A

N

N

P

P

K

K

A

I

H

H

Y

Y

L

E

T

T

G

G

P

P

E

E

I

I

Y

W

M

K

D

G

M

T

E

G

G

G

N

K

I

I

D

D

Y

G

L

F

V

V

A

S

G
|
G

A

I

G
|
G

S
x
T

G
|
G

G

G

T
|
T

F

I

T

T

G

G

V

A

A

G

Q

K

Y

Y

L

L

K

K

E

E

K

Q

N

N

K

A

N

N

I

V

K

K

S

L

I

Y

L

G

V

V

D

E

P

P

-

V

E

E

G

S

S

A

T

I

M

L

G

S

G

G

T

K

E

P

G
|
G

C
x
P

Y
x
H

G

K

I

I

E
x
Q

G
|
G

I

I

G

G

N

A

N

G

F

F

I

I

P

P

E

S

T

V

M

L

D

N

M

V

G

D

L

L

V

I

D

D

K

E

I

V

K

Q

V

V

N

S

D

S

E

D

E

E

A

S

F

I

H

D

M

M

V

A

R

R

K

Q

L

L

A

A

E

L

K

K

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

A

V

A

G

A

A

A

L

I

K

K

L

L

A

A

Q

Q

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

F

V

V

V

A

V

I

F

F

P
|
P

D

S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

V

I

L

Y

F

active site: K44 (= K44), S267 (= S265)
binding pyridoxal-5'-phosphate: K44 (= K44), N75 (= N74), G177 (= G176), G179 (= G178), T180 (≠ S179), G181 (= G180), T183 (= T182), G223 (= G221), S267 (= S265), P294 (= P290)
binding : T72 (= T71), S73 (≠ A72), G74 (= G73), T76 (= T75), G122 (= G121), M123 (= M122), K124 (≠ L123), G217 (= G215), P218 (≠ C216), H219 (≠ Y217), Q222 (≠ E220), G223 (= G221)

4aecA Crystal structure of the arabidopsis thaliana o-acetyl-serine-(thiol)- lyasE C (see paper)
44% identity, 99% coverage: 5:303/303 of query aligns to 15:317/323 of 4aecA

query
sites
4aecA

N

D

D

N

I

V

K

S

E

Q

M

L

V

I

G

G

N

K

T

T

P

P

I

M

L

V

K

Y

L

L

N

N

N

S

L

I

N

A

V

K

K

G

R

C

E

V

I

A

G

N

I

I

F

A

A

A

K

K

L

L

E

E

S

I

F

M

N

E

P

P

G

C

S

S

V

V

K
|
K

D

D

R

R

I

I

G

G

L

Y

Y

S

M

M

I

V

D

T

S

D

A

A

E

E

K

Q

K

K

G

G

L

F

L

I

N

S

K

P

G

G

Y

K

T

S

I

V

-

L

V

V

E

E

A

P

T

T

A

S

G

G

N
|
N

T

T

G

G

L

I

G

G

I

L

A

A

L

F

G

I

A

A

L

A

N

S

R

R

G

G

Y

Y

K

R

V

L

I

I

F

L

V

T

V

M

P

P

E

A

K

S

F

M

S

S

Q

M

E

E

K

R

Q

R

I

V

L

L

M

L

K

K

A

A

L

F

G

G

A

A

E

E

I

L

I

V

N

L

T

T

P

D

K

P

E

A

E

K

G

G

M

M

L

T

G

G

A

A

I

V

E

Q

K

K

S

A

Q

E

E

E

L

I

L

L

R

K

D

N

I

T

P

P

N

D

S

A

I

Y

S

M

L

L

K

Q

Q

Q

F

F

E

D

N

N

E

P

D

A

N

N

P

P

K

K

A

I

H

H

Y

Y

L

E

T

T

G

G

P

P

E

E

I

I

Y

W

M

D

D

D

M

T

E

K

G

G

N

K

I

V

D

D

Y

I

L

F

V

V

A

A

G

G

A
x
I

G
|
G

S
x
T

G
|
G

T
|
T

F

I

T

T

G

G

V

V

A

G

Q

R

Y

F

L

I

K

K

E

E

K

K

N

N

K

P

N

K

I

T

K

Q

S

V

I

I

L

G

V

V

D

E

P

P

-

T

E

E

G

S

S

D

T

I

M

L

G

S

G

G

T

K

E

P

G

G

C

P

Y

H

G

K

I

I

E

Q

G
|
G

I

I

G

G

N

A

N

G

F

F

I

I

P

P

E

K

T

N

M

L

D

D

M

Q

G

K

L

I

V

M

D

D

K

E

I

V

I

I

K

A

V

I

N

S

D

S

E

E

A

A

F

I

H

E

M

T

V

A

R

K

K

Q

L

L

A

A

E

L

K

K

E

E

G

G

L

L

I

M

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

A

V

A

G

A

A

A

L

I

K

K

L

V

A

A

Q

K

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

I

V

A

V

V

F

F

P
|
P

D

S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

P

I

L

Y

F

H

Q

active site: K54 (= K44), S277 (= S265)
binding pyridoxal-5'-phosphate: K54 (= K44), N85 (= N74), I188 (≠ A177), G189 (= G178), T190 (≠ S179), G191 (= G180), G192 (= G181), T193 (= T182), G233 (= G221), S277 (= S265), P304 (= P290)

5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
49% identity, 97% coverage: 6:299/303 of query aligns to 34:335/488 of 5ohxA

query
sites
5ohxA

D

D

I

I

K

L

E

T

M

A

V

I

G

G

N

Q

T

T

P

P

I

L

L

I

K

K

L

L

N

N

L

I

N

P

-

K

-

S

-

Y

-

G

V

I

K

K

R

C

E

E

I

I

G

-

I

-

F

Y

A

A

K

K

L

C

E

E

S

F

F

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

G

A

L

Y

Y

R

M

M

I

I

D

Q

S

D

A

A

E

E

K

D

K

K

G

G

L

L

N

K

K

P

G

G

Y

C

T

T

I

I

V

I

E

E

A

P

T

T

A

S

G

G

N
|
N

T

T

G

G

L

I

G

G

I

L

A

A

L

M

G

A

A

A

L

A

N

V

R

R

G

G

Y

Y

K

K

V

C

I

I

F

I

V

V

V

M

P

P

E

E

K

K

F

M

S

S

Q

D

E

E

K

K

Q

I

I

S

L

T

M

L

K

Y

A

A

L

L

G

G

A

A

E

K

I

I

N

R

T

T

P

P

K

T

E

E

E

A

G

S

M

W

L

H

G

S

A

P

-

E

-

A

-

H

I

I

E

S

K

V

S

A

Q

Q

E

K

L

L

L

Q

R

K

D

E

I

I

P

P

N

N

S

S

I

I

S

I

L

L

K

D

Q

Q

F

Y

E

T

N

N

E
x
P

D

G

N

N

P
|
P

K

L

A

A

H

H

Y
|
Y

L

D

T

Q

T

T

G

A

P

I

E

E

I

I

Y

W

M

K

D

Q

M

C

E

E

G

G

N

K

I

I

D

D

Y

Y

L

L

V

V

A

A

G
|
G

A

A

G
|
G

S
x
T

G
|
G

T
|
T

F

I

T

S

G

G

V

I

A

G

Q
x
R

Y

K

L

L

K

K

E

E

K

L

N

S

K

P

N

N

I

I

K

K

S

I

I

I

L

A

V

V

D

D

P

P

E

K

G

G

S

S

T

I

M

L

G

D

G

P

G

S

T

S

E

D

-

E

-

V

G

G

C

F

Y

Y

G

E

I

V

E

E

G
|
G

I

I

G

G

N

Y

N

D

F

F

I

I

P

P

E

T

T

V

M

L

D

D

M

R

G

N

L

V

V

I

D

D

K

K

I

W

I

I

K

K

V

T

N

E

D

D

E

N

E

E

A

S

F

L

H

N

M

A

V

A

R

R

K

M

L

L

A

I

E

R

K

Q

E

E

G

G

L

L

I

L

V

C

G

G

S

G

S
|
S

S

S

G

G

A

A

L

L

V

I

G

A

A

A

L

L

K

K

L

I

A

A

Q

K

S

D

I

I

-

P

D

E

K

E

G

K

N

R

I

M

V

V

V

I

F

L

P
|
P

D
|
D

R

G

G

I

D

R

R

N

Y

Y

F

L

S

T

K

K

binding protoporphyrin ix containing fe: P181 (≠ E148), P184 (= P151), Y188 (= Y155), R221 (≠ Q188)
binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (= G176), G211 (= G178), T212 (≠ S179), G213 (= G180), G214 (= G181), T215 (= T182), G256 (= G221), S300 (= S265), P326 (= P290), D327 (= D291)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 4, 7, 8, 9, 10, 14, 16, 17, 18, 19

1z7yA Crystal structure of the arabidopsis thaliana o-acetylserine sulfhydrylase k46a mutant (see paper)
46% identity, 98% coverage: 6:302/303 of query aligns to 6:306/320 of 1z7yA

query
sites
1z7yA

D

D

I

V

K

T

E

E

M

L

V

I

G

G

N

N

T

T

P

P

I

L

L

V

K

Y

L

L

N

N

L

V

N

A

V

E

K

G

R

C

E

V

I

G

G

R

I

V

F

A

A

A

K

K

L

L

E

E

S

M

F

M

N

E

P

P

G

C

G

S

S

S

V

V

K
x
A

D

D

R

R

I

I

G

G

L

F

Y

S

M

M

I

I

D

S

S

D

A

A

E

E

K

K

G

G

L

L

L

I

N

K

K

P

G

G

Y

E

T

S

I

V

-

L

V

I

E

E

A

P

T

T

A

S

G
|
G

N
|
N

T
|
T

G

G

L

V

G

G

I

L

A

A

L

F

G

T

A

A

L

A

N

A

R

K

G

G

Y

Y

K

K

V

L

I

I

F

I

V

T

V

M

P

P

E

A

K

S

F

M

S

S

Q

T

E

E

K

R

Q

R

I

I

L

I

M

L

K

L

A

A

L

F

G

G

A

V

E

E

I

L

I

V

N

L

T

T

P

D

K

P

E

A

E

K

G

G

M

M

L

K

G

G

A

A

I

I

E

A

K

K

S

A

Q

E

E

E

L

I

L

L

R

A

D

K

I

T

P

P

N

N

S

G

I

Y

S

M

L

L

K

Q

Q
|
Q

F

F

E

E

N

N

E

P

D

A

N

N

P

P

K

K

A

I

H

H

Y

Y

L

E

T

T

G

G

P

P

E

E

I

I

Y

W

M

K

D

G

M

T

E

G

G

G

N

K

I

I

D

D

Y

G

L

F

V

V

A

S

G

G

A
x
I

G
|
G

S
x
T

G
|
G

G

G

T
|
T

F

I

T

T

G

G

V

A

A

G

Q

K

Y

Y

L

L

K

K

E

E

K

Q

N

N

K

A

N

N

I

V

K

K

S

L

I

Y

L

G

V

V

D

E

P

P

-

V

E

E

G

S

S

A

T

I

M

L

G

S

G

G

T

K

E

P

G

G

C

P

Y

H

G

K

I

I

E

Q

G
|
G

I

I

G

G

N

A

N

G

F

F

I

I

P

P

E

S

T

V

M

L

D

N

M

V

G

D

L

L

V

I

D

D

K

E

I

V

K

Q

V

V

N

S

D

S

E

D

E

E

A

S

F

I

H

D

M

M

V

A

R

R

K

Q

L

L

A

A

E

L

K

K

E

E

G

G

L

L

I

L

V

V

G

G

S

I

S
|
S

S

S

G

G

A

A

L

A

V

A

G

A

A

A

L

I

K

K

L

L

A

A

Q

Q

S

R

I

P

D

E

K

N

G

A

N

G

-

K

-

L

I

F

V

V

V

A

V

I

F

F

P
|
P

D
x
S

R

F

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

V

I

L

Y

F

active site: A44 (≠ K44), S267 (= S265)
binding n-[(3-hydroxy-2-methyl-5-{[(trihydroxyphosphoranyl)oxy]methyl}pyridin-4-yl)methylene]methionine: G74 (= G73), N75 (= N74), T76 (= T75), Q145 (= Q144), I178 (≠ A177), G179 (= G178), T180 (≠ S179), G181 (= G180), T183 (= T182), G223 (= G221), S267 (= S265), P294 (= P290), S295 (≠ D291)

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
49% identity, 97% coverage: 6:299/303 of query aligns to 38:342/504 of Q2V0C9

query
sites
Q2V0C9

D

D

I

I

K

L

E

T

M

A

V

I

G

G

N

Q

T

T

P

P

I

L

L

I

K

K

L

L

N

N

L

I

-

P

-

K

-

S

-

Y

N

G

V

I

K

K

R

C

E

E

I

I

G

-

I

-

F

Y

A

A

K

K

L

C

E

E

S

F

F

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

G

A

L

Y

Y

R

M

M

I

I

D

Q

S

D

A

A

E

E

K

D

K

K

G

G

L

L

N

K

K

P

G

G

Y

C

T

T

I

I

V

I

E

E

A

P

T

T

A

S

G

G

N
|
N

T

T

G

G

L

I

G

G

I

L

A

A

L

M

G

A

A

A

L

A

N

V

R

R

G

G

Y

Y

K

K

V

C

I

I

F

I

V

V

V

M

P

P

E

E

K

K

F

M

S

S

Q

D

E

E

K

K

Q

I

I

S

L

T

M

L

K

Y

A

A

L

L

G

G

A

A

E

K

I

I

N

R

T

T

P

P

K

T

E

E

E

A

G

S

M

W

L

H

G

S

A

P

-

E

-

A

-

H

I

I

E

S

K

V

S

A

Q

Q

E

K

L

L

L

Q

R

K

D

E

I

I

P

P

N

N

S

S

I

I

S

I

L

L

K

D

Q

Q

F

Y

E

T

N

N

E

P

D

G

N

N

P

P

K

L

A

A

H

H

Y

Y

L

D

T

Q

T

T

G

A

P

I

E

E

I

I

Y

W

M

K

D

Q

M

C

E

E

G

G

N

K

I

I

D

D

Y

Y

L

L

V

V

A

A

G

G

A

A

G
|
G

S
x
T

G
|
G

T
|
T

F

I

T

S

G

G

V

I

A

G

Q

R

Y

K

L

L

K

K

E

E

K

L

N

S

K

P

N

N

I

I

K

K

S

I

I

I

L

A

V

V

D

D

P

P

E

K

G

G

S

S

T

I

M

L

G

D

G

P

G

S

T

S

E

D

-

S

-

Q

-

N

-

E

-

V

G

G

C

F

Y

Y

G

E

I

V

E

E

G

G

I

I

G

G

N

Y

N

D

F

F

I

I

P

P

E

T

T

V

M

L

D

D

M

R

G

N

L

V

V

I

D

D

K

K

I

W

I

I

K

K

V

T

N

E

D

D

E

N

E

E

A

S

F

L

H

N

M

A

V

A

R

R

K

M

L

L

A

I

E

R

K

Q

E

E

G

G

L

L

I

L

V

C

G

G

S

G

S
|
S

S

S

G

G

A

A

L

L

V

I

G

A

A

A

L

L

K

K

L

I

A

A

Q

K

S

D

I

I

-

P

D

E

K

E

G

K

N

R

I

M

V

V

V

I

F

L

P

P

D

D

R

G

G

I

D

R

R

N

Y

Y

F

L

S

T

K

K

K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
N108 (= N74) binding pyridoxal 5'-phosphate
GTGGT 215:219 (≠ GSGGT 178:182) binding pyridoxal 5'-phosphate
S307 (= S265) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

12 binding axial binding residue
23 binding axial binding residue

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
43% identity, 100% coverage: 1:302/303 of query aligns to 2:306/310 of 5xoqA

query
sites
5xoqA

M

M

V

P

Y

I

Y

F

N

K

D

D

I

N

K

S

E

E

M

S

V

I

G

G

N

R

T

T

P

P

I

L

L

V

K

Q

L

I

N

N

N

R

L

L

N

T

V

A

K

G

R

L

E

S

I

S

G

R

I

V

F

L

A

A

K

K

L

I

E

E

S

G

F

R

N

N

P

P

G

A

G

Y

S

S

V

V

K

K

D

C

R

R

I

I

G

G

L

A

Y

A

M

M

I

I

D

W

S

D

A

A

E

E

K

Q

K

S

G

G

L

K

L

L

N

K

K

P

G

G

Y

M

T

H

I

V

V

V

E

E

A

P

T
|
T

A
x
S

G
|
G

N

N

T
|
T

G

G

L

I

G

A

I

L

A

A

L

F

G

V

A

C

L

A

N

A

R

R

G

G

Y

Y

K

K

V

L

I

T

F

L

V

T

V

M

P

P

E

E

K

T

F

M

S

S

Q

I

E

E

K

R

Q

R

I

M

L

M

M

L

K

K

A

S

L

F

G

G

A

A

E

D

I

L

I

V

N

L

T

T

P

P

K

G

E

A

E

D

G

G

M
|
M

L

K

G

G

A

A

I

I

E

S

K

K

S

A

Q

E

E

E

L

L

L

A

R

A

D

Q

I

-

P

P

N

G

S

W

I

F

S

I

L

P

K

Q

Q
|
Q

F

F

E

K

N

N

E

P

D

A

N

N

P

P

K

A

A

I

H

H

Y

V

L

K

T

T

G

G

P

P

E

E

I

I

Y

W

M

N

D

D

M

T

E

E

G

G

N

Q

I

V

D

D

Y

V

L

F

V

V

A

A

G

G

A

V

G

G

S

T

G

G

T

T

F

I

T

T

G

G

V

V

A

A

Q

R

Y

F

L

L

K

K

-

H

E

E

K

K

N

K

K

H

N

P

I

V

K

H

S

V

I

V

L

A

V

V

D

E

P

P

E

A

G

A

S

S

-

P

T

V

M

L

G

A

G

G

T

P

E

A

G

G

C
x
R

Y
x
H

G

K

I

I

E
x
Q

G
|
G

I

I

G

G

N
x
A

N

G

F

F

I

V

P

P

E

D

T

T

M

F

D

D

M

R

G

S

L

V

V

V

D

D

K

E

I

I

I

L

K

S

V

V

N

T

D

D

E

D

E

E

A

A

F

I

H

E

M

T

V

A

R

R

K

K

L

L

A

A

E

M

K

E

E

E

G

G

L

I

I

S

V

C

G

G

S

I

S

S

S

C

G

G

A

A

L

M

V

A

G

G

A

A

L

L

K

K

L

V

A

A

Q

A

S

R

I

P

D

E

K

F

G

A

-

G

-

K

N

T

I

I

V

V

V

T

V

V

F

L

P

P

D

D

R

A

G

G

D

E

R

R

Y

Y

F

L

S

S

K

T

N

A

I

L

Y

F

binding : T72 (= T71), S73 (≠ A72), G74 (= G73), T76 (= T75), M123 (= M122), Q144 (= Q144), R218 (≠ C216), H219 (≠ Y217), Q222 (≠ E220), G223 (= G221), A226 (≠ N224)

Query Sequence

>WP_012101376.1 NCBI__GCF_000016505.1:WP_012101376.1
MVYYNDIKEMVGNTPILKLNNLNVKREIGIFAKLESFNPGGSVKDRIGLYMIDSAEKKGL
LNKGYTIVEATAGNTGLGIALGALNRGYKVIFVVPEKFSQEKQILMKALGAEIINTPKEE
GMLGAIEKSQELLRDIPNSISLKQFENEDNPKAHYLTTGPEIYMDMEGNIDYLVAGAGSG
GTFTGVAQYLKEKNKNIKSILVDPEGSTMGGGTEGCYGIEGIGNNFIPETMDMGLVDKII
KVNDEEAFHMVRKLAEKEGLIVGSSSGAALVGALKLAQSIDKGNIVVVFPDRGDRYFSKN
IYH

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