SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_005459144.1 NCBI__GCF_000244975.1:WP_005459144.1 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)

P9WP51 Probable cystathionine beta-synthase Rv1077; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
72% identity, 99% coverage: 1:454/457 of query aligns to 1:458/464 of P9WP51

query
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P9WP51

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K428 (= K424) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

7xoyA Cystathionine beta-synthase of mycobacterium tuberculosis in the presence of s-adenosylmethionine and serine. (see paper)
73% identity, 99% coverage: 4:454/457 of query aligns to 2:456/458 of 7xoyA

query
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7xoyA

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binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: K42 (= K44), S70 (= S72), N72 (= N74), T73 (= T75), T180 (= T182), G182 (= G184), T183 (= T185), S267 (= S269), P293 (= P295)

7xnzB Native cystathionine beta-synthase of mycobacterium tuberculosis. (see paper)
73% identity, 99% coverage: 4:454/457 of query aligns to 2:456/458 of 7xnzB

query
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7xnzB

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E

E

D

E

G

G

K

K

P

P

A

V

G

G

V

V

V

I

T

T

R

R

H

Y

D

D

L

L

A

G

F

F

L

L

S

S

binding pyridoxal-5'-phosphate: K42 (= K44), G179 (= G181), T180 (= T182), G181 (= G183), G182 (= G184), T183 (= T185), S267 (= S269), P293 (= P295), D294 (= D296)

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
39% identity, 98% coverage: 11:456/457 of query aligns to 44:496/500 of 7qgtB

query
sites
7qgtB

V

I

G

G

N

D

T

T

P

P

L

M

V

V

K

R

L

I

N

N

A

K

L

I

T

G

Q

K

D

K

-

F

-

G

V

L

E

K

P

C

L

E

V

L

L

L

A

A

K

K

V

C

E

E

Y

F

L

F

N

N

P

A

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

A

S

Q

L

R

R

M

M

I

I

E

E

A

D

A

A

E

E

A

R

S

D

G

G

E

T

L

L

R

K

P

P

G

G

G

D

T

T

I

I

V

I

E

E

P

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

V

I

G

G

L

L

A

A

M

L

V

A

A

A

Q

A

R

V

K

R

G

G

Y

Y

R

R

C

C

V

I

F

I

V

V

C

M

P

P

D

E

K

K

V

M

S

S

E

S

D

E

K

K

R

V

N

D

V

V

L

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

V

V

V

R

C

T

P

P

T

T

A

N

V

A

P

R

P

F

E

D

H

S

P

P

E

E

S

S

Y

H

Y

V

S

G

V

V

S

A

D

W

R

R

L

L

T

K

R

N

E

E

I

I

E

P

G

N

A

S

W

H

K

I

P

L

N

D

Q
|
Q

Y

Y

A

R

N

N

P
x
A

H

S

N

N

P
|
P

E
x
L

S

A

H

H

Y
|
Y

H

D

S

T

T

T

G

A

P

D

E

E

I

I

W

L

K

Q

Q

Q

T

C

E

D

G

G

K

K

V

L

T

D

H

M

F

L

V

V

A

A

G

S

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

S

T

G

G

T

I

G

A

R
|
R

Y

K

L

L

K

K

E

E

V

K

S

C

E

P

G

G

R

-

V

C

K

R

V

I

G

G

A

V

D

D

P

P

E

E

G

G

S

S

V

I

-

L

-

A

-

E

-

P

-

E

Y

L

S

N

G

Q

G

T

T

E

G

Q

R

T

P

T

Y

Y

L

E

V

V

E

E

G
|
G

V

I

G

G

E

Y

D

D

F

F

W

I

P

P

D

T

T

V

Y

L

D

D

C

R

G

T

V

V

A

V

D

D

E

K

I

W

I

F

P

K

V

S

S

N

D

D

A

E

D

E

S

A

F

F

T

T

V

F

T

A

R

R

R

M

L

L

A

I

R

A

E

Q

E

E

G

G

L

L

V

C

G

G

S
|
S

C

A

G

G

M

S

A

T

V

V

A

A

A

V

A

A

L

V

E

K

L

A

A

A

K

Q

R

E

C

L

G

Q

P

E

D

G

D

Q

V

R

I

C

V

V

L

I

L

L

P
|
P

D
|
D

G

S

G

V

R

R

G

N

Y

Y

L

M

G

T

K

K

V

F

F

L

N

S

D

D

T

R

W

W

M

M

S

L

S

Q

Y

K

G

G

F

F

L

L

S

K

P

E

E

E

-

D

-

L

S

T

Q

E

D

K

A

K

T

P

V

W

S

W

D

W

V

H

L

L

R

R

R

V

K

Q

D

E

G

L

T

G

L

L

P

S

D

A

L

P

V

L

H

T

T

V

H

L

P

P

N

T

E

I

T

T

V

C

A

G

E

H

A

T

V

I

A

E

I

I

L

L

R

R

E

E

F

K

G

G

V

F

S

D

Q

Q

M

A

P

P

V

V

S

D

A

E

E

-

P

-

V

-

M

-

A

A

A

G

E

V

V

I

V

L

G

G

A

M

V

V

N

T

E

L

R

G

D

N

L

M

L

L

E

S

A

S

L

L

F

L

T

A

G

G

K

K

A

V

A

Q

L

P

A

S

D

D

R

Q

L

V

E

G

Q

K

H

V

M

I

S

Y

P

K

P

Q

L

F

P

K

T

Q

I

I

G

R

A

L

G

T

E

D

Q

T

I

L

G

G

A

R

A

L

M

S

K

H

A

I

L

L

G

E

A

M

A

D

S

H

G

F

A

A

L

L

V

V

L

V

E

H

D

E

G

Q

K

Q

P

R

A

Q

-

M

-

V

-

F

G

G

V

V

T

T

R

A

H

I

D

D

L

L

A

N

F

F

L

V

S

A

G

A

H

Q

binding protoporphyrin ix containing fe: A186 (≠ P151), P189 (= P154), L190 (≠ E155), Y193 (= Y158), R226 (= R191)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K44), T106 (= T71), S107 (= S72), N109 (= N74), T110 (= T75), Q182 (= Q147), G216 (= G181), T217 (= T182), G218 (= G183), T220 (= T185), G265 (= G225), S309 (= S269), P335 (= P295), D336 (= D296)

Sites not aligning to the query:

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

4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
40% identity, 97% coverage: 11:455/457 of query aligns to 42:486/486 of 4pcuA

query
sites
4pcuA

V

I

G

G

N

D

T

T

P

P

L

M

V

V

K

R

L

I

N

N

A

K

L

I

T

G

Q

K

D

K

-

F

-

G

V

L

E

K

P

C

L

E

V

L

L

L

A

A

K

K

V

C

E

E

Y

F

L

F

N

N

P

A

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

A

S

Q

L

R

R

M

M

I

I

E

E

A

D

A

A

E

E

A

R

S

D

G

G

E

T

L

L

R

K

P

P

G

G

G

D

T

T

I

I

V

I

E

E

P

P

T

T

S
|
S

G

G

N
|
N

T

T

G

G

V

I

G

G

L

L

A

A

M

L

V

A

A

A

Q

A

R

V

K

R

G

G

Y

Y

R

R

C

C

V

I

F

I

V

V

C

M

P

P

D

E

K

K

V

M

S

S

E

S

D

E

K

K

R

V

N

D

V

V

L

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

V

V

V

R

C

T

P

P

T

A

A

R

V

F

P

-

E

D

H

S

P

P

E

S

S

S

Y

H

Y

V

S

G

V

V

S

A

D

W

R

R

L

L

T

K

R

N

E

E

I

I

E

P

G

N

A

S

W

H

K

I

P

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

H

S

N

N

P
|
P

E
x
L

S

A

H

H

Y
|
Y

H

D

S

T

T

T

G

A

P

D

E

E

I

I

W

L

K

Q

Q

Q

T

C

E

D

G

G

K

K

V

L

T

D

H

M

F

L

V

V

A

A

G

S

V

V

G
|
G

T
|
T

G
|
G

G

G

T
|
T

I

I

S

T

G

G

T

I

G

A

R
|
R

Y

K

L

L

K

K

E

E

V

K

S

C

E

P

G

G

R

-

V

C

K

R

V

I

G

G

A

V

D
|
D

P

P

E

E

G

G

S

S

V

I

-

L

-

A

-

E

-

P

-

E

Y

L

S

N

G

Q

G

T

T

E

G

Q

R

T

P

T

Y

Y

L

E

V

V

E

E

G
|
G

V

I

G

G

E

Y

D

D

F

F

W

I

P

P

D
x
T

T

V

Y

L

D

D

C

R

G

T

V

V

A

V

D

D

E

K

I

W

I

F

P

K

V

S

S

N

D

D

A

E

D

E

S

A

F

F

T

T

V

F

T

A

R

R

R

M

L

L

A

I

R

A

E

Q

E

E

G

G

L

L

V

C

G

G

S
|
S

C

A

G

G

M

S

A

T

V

V

A

A

A

V

A

A

L

V

E

K

L

A

A

A

K

Q

R

E

C

L

G

Q

P

E

D

G

D

Q

V

R

I

C

V

V

L

I

L

L

P
|
P

D
|
D

G

S

G

V

R

R

G

N

Y

Y

L

M

G

T

K

K

V

F

F

L

N

S

D

D

T

R

W

W

M

M

S

L

S

Q

Y

K

G

G

F

F

L

L

S

K

P

E

E

E

S

D

Q

L

D

K

A

K

T

P

V

W

S

W

D

W

V

H

L

L

R

R

R

V

K

Q

D

E

G

L

T

G

L

L

P

S

D

A

L
x
P

V

L

H

T

T

V

H

L

P

P

N

T

E

I

T

T

V

C

A

G

E

H

A

T

V

I

A

E

I

I

L

L

R

R

E

E

F

K

G
|
G

V
x
F

S
x
D

Q
|
Q

M

A

P

P

V

V

S

D

A

E

E

-

P

-

V

-

M

-

A

A

A

G

E

V

V

I

V

L

G

G

A

M

V

V

N

T

E

L

R

G

D

N

L

M

L

L

E

S

A

S

L

L

F

L

T

A

G

G

K

K

A

V

A

Q

L

P

A

S

D

D

R

Q

L

V

E

G

Q

K

H

V

M

I

S

Y

P

K

P

Q

L

F

P

K

T

Q

I

I

G

R

A

L

G

T

E

D

Q

T

I

L

G

G

A

R

A

L

M

S

K

H

A

I

L

L

G

E

A

M

A

D

S

H

G

F

A

A

L

L

V

V

L

V

E

H

D

E

G

Q

K

M

P

V

A

F

G

G

V

V

T
|
T

R

A

H
x
I

D
|
D

L

L

A

N

F

F

L

V

S

A

G

A

active site: K77 (= K44), S105 (= S72), D237 (= D207), S305 (= S269)
binding protoporphyrin ix containing fe: A182 (≠ P151), P185 (= P154), L186 (≠ E155), Y189 (= Y158), R222 (= R191), T269 (≠ D233)
binding pyridoxal-5'-phosphate: K77 (= K44), N107 (= N74), G212 (= G181), T213 (= T182), G214 (= G183), T216 (= T185), G261 (= G225), S305 (= S269), P331 (= P295), D332 (= D296)
binding s-adenosylmethionine: P376 (≠ L340), G396 (= G360), F397 (≠ V361), D398 (≠ S362), Q399 (= Q363), T476 (= T445), I478 (≠ H447), D479 (= D448)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23

8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
39% identity, 98% coverage: 11:456/457 of query aligns to 43:505/507 of 8s5hA

query
sites
8s5hA

V

I

G

G

N

D

T

T

P

P

L

M

V

V

K

R

L

I

N

N

A

K

L

I

T

G

Q

K

D

K

-

F

-

G

V

L

E

K

P

C

L

E

V

L

L

L

A

A

K

K

V

C

E

E

Y

F

L

F

N

N

P

A

G

G

S

S

V

V

K

K

D

D

R

R

I

I

A

S

Q

L

R

R

M

M

I

I

E

E

A

D

A

A

E

E

A

R

S

D

G

G

E

T

L

L

R

K

P

P

G

G

G

D

T

T

I

I

V

I

E

E

P

P

T

T

S

S

G

G

N

N

T

T

G

G

V

I

G

G

L

L

A

A

M

L

V

A

A

A

Q

A

R

V

K

R

G

G

Y

Y

R

R

C

C

V

I

F

I

V

V

C

M

P

P

D

E

K

K

V

M

S

S

E

S

D

E

K

K

R

V

N

D

V

V

L

L

K

R

A

A

Y

L

G

G

A

A

E

E

V

I

V

V

V

R

C

T

P

P

T

T

A

N

V

A

P

R

P

F

E

D

H

S

P

P

E

E

S

S

Y

H

Y

V

S

G

V

V

S

A

D

W

R

R

L

L

T

K

R

N

E

E

I

I

E

P

G

N

A

S

W

H

K

I

P

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

H

S

N

N

P

P

E

L

S

A

H

H

Y
|
Y

H

D

S

T

T

T

G

A

P

D

E

E

I

I

W

L

K

Q

Q

Q

T

C

E

D

G

G

K

K

V

L

T

D

H

M

F

L

V

V

A

A

G

S

V

V

G

G

T

T

G

G

T

T

I

I

S

T

G

G

T

I

G

A

R
|
R

Y

K

L

L

K

K

E

E

V

K

S

C

E

P

G

G

R

-

V

C

K

R

V

I

G

G

A

V

D

D

P

P

E

E

G

G

S

S

V

I

-

L

-

A

-

E

-

P

-

E

Y

L

S

N

G

Q

G

T

T

E

G

Q

R

T

P

T

Y

Y

L

E

V

V

E

E

G

G

V

I

G

G

E

Y

D

D

F

F

W

I

P

P

D

T

T

V

Y

L

D

D

C

R

G

T

V

V

A

V

D

D

E

K

I

W

I

F

P

K

V

S

S

N

D

D

A

E

D

E

S

A

F

F

T

T

V

F

T

A

R

R

R

M

L

L

A

I

R

A

E

Q

E

E

G

G

L

L

V

C

G

G

S

S

C

A

G

G

M

S

A

T

V

V

A

A

A

V

A

A

L

V

E

K

L

A

A

A

K

Q

R

E

C

L

G

Q

P

E

D

G

D

Q

V

R

I

C

V

V

L

I

L

L

P

P

D

D

G

S

G

V

R

R

G

N

Y

Y

L

M

G

T

K

K

V

F

F

L

N

S

D

D

T

R

W

W

M

M

S

L

S

Q

Y

K

G

G

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binding protoporphyrin ix containing fe: A185 (≠ P151), Y192 (= Y158), R225 (= R191)

Sites not aligning to the query:

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

P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
39% identity, 98% coverage: 11:456/457 of query aligns to 84:546/551 of P35520

query
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P35520

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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 (≠ V26) 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 (≠ V34) 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 (= R50) 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 (= L79) 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 (= C90) 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 (≠ V98) 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 (≠ D101) 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 (= V105) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ C116) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ T136) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ P151) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N153) 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 (≠ S156) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ H159) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
GTGGT 256:260 (= GTGGT 181:185) binding pyridoxal 5'-phosphate
T257 (= T182) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (≠ S187) 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 (= R191) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K194) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ S197) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ V201) 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 (≠ V204) 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 (= D207) to N: in CBSD; loss of activity
A288 (vs. gap) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (≠ L222) 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 (= G225) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (= G227) 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 (≠ A240) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D241) to V: in CBSD; loss of activity
R336 (= R256) 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 (= L258) 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 (= G267) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (= S269) 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 (≠ A273) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ V289) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D296) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (= R299) 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 (= K304) to E: in CBSD; severe form; dbSNP:rs121964967
P422 (≠ L340) to L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
P427 (= P345) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
I435 (≠ V353) to T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
R439 (= R357) to Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
D444 (≠ S362) to N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
V449 (= V367) to G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
L456 (≠ V379) to P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
S466 (≠ E389) to L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
S500 (≠ M423) to L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
Q526 (vs. gap) to K: in CBSD; has significantly decreased levels of enzyme activity
L539 (= L449) to S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
L540 (= L450) to Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet

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
548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989

5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
38% identity, 100% coverage: 2:456/457 of query aligns to 27:488/488 of 5ohxA

query
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5ohxA

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Q

Q

T

C

E

E

G

G

K

K

V

I

T

D

H

Y

F

L

V

V

A

A

G
|
G

V

A

G
|
G

T
|
T

G
|
G

T
|
T

I

I

S

S

G

G

T

I

G

G

R
|
R

Y

K

L

L

K

K

E

E

V

L

S

S

E

P

G

N

R

-

V

I

K

K

V

I

G

A

A

V

D

D

P

P

E

K

G

G

S

S

V

I

Y

L

S

D

G

P

G

S

T

S

G

D

R

E

P

V

-

G

-

F

Y

Y

L

E

V

V

E

E

G
|
G

V

I

G

G

E

Y

D

D

F

F

W

I

P

P

D

T

T

V

Y

L

D

D

C

R

G

N

V

V

A

I

D

D

E

K

I

W

I

I

P

K

V

T

S

E

D

D

A

N

D

E

S

S

F

L

T

N

V

A

T

A

R

R

R

M

L

L

A

I

R

R

E

Q

E

E

G

G

L

L

V

C

G

G

S
|
S

C

S

G

G

M

A

A

A

V

L

A

I

A

A

L

L

E

K

L

I

A

A

K

K

R

D

C

I

G

P

P

E

D

E

D

K

V

R

I

M

V

V

V

I

L

I

L

L

P
|
P

D
|
D

G

G

G

I

R

R

G

N

Y

Y

L

L

G

T

K

K

V

F

F

V

N

S

D

E

T

Y

W

W

M

M

S

E

S

T

Y

R

G

G

F

F

L

L

S

Q

P

P

E

V

S

C

Q

Q

D

N

A

E

T

M

V

N

S

K

D

W

V

W

L

W

R

N

R

M

K

K

D

I

G

S

T

N

L

L

P

S

D

F

L

D

V

K

H

Q

T

S

H

L

P

L

N

K

E

E

-

N

-

T

-

V

T

T

V

C

A

Q

E

E

A

A

V

M

A

H

I

M

L

L

R

K

E

N

F

-

G

A

V

D

S

S

Q

Q

M

L

P

L

V

V

V

I

S

S

A

D

E

D

P

-

V

-

M

-

A

N

A

I

E

H

V

I

V

K

G

G

A

V

V

I

N

S

E

L

R

N

D

K

L

L

L

T

E

S

A

Y

L

V

F

I

T

S

G

G

K

I

A

V

A

K

L

C

A

T

D

D

R

F

L

V

E

D

Q

K

H

A

M

M

S

V

P

K

P

Q

L

Y

P

V

T

K

I

V

G

K

A

H

G

S

E

A

Q

T

I

L

G

G

A

Y

A

I

M

S

K

R

A

V

L

L

G

E

A

K

A

E

S

P

G

Y

A

V

L

I

V

I

L

L

E

D

D

D

G

E

K

H

P

D

-

D

-

A

-

F

A

I

G

G

V

I

V

V

T

N

R

Q

H

F

D

H

L

I

L

L

A

Q

F

F

L

I

S

T

G

K

H

N

binding protoporphyrin ix containing fe: P181 (= P151), P184 (= P154), Y188 (= Y158), R221 (= R191)
binding pyridoxal-5'-phosphate: K74 (= K44), N104 (= N74), G209 (= G179), G211 (= G181), T212 (= T182), G213 (= G183), G214 (= G184), T215 (= T185), G256 (= G225), S300 (= S269), P326 (= P295), D327 (= D296)

Sites not aligning to the query:

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

Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
38% identity, 100% coverage: 2:456/457 of query aligns to 31:495/504 of Q2V0C9

query
sites
Q2V0C9

D

D

Y

Y

A

T

E

K

H

I

V

M

T

P

D

D

L

I

-

L

-

T

-

A

V

I

G

G

N

Q

T

T

P

P

L

L

V

I

K

K

L

L

N

N

A

N

L

I

T

P

Q

K

D

S

-

Y

-

G

V

I

E

K

P

C

L

E

V

I

L

Y

A

A

K

K

V

C

E

E

Y

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

A

A

Q

Y

R

R

M

M

I

I

E

Q

A

D

A

A

E

E

A

D

S

K

G

G

E

L

L

L

R

K

P

P

G

G

G

C

T

T

I

I

V

I

E

E

P

P

T

T

S

S

G

G

N
|
N

T

T

G

G

V

I

G

G

L

L

A

A

M

M

V

A

A

A

Q

A

R

V

K

R

G

G

Y

Y

R

K

C

C

V

I

F

I

V

V

C

M

P

P

D

E

K

K

V

M

S

S

E

D

D

E

K

K

R

I

N

S

V

T

L

L

K

Y

A

A

Y

L

G

G

A

A

E

K

V

I

V

R

C

T

P

P

T

T

A

E

V

A

P

S

P

W

E

H

H

S

P

P

E

E

S

A

Y

H

Y

I

S

S

V

V

S

A

D

Q

R

K

L

L

T

Q

R

K

E

E

I

I

E

P

G

N

A

S

W

I

K

I

P

L

N

D

Q

Q

Y

Y

A

T

N

N

P

P

H

G

N

N

P

P

E

L

S

A

H

H

Y

Y

H

D

S

Q

T

T

G

A

P

I

E

E

I

I

W

W

K

K

Q

Q

T

C

E

E

G

G

K

K

V

I

T

D

H

Y

F

L

V

V

A

A

G

G

V

A

G
|
G

T
|
T

G
|
G

T
|
T

I

I

S

S

G

G

T

I

G

G

R

R

Y

K

L

L

K

K

E

E

V

L

S

S

E

P

G

N

R

-

V

I

K

K

V

I

G

A

A

V

D

D

P

P

E

K

G

G

S

S

V

I

Y

L

S

D

G

P

G

S

T

S

G

D

R

S

P

Q

-

N

-

E

-

V

-

G

-

F

Y

Y

L

E

V

V

E

E

G

G

V

I

G

G

E

Y

D

D

F

F

W

I

P

P

D

T

T

V

Y

L

D

D

C

R

G

N

V

V

A

I

D

D

E

K

I

W

I

I

P

K

V

T

S

E

D

D

A

N

D

E

S

S

F

L

T

N

V

A

T

A

R

R

R

M

L

L

A

I

R

R

E

Q

E

E

G

G

L

L

V

C

G

G

S
|
S

C

S

G

G

M

A

A

A

V

L

A

I

A

A

L

L

E

K

L

I

A

A

K

K

R

D

C

I

G

P

P

E

D

E

D

K

V

R

I

M

V

V

V

I

L

I

L

L

P

P

D

D

G

G

G

I

R

R

G

N

Y

Y

L

L

G

T

K

K

V

F

F

V

N

S

D

E

T

Y

W

W

M

M

S

E

S

T

Y

R

G

G

F

F

L

L

S

Q

P

P

E

V

S

C

Q

Q

D

N

A

E

T

M

V

N

S

K

D

W

V

W

L

W

R

N

R

M

K

K

D

I

G

S

T

N

L

L

P

S

D

F

L

D

V

K

H

Q

T

S

H

L

P

L

N

K

E

E

-

N

-

T

-

V

T

T

V

C

A

Q

E

E

A

A

V

M

A

H

I

M

L

L

R

K

E

N

F

-

G

A

V

D

S

S

Q

Q

M

L

P

L

V

V

V

I

S

S

A

D

E

D

P

-

V

-

M

-

A

N

A

I

E

H

V

I

V

K

G

G

A

V

V

I

N

S

E

L

R

N

D

K

L

L

L

T

E

S

A

Y

L

V

F

I

T

S

G

G

K

I

A

V

A

K

L

C

A

T

D

D

R

F

L

V

E

D

Q

K

H

A

M

M

S

V

P

K

P

Q

L

Y

P

V

T

K

I

V

G

K

A

H

G

S

E

A

Q

T

I

L

G

G

A

Y

A

I

M

S

K

R

A

V

L

L

G

E

A

K

A

E

S

P

G

Y

A

V

L

I

V

I

L

L

E

D

D

D

G

E

K

H

P

D

-

D

-

A

-

F

A

I

G

G

V

I

V

V

T

N

R

Q

H

F

D

H

L

I

L

L

A

Q

F

F

L

I

S

T

G

K

H

N

K78 (= K44) modified: N6-(pyridoxal phosphate)lysine
N108 (= N74) binding pyridoxal 5'-phosphate
GTGGT 215:219 (= GTGGT 181:185) binding pyridoxal 5'-phosphate
S307 (= S269) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

12 binding axial binding residue
23 binding axial binding residue

3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
38% identity, 98% coverage: 6:455/457 of query aligns to 40:498/500 of 3pc2A

query
sites
3pc2A

H

N

V

I

T

L

D

E

L

V

V

I

G

G

N

C

T

T

P

P

L

L

V

V

K

K

L

L

N

N

A

N

L

I

-

P

-

A

T

S

Q

D

D

G

V

I

E

E

P

C

L

E

V

M

L

Y

A

A

K

K

V

C

E

E

Y

F

L

L

N

N

P

P

G

G

S

S

V

V

K
|
K

D

D

R

R

I

I

A

G

Q

Y

R

R

M

M

I

V

E

Q

A

D

A

A

E

E

A

E

S

Q

G

G

E

L

L

L

R

K

P

P

G

G

G

Y

T

T

I

I

V

I

E

E

P

P

T

T

S

S

G

G

N
|
N

T

T

G

G

V

I

G

G

L

L

A

A

M

M

V

A

A

C

Q

A

R

V

K

K

G

G

Y

Y

R

K

C

C

V

I

F

I

V

V

C

M

P

P

D

E

K

K

V

M

S

S

E

N

D

E

K

K

R

V

N

S

V

A

L

L

K

R

A

T

Y

L

G

G

A

A

E

K

V

I

V

R

C

T

P

P

T

T

A

E

V

A

P

A

P

Y

E

D

H

S

P

P

E

E

S

G

Y

L

Y

I

S

Y

V

V

S

A

D

Q

R

Q

L

L

T

Q

R

R

E

E

I

T

E

P

G

N

A

S

W

I

K

V

P

L

N

D

Q

Q

Y

Y

A

R

N

N

P
x
A

H

G

N

N

P
|
P

E
x
L

S

A

H

H

Y
|
Y

H

D

S

G

T

T

G

A

P

A

E

E

I

I

W

L

K

W

Q

Q

T

L

E

D

G

N

K

K

V

V

T

D

H

M

F

I

V

V

A

V

G

S

V
x
A

G
|
G

T
|
T

G
x
A

G

G

T
|
T

I

I

S

S

G

G

T

I

G

G

R
|
R

Y

K

L

I

K

K

E

E

V

Q

S

V

E

P

G

S

R

-

V

C

K

Q

V

I

V

V

G

G

A

V

D

D

P

P

E

Y

G

G

S

S

V

I

Y

L

S

A

G

-

T

-

G

-

R

R

P

P

-

A

-

E

-

L

-

N

-

K

-

T

-

D

-

V

-

Q

-

F

Y

Y

L

E

V

V

E

E

G
|
G

V

I

G

G

E

Y

D

D

F

F

W

P

P

P

D

T

T

V

Y

F