SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010963544.1 NCBI__GCF_000008765.1:WP_010963544.1 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)

Q988B8 Pyridoxamine--pyruvate transaminase; Pyridoxamine-pyruvate aminotransferase; EC 2.6.1.30 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
34% identity, 90% coverage: 5:342/377 of query aligns to 12:353/393 of Q988B8

query
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Q988B8

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E68 (= E62) binding pyridoxal 5'-phosphate; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
Y95 (≠ F89) binding pyridoxal 5'-phosphate
T146 (= T140) binding pyridoxal 5'-phosphate
K197 (= K191) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
C198 (= C192) mutation to A: No effect on enzyme activity.
R336 (≠ F325) mutation to A: Strongly decreased affinity for pyruvate.
R345 (= R334) binding pyridoxal 5'-phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
34% identity, 90% coverage: 5:342/377 of query aligns to 11:352/392 of 2z9xA

query
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2z9xA

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binding alanine: Y94 (≠ F89), R344 (= R334)
binding 3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde: E67 (= E62), Y94 (≠ F89), T145 (= T140), D170 (= D165), V172 (= V167), K196 (= K191)

2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
34% identity, 90% coverage: 5:342/377 of query aligns to 11:352/392 of 2z9wA

query
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2z9wA

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binding 3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde: E67 (= E62), P68 (≠ G63), Y94 (≠ F89), T145 (= T140), D170 (= D165), V172 (= V167), S173 (= S168), K196 (= K191)

2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
34% identity, 90% coverage: 5:342/377 of query aligns to 11:352/392 of 2z9vA

query
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2z9vA

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D

R

A

A

F

W

S

A

A

K

M

M

K

K

-

A

N

N

R

P

K

L

T

A

P

P

I

R

A

A

S

S

F

M

Y

-

C

L

N

S

L

I

L

V

V

D

W

W

E

E

D

N

Y

A

Y

W

N

S

K

R

-

D

K

K

W

P

F

F

P

P

Y

F

T

T

P

P

P

S

I

V

S

S

D

E

I

I

V

N

A

G

L

L

R

D

K

V

A

A

V

L

E

D

N

L

I

Y

L

L

E

N

E

E

-

G

-

P

K

E

D

A

I

V

I

W

A

A

R

R

H

H

D

A

K

L

I

T

A

A

S

K

A

A

T

M

R

R

A

A

A

G

V

V

V

T

L

A

G

M

G

G

L

L

E

S

I

V

Y

W

I

A

E

A

D

S

G

D

-

S

-

I

F

A

S

S

N

P

T

T

V

T

T

T

V

A

I

V

K

R

V

T

P

P

H

D

G

G

M

V

N

D

D

E

D

K

K

A

I

L

L

R

S

Q

Y

A

M

A

K

R

E

A

N

R

Y

Y

N

G

V

V

M

V

I

F

A

S

G

S

A

G

F

R

D

G

Y

E

L

T

K

L

G

G

K

K

V

L

L

T

R

R

I

I

G

G

H

H

M

M

G

G

E

P

N

T

A

A

binding 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol: E67 (= E62), V69 (≠ I64), Y94 (≠ F89), T145 (= T140), D170 (= D165), V172 (= V167)

6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
30% identity, 94% coverage: 5:359/377 of query aligns to 20:381/386 of 6mfbD

query
sites
6mfbD

I

I

I

M

M

M

T

G

P

P

G

G

P

P

T

S

S

N

V

C

R

S

E

K

N

R

V

V

R

-

L

L

S

A

R

A

A

L

E

N

K

N

T

T

T

C

N

L

P

S

D

N

L

F

D

H

M

D

D

E

F

L

Y

F

D

Q

F

V

Y

I

K

D

K

E

T

V

T

K

E

D

K

G

I

L

G

R

K

Y

F

I

L

F

K

Q

T

T

K

E

N

N

E

R

V

T

R

T

I

M

-

C

L

I

S

T

G

G

E
x
S

G
x
A

I
x
H

L

T

G

G

L

M

E

E

A

A

A

L

C

L

A

C

S

N

L

L

T

L

E

E

K

E

G

G

D

D

R

I

V

V

L

L

V

I

I

A

E

N

N

N

G

G

I

I

F
x
W

G

A

E

E

G

R

F

A

A

I

D

N

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

F

L

R

E

G

G

N

P

K

A

K

D

C

K

S

P

I

F

N

S

I

M

E

T

E

D

L

F

E

K

R

K

F

A

L

I

D

E

S

Q

D

H

S

R

E

P

F

-

K

K

Y

C

A

L

T

F

V

V

H

H

C

G

D

D

T
x
S

P

S

S

S

G

G

M

L

L

L

N

Q

N

P

V

L

G

E

A

G

I

L

C

G

K

K

L

I

L

C

K

H

K

D

K

Y

G

D

I

C

M

L

T

L

V

L

V

V

D
|
D

S

A

V
|
V

S

A

A

S

M

L

G

C

G

G

E

V

E

P

L

F

K

Y

V

M

D

D

E

K

W

W

D

E

I

I

D

D

I

G

V

V

I

Y

G

T

G

G

S

S

Q
|
Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

I

S

S

I

I

S

S

D

P

D

K

A

A

F

L

S

E

A

V

M

I

K

R

N

S

R

R

K

K

T

T

P

P

I

S

A

K

S

V

F

F

Y

Y

C

W

N

D

L

L

V

I

-

L

-

G

-

N

-

Y

W

W

E

G

D

C

Y

Y

Y

D

N

E

K

Q

K

K

W

R

F
x
Y

P

H

Y

H

T
|
T

P

V

P

P

I

S

S

N

D

L

I

I

V

F

A

A

L

L

R

R

K

E

A

A

V

I

E

A

N

Q

I

I

L

A

E

E

-

G

-

L

K

E

D

P

I

V

I

I

A

R

R

R

H

R

D

Q

K

E

I

C

A

A

S

E

A

Q

T

M

R

Y

A

R

A

G

V

L

V

Q

L

A

G

M

G

G

L

L

E

E

I

I

Y

F

I

V

E

K

D

D

G

P

F

E

S

Y

N

R

-

L

-

P

T

T

V

V

T

T

V

C

I

I

K

M

V

I

P

P

H

K

G

G

M

V

N

N

D

W

K

K

I

V

L

S

S

E

Y

Y

M

A

K

M

E

N

N

N

Y

F

N

S

V

L

M

E

I

I

A

Q

G

G

A

G

F

F

D

G

Y

P

L

T

K

M

G

G

K

I

V

A

L

W

R

R

I

A

G

G

H

I

M

M

G

G

E

E

N

S

A

S

Y

T

V

L

D

Q

K

R

V

V

S

N

Y

F

T

Y

L

L

F

Y

A

A

L

F

Q

K

R

E

T

S

L

L

E

K

binding pyridoxal-5'-phosphate: S77 (≠ E62), A78 (≠ G63), H79 (≠ I64), W104 (≠ F89), S154 (≠ T140), D179 (= D165), V181 (= V167), Q204 (= Q190), K205 (= K191), Y256 (≠ F238), T259 (= T241)

Q0IG34 3-hydroxykynurenine transaminase; 3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase; Ae-HKT/AGT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
30% identity, 96% coverage: 5:367/377 of query aligns to 20:391/400 of Q0IG34

query
sites
Q0IG34

I

I

I

M

M

M

T

G

P

P

G

G

P

P

T

S

S

N

V

C

R

S

E

K

N

R

V

V

R

-

L

L

S

A

R

A

A

L

E

N

K

N

T

T

T

C

N

L

P

S

D

N

L

F

D

H

M

D

D

E

F

L

Y

F

D

Q

F

V

Y

I

K

D

K

E

T

V

T

K

E

D

K

G

I

L

G

R

K

Y

F

I

L

F

K

Q

T

T

K

E

N

N

E

R

V

T

R

T

I

M

-

C

L

I

S

T

G

G

E
x
S

G
x
A

I
x
H

L

T

G

G

L

M

E

E

A

A

A

L

C

L

A

C

S

N

L

L

T

L

E

E

K

E

G

G

D

D

R

I

V

V

L

L

V

I

I

A

E

N

N

N

G

G

I

I

F

W

G

A

E

E

G

R

F

A

A

I

D

N

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

F

L

R

G

G

G

N

P

K

A

K

D

C

K

S

P

I

F

N

S

I

M

E

T

E

D

L

F

E

K

R

K

F

A

L

I

D

E

S

Q

D

H

S

R

E

P

F

-

K

K

Y

C

A

L

T

F

V

V

H

H

C

G

D

D

T
x
S

P

S

S

S

G

G

M

L

L

L

N

Q

N

P

V

L

G

E

A

G

I

L

C

G

K

K

L

I

L

C

K

H

K

D

K

Y

G

D

I

C

M

L

T

L

V

L

V

V

D

D

S

A

V

V

S

A

A

S

M

L

G

C

G

G

E

V

E

P

L

F

K

Y

V

M

D

D

E

K

W

W

D

E

I

I

D

D

I

G

V

V

I

Y

G

T

G

G

S

S

Q
|
Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

I

S

S

I

I

S

S

D

P

D

K

A

A

F

L

S

E

A

V

M

I

K

R

N

S

R

R

K

K

T

T

P

P

I

S

A

K

S

V

F

F

Y

Y

C

W

N

D

L

L

V

I

-

L

-

G

-

N

-

Y

W

W

E

G

D

C

Y

Y

Y

D

N

E

K

Q

K

K

W

R

F
x
Y

P

H

Y

H

T
|
T

P

V

P

P

I

S

S

N

D

L

I

I

V

F

A

A

L

L

R

R

K

E

A

A

V

I

E

A

N

Q

I

I

L

A

E

E

-

G

-

L

K

E

D

P

I

V

I

I

A

R

R

R

H

R

D

Q

K

E

I

C

A

A

S

E

A

Q

T

M

R

Y

A

R

A

G

V

L

V

Q

L

A

G

M

G

G

L

L

E

E

I

I

Y

F

I

V

E

K

D

D

G

P

F

E

S

Y

N

R

-

L

-

P

T

T

V

V

T

T

V

C

I

I

K

M

V

I

P

P

H

K

G

G

M

V

N

N

D

W

K

K

I

V

L

S

S

E

Y

Y

M

A

K

M

E

N

N

N

Y

F

N

S

V

L

M

E

I

I

A

Q

G

G

A

G

F

F

D

G

Y

P

L

T

K

M

G

G

K

I

V

A

L

W

R

R

I

A

G

G

H

I

M

M

G

G

E

E

N

S

A

S

Y

T

V

L

D

Q

K

R

V

V

S

N

Y

F

T

Y

L

L

F

Y

A

A

L

F

Q

K

R

E

T

S

L

L

E

K

-

A

-

T

H

H

Y

P

G

D

F

Y

E

V

F

F

K

E

R

K

SAH 77:79 (≠ EGI 62:64) binding in other chain
S154 (≠ T140) binding in other chain
Q204 (= Q190) binding in other chain
K205 (= K191) modified: N6-(pyridoxal phosphate)lysine
Y256 (≠ F238) binding pyridoxal 5'-phosphate
T259 (= T241) binding pyridoxal 5'-phosphate

2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
29% identity, 94% coverage: 5:359/377 of query aligns to 19:380/388 of 2ch1A

query
sites
2ch1A

I

I

I

M

M

M

T

G

P

P

G

G

P

P

T

S

S

N

V

C

R

S

E

K

N

R

V

V

R

-

L

L

S

T

R

A

A

M

E

T

K

N

T

T

T

V

N

L

P

S

D

N

L

F

D

H

M

A

D

E

F

L

Y

F

D

R

F

T

Y

M

K

D

K

E

T

V

T

K

E

D

K

G

I

L

G

R

K

Y

F

I

L

F

K

Q

T

T

K

E

N

N

E

R

V

A

R

T

I

M

-

C

L

V

S

S

G

G

E
x
S

G
x
A

I
x
H

L

A

G

G

L

M

E

E

A

A

A

M

C

L

A

S

S

N

L

L

T

L

E

E

K

E

G

G

D

D

R

R

V

V

L

L

V

I

I

A

E

V

N

N

G

G

I

I

F
x
W

G

A

E

E

G

R

F

A

A

V

D

E

F

M

V

S

K

E

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

T

F

I

R

E

G

G

N

P

K

P

K

D

C

R

S

P

I

F

N

S

I

L

E

E

E

T

L

L

E

A

R

R

F

A

L

I

D

E

S

L

D

H

S

Q

E

P

F

-

K

K

Y

C

A

L

T

F

V

L

V

T

H

H

C

G

D

D

T
x
S

P

S

S

S

G

G

M

L

L

L

N

Q

N

P

V

L

G

E

A

G

I

V

C

G

K

Q

L

I

L

C

K

H

K

Q

K

H

G

D

I

C

M

L

T

L

V

I

V

V

D
|
D

S

A

V
|
V

S

A

A

S

M

L

G

C

G

G

E

V

E

P

L

F

K

Y

V

M

D

D

E

K

W

W

D

E

I

I

D

D

I

A

V

V

I

Y

G

T

G

G

S

A

Q
|
Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

I

S

S

I

I

S

S

D

P

D

K

A

A

F

L

S

D

A

V

M

I

K

R

N

N

R

R

K

R

T

T

P

K

I

S

A

K

S

V

F

F

Y

Y

C

W

N

D

L

L

V

L

-

L

-

G

-

N

-

Y

W

W

E

G

D

C

Y

Y

Y

D

N

E

K

P

K

K

W

R

F
x
Y

P

H

Y

H

T
|
T

P

V

P

A

I

S

S

N

D

L

I

I

V

F

A

A

L

L

R

R

K

E

A

A

V

L

E

A

N

Q

I

I

L

A

E

E

-

G

-

L

K

E

D

N

I

Q

I

I

A

K

R

R

H

R

D

I

K

E

I

C

A

A

S

Q

A

I

T

L

R

Y

A

E

A

G

V

L

V

G

L

K

G

M

G

G

L

L

E

D

I

I

Y

F

I

V

E

K

D

D

G

P

F

R

S

H

N

R

-

L

-

P

T

T

V

V

T

T

V

G

I

I

K

M

V

I

P

P

H

K

G

G

M

V

N

D

D

W

K

K

I

V

L

S

S

Q

Y

Y

M

A

K

M

E

N

N

N

Y

F

N

S

V

L

M

E

I

V

A

Q

G

G

A

G

F

L

D

G

Y

P

L

T

K

F

G

G

K

K

V

A

L

W

R

R

I

V

G

G

H

I

M

M

G

G

E

E

N

C

A

S

Y

T

V

V

D

Q

K

K

V

I

S

Q

Y

F

T

Y

L

L

F

Y

A

G

L

F

Q

K

R

E

T

S

L

L

E

K

binding pyridoxal-5'-phosphate: S76 (≠ E62), A77 (≠ G63), H78 (≠ I64), W103 (≠ F89), S153 (≠ T140), D178 (= D165), V180 (= V167), Q203 (= Q190), K204 (= K191), Y255 (≠ F238), T258 (= T241)

Q7PRG3 3-hydroxykynurenine transaminase; AgHKT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Anopheles gambiae (African malaria mosquito) (see paper)
29% identity, 94% coverage: 5:359/377 of query aligns to 20:381/396 of Q7PRG3

query
sites
Q7PRG3

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SAH 77:79 (≠ EGI 62:64) binding in other chain
S154 (≠ T140) binding in other chain
Q204 (= Q190) binding in other chain
K205 (= K191) modified: N6-(pyridoxal phosphate)lysine
Y256 (≠ F238) binding pyridoxal 5'-phosphate
T259 (= T241) binding pyridoxal 5'-phosphate

2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
29% identity, 94% coverage: 5:359/377 of query aligns to 18:379/387 of 2ch2A

query
sites
2ch2A

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binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G10), S41 (≠ P29), N42 (≠ D30), S152 (≠ T140), Y254 (≠ F238), Q342 (≠ A322), L345 (≠ F325), R354 (= R334)
binding pyridoxal-5'-phosphate: S75 (≠ E62), A76 (≠ G63), H77 (≠ I64), W102 (≠ F89), S152 (≠ T140), D177 (= D165), V179 (= V167), K203 (= K191), Y254 (≠ F238), T257 (= T241)

5hhyA Structure of human alanine:glyoxylate aminotransferase major allele (agt-ma) showing x-ray induced reduction of plp internal aldimine to 4'-deoxy-piridoxine-phosphate (plr) (see paper)
28% identity, 94% coverage: 5:360/377 of query aligns to 19:381/385 of 5hhyA

query
sites
5hhyA

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H

H

binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ E62), G77 (= G63), H78 (≠ I64), W103 (≠ F89), S153 (≠ T140), D178 (= D165), V180 (= V167), Q203 (= Q190), K204 (= K191), Y255 (≠ F238), T258 (= T241)

3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
29% identity, 94% coverage: 6:358/377 of query aligns to 10:365/387 of 3islA

query
sites
3islA

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binding pyridoxal-5'-phosphate: T66 (≠ E62), S67 (≠ G63), R68 (≠ I64), F93 (= F89), T143 (= T140), D168 (= D165), V170 (= V167), Q193 (= Q190), K194 (= K191)

P21549 Alanine--glyoxylate aminotransferase; AGT; Serine--pyruvate aminotransferase; SPT; EC 2.6.1.44; EC 2.6.1.51 from Homo sapiens (Human) (see 24 papers)
28% identity, 94% coverage: 5:360/377 of query aligns to 24:386/392 of P21549

query
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R36 (≠ N17) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
G41 (≠ R22) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; associated in cis with L-11 and M-340; results in loss of protein stability; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; partial mitochondrial mistargeting; intraperoxisomal protein aggregation seen; dbSNP:rs121908523; to V: in HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177168
G47 (≠ N28) to R: in HP1; associated in cis with L-11 and M-340; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; reduced expression levels; reduced pyridoxal phosphate binding; reduced dimerization; reduced thermostability; increased propensity to aggregation; increased susceptibility to proteolytic degradation within the N-terminal region; mitochondrial mistargeting; exposure to pyridoxine can rescue the functionality by partially preventing aggregation and degradation and by redirecting all the protein to the peroxisome; dbSNP:rs180177173
G82 (= G63) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
W108 (≠ F89) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
A112 (≠ F93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
L150 (≠ Y132) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
F152 (≠ T134) to I: in HP1; associated in cis with L-11 and M-340; results in protein destabilization; no loss of dimerization; decreased alanine--glyoxylate aminotransferase activity; loss of alanine--glyoxylate aminotransferase activity when associated with L-11 and M-340; mitochondrial mistargeting when associated with L-11 and M-340; dbSNP:rs121908524
G156 (≠ C138) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
S158 (≠ T140) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
G161 (= G143) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227; to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; loss of dimerization; dbSNP:rs180177227; to S: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227
L166 (≠ V148) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
G170 (≠ C152) to R: in HP1; associated in cis with L-11 and M-340; decrease in alanine--glyoxylate aminotransferase activity; loss of dimerization; partial loss of protein stability but protein stability increases in the presence of pyridoxal phosphate; causes protein aggregation; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; results in mitochondrial mistargeting when associated with L-11 and M-340; dbSNP:rs121908529
C173 (≠ L155) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
D183 (= D165) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
S187 (≠ A169) to F: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization but improved dimerization in the presence of pyridoxal phosphate; decreased protein stability; dbSNP:rs180177238
I202 (= I184) to N: in HP1; uncertain significance; dbSNP:rs536352238
S205 (≠ G187) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
K209 (= K191) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
S218 (≠ T200) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
R233 (= R215) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
I244 (≠ L226) to T: in HP1; associated in cis with L-11 and M-340; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity in vitro; no loss of dimerization; partial mitochondrial mistargeting; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; dbSNP:rs121908525
C253 (vs. gap) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
I279 (= I257) to T: in dbSNP:rs140992177
A280 (≠ L258) to V: in dbSNP:rs73106685
V326 (= V300) to I: in dbSNP:rs115057148
I340 (≠ K314) to M: in allele minor; associated in cis with L-11; no effect on alanine--glyoxylate aminotransferase activity in vitro; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with L-11; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and I-152; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and R-170; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and T-244; results in mitochondrial mistargeting when associated with L-11 and R-170; dbSNP:rs4426527

Sites not aligning to the query:

9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
11 P → L: in allele minor; associated in cis with M-340; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with I-152 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with R-170 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with T-244 and M-340; causes mitochondrial mistargeting when associated with R-170 and M-340; dbSNP:rs34116584

6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
28% identity, 94% coverage: 5:360/377 of query aligns to 19:381/384 of 6rv0A

query
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binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: S76 (≠ E62), G77 (= G63), H78 (≠ I64), W103 (≠ F89), D178 (= D165), V180 (= V167), A181 (≠ S168), K204 (= K191)

1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
28% identity, 94% coverage: 5:360/377 of query aligns to 21:383/387 of 1j04A

query
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E

L

K

Q

T

M

T

I

N

G

P

-

D

S

L

M

D

S

M

K

D

D

F

M

Y

Y

D

Q

F

I

Y

M

K

D

K

E

T

I

T

K

E

E

K

G

I

I

G

Q

K

Y

F

V

L

F

K

Q

T

T

K

R

N

N

E

P

V

L

R

T

-

L

I

V

L

I

S

S

G

G

E

S

G

G

I

H

L

C

G

A

L

L

E

E

A

A

C

L

A

V

S

N

L

V

T

L

E

E

K

P

G

G

D

D

R

S

V

F

L

L

V

V

I

G

E

A

N

N

G

G

I

I

F

W

G

G

E

Q

G

R

F

A

A

V

D

D

F

I

V

G

K

E

M

R

Y

I

G

G

G

A

E

R

P

V

F

H

F

P

F

M

R

T

G

K

N

D

K

P

K

G

C

G

S

H

I

Y

N

T

I

L

E

Q

E

E

L

V

E

E

R

E

F

G

L

L

D

A

S

Q

D

H

S

K

E

P

F

V

K

-

Y

L

A

L

T

F

V

L

V

T

H

H

C

G

D

E

T

S

P

S

S

T

G

G

M

V

L

L

N

Q

N

P

V

L

G

D

A

G

I

F

C

R

K

E

L

L

L

C

K

H

K

R

K

Y

G

K

I

C

M

L

T

L

V

L

V

V

D

D

S

S

V

V

S

A

A

S

M

L

G

G

E

T

E

P

L

L

K

Y

V

M

D

D

E

R

W

Q

D

G

I

I

D

D

I

I

V

L

I

Y

G

S

G

G

S

S

Q

Q

K

K

C

A

I

L

S

N

A

A

P

P

G

G

L

T

T

S

I

L

V

I

S

S

I

F

S

S

D

D

D

K

A

A

F

K

S

K

A

K

M

M

K

Y

N

S

R

R

K

K

T

T

P

K

I

P

A

F

S

S

F

F

Y

Y

C

L

N

D

L

I

L

K

V

W

W

L

E

A

D

N

Y

F

Y

W

-

G

-

C

-

D

N

Q

K

P

K

R

W

M

F

Y

P

H

Y

H

T

T

P

I

P

P

I

V

S

I

D

S

I

L

V

Y

A

S

L

L

R

R

K

E

A

S

V

L

E

A

N

L

I

I

L

A

E

E

E

Q

-

G

-

L

K

E

D

N

I

S

I

W

A

R

R

Q

H

H

D

R

K

E

I

A

A

A

S

A

A

Y

T

L

R

H

A

G

A

R

V

L

V

Q

L

A

G

L

G

G

L

L

E

Q

I

L

Y

F

I

V

E

K

D

D

G

P

F

A

S

L

N

R

-

L

-

P

T

T

V

V

T

T

V

T

I

V

K

A

V

V

P

P

H

A

G

G

M

Y

N

D

D

W

D

R

K

D

I

I

L

V

S

S

Y

Y

M

V

K

I

E

D

N

H

Y

F

N

D

V

I

M

E

I

I

A

M

G

G

A

G

F

L

D

G

Y

P

L

S

K

T

G

G

K

K

V

V

L

L

R
|
R

I

I

G

G

H

L

M

L

G

G

E

C

N

N

A

A

Y

T

V

R

D

E

K

N

V

V

S

D

Y

R

T

V

L

T

F

E

A

A

L

L

Q

R

R

A

T

A

L

L

E

Q

H

H

binding (aminooxy)acetic acid: P25 (= P9), R357 (= R334)

1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
28% identity, 94% coverage: 5:360/377 of query aligns to 21:381/385 of 1h0cA

query
sites
1h0cA

I

L

M

L

T

G

P
|
P

G
|
G

P

P

T

S

S

N

V

L

R

P

E

P

N

R

V

I

R

M

L

A

S

A

R

G

A

G

E

L

K

Q

T

M

T

I

N

G

P

-

D

S

L

M

D

S

M

K

D

D

F

M

Y

Y

D

Q

F

I

Y

M

K

D

K

E

T

I

T

K

E

E

K

G

I

I

G

Q

K

Y

F

V

L

F

K

Q

T

T

K

R

N

N

E

P

V

L

R

T

-

L

I

V

L

I

S

S

G

G

E
x
S

G
|
G

I
x
H

L

C

G

A

L

L

E

E

A

A

C

L

A

V

S

N

L

V

T

L

E

E

K

P

G

G

D

D

R

S

V

F

L

L

V

V

I

G

E

A

N

N

G

G

I

I

F
x
W

G

G

E

Q

G

R

F

A

A

V

D

D

F

I

V

G

K

E

M

R

Y

I

G

G

G

V

E

H

P

P

F

M

F

-

R

T

G

K

N

D

K

P

K

G

C

G

S

H

I

Y

N

T

I

L

E

Q

E

E

L

V

E

E

R

E

F

G

L

L

D

A

S

Q

D

H

S

K

E

P

F

V

K

-

Y

L

A

L

T

F

V

L

V

T

H

H

C

G

D

E

T
x
S

P

S

S

T

G

G

M

V

L

L

N

Q

N

P

V

L

G

D

A

G

I

F

C

G

K

E

L

L

L

C

K

H

K

R

K

Y

G

K

I

C

M

L

T

L

V

L

V

V

D
|
D

S

S

V
|
V

S

A

A

S

M

L

G

G

E

T

E

P

L

L

K

Y

V

M

D

D

E

R

W

Q

D

G

I

I

D

D

I

I

V

L

I

Y

G

S

G

G

S

S

Q

Q

K
|
K

C

A

I

L

S

N

A

A

P

P

G

G

L

T

T

S

I

L

V

I

S

S

I

F

S

S

D

D

D

K

A

A

F

K

S

K

A

K

M

M

K

Y

N

S

R

R

K

K

T

T

P

K

I

P

A

F

S

S

F

F

Y

Y

C

L

N

D

L

I

L

K

V

W

W

L

E

A

D

N

Y

F

Y

W

-

G

-

C

-

D

N

Q

K

P

K

R

W

M

F

Y

P

H

Y

H

T

T

P

I

P

P

I

V

S

I

D

S

I

L

V

Y

A

S

L

L

R

R

K

E

A

S

V

L

E

A

N

L

I

I

L

A

E

E

E

Q

-

G

-

L

K

E

D

N

I

S

I

W

A

R

R

Q

H

H

D

R

K

E

I

A

A

A

S

A

A

Y

T

L

R

H

A

G

A

R

V

L

V

Q

L

A

G

L

G

G

L

L

E

Q

I

L

Y

F

I

V

E

K

D

D

G

P

F

A

S

L

N

R

-

L

-

P

T

T

V

V

T

T

V

T

I

V

K

A

V

V

P

P

H

A

G

G

M

Y

N

D

D

W

D

R

K

D

I

I

L

V

S

S

Y

Y

M

V

K

I

E

D

N

H

Y

F

N

D

V

I

M

E

I

I

A

M

G

G

A

G

F
x
L

D

G

Y

P

L

S

K

T

G

G

K

K

V

V

L

L

R
|
R

I

I

G

G

H

L

M

L

G

G

E

C

N

N

A

A

Y

T

V

R

D

E

K

N

V

V

S

D

Y

R

T

V

L

T

F

E

A

A

L

L

Q

R

R

A

T

A

L

L

E

Q

H

H

binding (aminooxy)acetic acid: P25 (= P9), G26 (= G10), L346 (≠ F325), R355 (= R334)
binding pyridoxal-5'-phosphate: S78 (≠ E62), G79 (= G63), H80 (≠ I64), W105 (≠ F89), S153 (≠ T140), D178 (= D165), V180 (= V167), K204 (= K191)

Sites not aligning to the query:

binding pyridoxal-5'-phosphate: 385

Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
29% identity, 94% coverage: 5:358/377 of query aligns to 21:380/393 of Q3LSM4

query
sites
Q3LSM4

I

L

M

M

T

G

P

P

G

G

P

P

T

S

S

N

V

A

R

P

E

Q

N

R

V

V

R

-

L

L

S

D

R

A

A

M

E

S

K

R

T

P

T

I

N

L

P

G

D

H

L

L

D

H

M

P

D

E

F

T

Y

L

D

K

F

I

Y

M

K

D

T

I

T

K

E

E

K

G

I

V

G

R

K

Y

F

L

L

F

K

Q

T

T

K

N

N

N

-

I

E

A

V

T

R

F

I

C

L

L

S

S

G

A

E
x
S

G
|
G

I
x
H

L

G

G

G

L

M

E

E

A

A

A

T

C

L

A

C

S

N

L

L

T

L

E

E

K

D

G

G

D

D

R

V

V

I

L

L

V

I

I

G

E

H

N

T

G

G

I

H

F

W

G

G

E

D

G

R

F

S

A

A

D

D

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

R

K

G

S

N

K

K

V

K

G

C

Q

S

S

I

L

N

S

I

L

E

D

E

E

L

I

-

R

E

D

R

A

F

L

L

L

D

I

S

H

D

K

S

P

E

S

F

V

K

L

Y

F

A

L

T

T

V

-

H

Q

C

G

D

D

T
x
S

P

S

S

T

G

G

M

V

L

L

N

Q

N

G

V

L

G

E

A

G

I

V

C

G

K

A

L

L

L

C

K

H

K

Q

K

H

G

N

I

C

M

L

T

L

V

I

V

V

D

D

S

T

V

V

S

A

A

S

M

L

G

G

E

A

E

P

L

M

K

F

V

M

D

D

E

R

W

W

D

E

I

I

D

D

I

A

V

M

I

Y

G

T

G

G

S

S

Q
|
Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

V

S

S

I

F

S

S

D

H

D

R

A

A

F

V

S

E

A

R

M

Y

K

K

N

R

R

R

K

N

T

T

P

K

I

V

A

K

S

V

F

Y

Y

Y

C

W

N

D

L

M

L

S

V

L

W

V

E

G

D

D

Y

Y

Y

W

N

G

-

C

-

F

-

G

-

R

K

P

K

R

W

I

F
x
Y

P

H

Y

H

T
|
T

P

I

P

S

I

S

S

T

D

L

I

L

V

Y

A

G

L

L

R

R

K

E

A

A

V

I

E

A

N

M

I

A

L

C

E

E

-

G

-

L

K

P

D

A

I

L

I

I

A

A

R

R

H

H

D

E

K

D

I

C

A

A

S

K

A

R

T

L

R

Y

A

R

A

G

V

L

V

Q

L

D

G

A

G

G

L

F

E

E

I

L

Y

Y

I

A

E

D

-

P

-

K

D

D

G

R

F

L

S

S

N

-

T

T

V

V

T

T

V

T

I

I

K

K

V

V

P

P

H

Q

G

G

M

V

N

D

D

W

D

L

K

K

I

A

L

A

S

Q

Y

Y

M

A

K

M

E

K

N

T

Y

Y

N

L

V

V

M

E

I

I

A

S

G

G

A

G

F

L

D

G

Y

P

L

T

K

A

G

G

K

Q

V

V

L

F

R
|
R

I

I

G

G

H

L

M

M

G

G

E

Q

N

N

A

A

Y

T

V

T

D

E

K

R

V

V

S

D

Y

R

T

V

L

L

F

Q

A

V

L

F

Q

Q

R

E

T

A

L

V

SGH 78:80 (≠ EGI 62:64) binding in other chain
S155 (≠ T140) binding glyoxylate; binding L-alanine
Q205 (= Q190) binding in other chain
K206 (= K191) modified: N6-(pyridoxal phosphate)lysine
Y257 (≠ F238) binding pyridoxal 5'-phosphate
T260 (= T241) binding pyridoxal 5'-phosphate
R356 (= R334) binding glyoxylate

2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
29% identity, 94% coverage: 5:358/377 of query aligns to 21:380/385 of 2huuA

query
sites
2huuA

I

L

M

M

T

G

P
|
P

G

G

P

P

T

S

S

N

V

A

R

P

E

Q

N

R

V

V

R

-

L

L

S

D

R

A

A

M

E

S

K

R

T

P

T

I

N

L

P

G

D
x
H

L

L

D

H

M

P

D

E

F

T

Y

L

D

K

F

I

Y

M

K

D

T

I

T

K

E

E

K

G

I

V

G

R

K

Y

F

L

L

F

K

Q

T

T

K

N

N

N

-

I

E

A

V

T

R

F

I

C

L

L

S

S

G

A

E

S

G

G

I

H

L

G

G

G

L

M

E

E

A

A

A

T

C

L

A

C

S

N

L

L

T

L

E

E

K

D

G

G

D

D

R

V

V

I

L

L

V

I

I

G

E

H

N

T

G

G

I

H

F

W

G

G

E

D

G

R

F

S

A

A

D

D

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

R

K

G

S

N

K

K

V

K

G

C

Q

S

S

I

L

N

S

I

L

E

D

E

E

L

I

-

R

E

D

R

A

F

L

L

L

D

I

S

H

D

K

S

P

E

S

F

V

K

L

Y

F

A

L

T

T

V

-

H

Q

C

G

D

D

T
x
S

P

S

S

T

G

G

M

V

L

L

N

Q

N

G

V

L

G

E

A

G

I

V

C

G

K

A

L

L

L

C

K

H

K

Q

K

H

G

N

I

C

M

L

T

L

V

I

V

V

D

D

S

T

V

V

S

A

A

S

M

L

G

G

E

A

E

P

L

M

K

F

V

M

D

D

E

R

W

W

D

E

I

I

D

D

I

A

V

M

I

Y

G

T

G

G

S

S

Q

Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

V

S

S

I

F

S

S

D

H

D

R

A

A

F

V

S

E

A

R

M

Y

K

K

N

R

R

R

K

N

T

T

P

K

I

V

A

K

S

V

F

Y

Y

Y

C

W

N

D

L

M

L

S

V

L

W

V

E

G

D

D

Y

Y

Y

W

N

G

-

C

-

F

-

G

-

R

K

P

K

R

W

I

F
x
Y

P

H

Y

H

T

T

P

I

P

S

I

S

S

T

D

L

I

L

V

Y

A

G

L

L

R

R

K

E

A

A

V

I

E

A

N

M

I

A

L

C

E

E

-

G

-

L

K

P

D

A

I

L

I

I

A

A

R

R

H

H

D

E

K

D

I

C

A

A

S

K

A

R

T

L

R

Y

A

R

A

G

V

L

V

Q

L

D

G

A

G

G

L

F

E

E

I

L

Y

Y

I

A

E

D

-

P

-

K

D

D

G

R

F

L

S

S

N

-

T

T

V

V

T

T

V

T

I

I

K

K

V

V

P

P

H

Q

G

G

M

V

N

D

D

W

D

L

K

K

I

A

L

A

S

Q

Y

Y

M

A

K

M

E

K

N

T

Y

Y

N

L

V

V

M

E

I

I

A

S

G

G

A

G

F
x
L

D

G

Y

P

L

T

K

A

G

G

K

Q

V

V

L

F

R
|
R

I

I

G

G

H

L

M

M

G

G

E

Q

N

N

A

A

Y

T

V

T

D

E

K

R

V

V

S

D

Y

R

T

V

L

L

F

Q

A

V

L

F

Q

Q

R

E

T

A

L

V

binding 1-butanol: H45 (≠ D30), Y257 (≠ F238)
binding alanine: P25 (= P9), S155 (≠ T140), K206 (= K191), L347 (≠ F325), R356 (= R334)

2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
29% identity, 94% coverage: 5:358/377 of query aligns to 21:380/385 of 2huiA

query
sites
2huiA

I

L

M

M

T

G

P
|
P

G

G

P

P

T

S

S

N

V

A

R

P

E

Q

N

R

V

V

R

-

L

L

S

D

R

A

A

M

E

S

K

R

T

P

T

I

N

L

P

G

D

H

L

L

D

H

M

P

D

E

F

T

Y

L

D

K

F

I

Y

M

K

D

T

I

T

K

E

E

K

G

I

V

G

R

K

Y

F

L

L

F

K

Q

T

T

K

N

N

N

-

I

E

A

V

T

R

F

I

C

L

L

S

S

G

A

E

S

G

G

I

H

L

G

G

G

L

M

E

E

A

A

A

T

C

L

A

C

S

N

L

L

T

L

E

E

K

D

G

G

D

D

R

V

V

I

L

L

V

I

I

G

E

H

N

T

G

G

I

H

F

W

G

G

E

D

G

R

F

S

A

A

D

D

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

R

K

G

S

N

K

K

V

K

G

C

Q

S

S

I

L

N

S

I

L

E

D

E

E

L

I

-

R

E

D

R

A

F

L

L

L

D

I

S

H

D

K

S

P

E

S

F

V

K

L

Y

F

A

L

T

T

V

-

H

Q

C

G

D

D

T
x
S

P

S

S

T

G

G

M

V

L

L

N

Q

N

G

V

L

G

E

A

G

I

V

C

G

K

A

L

L

L

C

K

H

K

Q

K

H

G

N

I

C

M

L

T

L

V

I

V

V

D

D

S

T

V

V

S

A

A

S

M

L

G

G

E

A

E

P

L

M

K

F

V

M

D

D

E

R

W

W

D

E

I

I

D

D

I

A

V

M

I

Y

G

T

G

G

S

S

Q

Q

K
|
K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

V

S

S

I

F

S

S

D

H

D

R

A

A

F

V

S

E

A

R

M

Y

K

K

N

R

R

R

K

N

T

T

P

K

I

V

A

K

S

V

F

Y

Y

Y

C

W

N

D

L

M

L

S

V

L

W

V

E

G

D

D

Y

Y

Y

W

N

G

-

C

-

F

-

G

-

R

K

P

K

R

W

I

F

Y

P

H

Y

H

T

T

P

I

P

S

I

S

S

T

D

L

I

L

V

Y

A

G

L

L

R

R

K

E

A

A

V

I

E

A

N

M

I

A

L

C

E

E

-

G

-

L

K

P

D

A

I

L

I

I

A

A

R

R

H

H

D

E

K

D

I

C

A

A

S

K

A

R

T

L

R

Y

A

R

A

G

V

L

V

Q

L

D

G

A

G

G

L

F

E

E

I

L

Y

Y

I

A

E

D

-

P

-

K

D

D

G

R

F

L

S

S

N

-

T

T

V

V

T

T

V

T

I

I

K

K

V

V

P

P

H

Q

G

G

M

V

N

D

D

W

D

L

K

K

I

A

L

A

S

Q

Y

Y

M

A

K

M

E

K

N

T

Y

Y

N

L

V

V

M

E

I

I

A

S

G

G

A

G

F

L

D

G

Y

P

L

T

K

A

G

G

K

Q

V

V

L

F

R
|
R

I

I

G

G

H

L

M

M

G

G

E

Q

N

N

A

A

Y

T

V

T

D

E

K

R

V

V

S

D

Y

R

T

V

L

L

F

Q

A

V

L

F

Q

Q

R

E

T

A

L

V

binding glyoxylic acid: P25 (= P9), S155 (≠ T140), K206 (= K191), R356 (= R334)

2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
29% identity, 94% coverage: 5:358/377 of query aligns to 21:380/385 of 2hufA

query
sites
2hufA

I

L

M

M

T

G

P

P

G

G

P

P

T

S

S

N

V

A

R

P

E

Q

N

R

V

V

R

-

L

L

S

D

R

A

A

M

E

S

K

R

T

P

T

I

N

L

P

G

D
x
H

L

L

D

H

M

P

D

E

F

T

Y

L

D

K

F

I

Y

M

K

D

T

I

T

K

E

E

K

G

I

V

G

R

K

Y

F

L

L

F

K

Q

T

T

K

N

N

N

-

I

E

A

V

T

R

F

I

C

L

L

S

S

G

A

E

S

G

G

I

H

L

G

G

G

L

M

E

E

A

A

A

T

C

L

A

C

S

N

L

L

T

L

E

E

K

D

G

G

D

D

R

V

V

I

L

L

V

I

I

G

E

H

N

T

G

G

I

H

F

W

G

G

E

D

G

R

F

S

A

A

D

D

F

M

V

A

K

T

M

R

Y

Y

G

G

G

A

E

D

P

V

F

R

F

V

R

K

G

S

N

K

K

V

K

G

C

Q

S

S

I

L

N

S

I

L

E

D

E

E

L

I

-

R

E

D

R

A

F

L

L

L

D

I

S

H

D

K

S

P

E

S

F

V

K

L

Y

F

A

L

T

T

V

-

H

Q

C

G

D

D

T
x
S

P

S

S

T

G

G

M

V

L

L

N

Q

N

G

V

L

G

E

A

G

I

V

C

G

K

A

L

L

L

C

K

H

K

Q

K

H

G

N

I

C

M

L

T

L

V

I

V

V

D

D

S

T

V

V

S

A

A

S

M

L

G

G

E

A

E

P

L

M

K

F

V

M

D

D

E

R

W

W

D

E

I

I

D

D

I

A

V

M

I

Y

G

T

G

G

S

S

Q

Q

K

K

C

V

I

L

S

G

A

A

P

P

G

G

L

I

T

T

I

P

V

V

S

S

I

F

S

S

D

H

D

R

A

A

F

V

S

E

A

R

M

Y

K

K

N

R

R

R

K

N

T

T

P

K

I

V

A

K

S

V

F

Y

Y

Y

C

W

N

D

L

M

L

S

V

L

W

V

E

G

D

D

Y

Y

Y

W

N

G

-

C

-

F

-

G

-

R

K

P

K

R

W

I

F
x
Y

P

H

Y

H

T

T

P

I

P

S

I

S

S

T

D

L

I

L

V

Y

A

G

L

L

R

R

K

E

A

A

V

I

E

A

N

M

I

A

L

C

E

E

-

G

-

L

K

P

D

A

I

L

I

I

A

A

R

R

H

H

D

E

K

D

I

C

A

A

S

K

A

R

T

L

R

Y

A

R

A

G

V

L

V

Q

L

D

G

A

G

G

L

F

E

E

I

L

Y

Y

I

A

E

D

-

P

-

K

D

D

G

R

F

L

S

S

N

-

T

T

V

V

T

T

V

T

I

I

K

K

V

V

P

P

H

Q

G

G

M

V

N

D

D

W

D

L

K

K

I

A

L

A

S

Q

Y

Y

M

A

K

M

E

K

N

T

Y

Y

N

L

V

V

M

E

I

I

A

S

G

G

A

G

F

L

D

G

Y

P

L

T

K

A

G

G

K

Q

V

V

L

F

R
|
R

I

I

G

G

H

L

M

M

G

G

E

Q

N

N

A

A

Y

T

V

T

D

E

K

R

V

V

S

D

Y

R

T

V

L

L

F

Q

A

V

L

F

Q

Q

R

E

T

A

L

V

binding 1-butanol: H45 (≠ D30), S155 (≠ T140), Y257 (≠ F238), R356 (= R334)

O32148 (S)-ureidoglycine--glyoxylate transaminase; UGXT; (S)-ureidoglycine--glyoxylate aminotransferase; Purine catabolism protein PucG; EC 2.6.1.112 from Bacillus subtilis (strain 168) (see paper)
28% identity, 94% coverage: 6:358/377 of query aligns to 14:387/416 of O32148

query
sites
O32148

I

I

M

M

T

T

P

P

G

G

P

P

T

V

S

E

V

V

R

D

E

P

N

R

V

V

R

-

L

L

S

R

R

V

A

M

E

S

K

T

T

P

T

V

N

V

P

G

D
x
Q

L

F

D

D

M

P

D

A

F

F

Y

T

D

G

F

I

Y

M

K

N

K

E

T

T

T

M

E

E

K

M

I

L

G

R

K

E

F

L

L

F

K

Q

T

T

K

K

N

N

E

R

-

W

V

A

R

Y

I

P

L

I

S

D

G

G

E

T

G

S

I

R

L

A

G

G

L

I

E

E

A

A

A

V

C

L

A

A

S

S

L

V

T

I

E

E

K

P

G

E

D

D

R

D

V

V

L

L

V

I

I

P

E

I

N

Y

G

G

I

R

F

F

G

G

E

Y

G

L

F

L

A

T

D

E

F

I

V

A

K

E

M

R

Y

Y

G

G

G

A

E

N

P

V

F

H

F

M

F

L

R

E

G

C

N

E

K

W

K

G

C

T

S

V

I

F

N

D

I

P

E

E

E

D

L

I

E

I

R

R

F

E

L

I

D

K

S

K

D

-

S

V

E

K

F

P

K

K

Y

I

A

V

T

A

V

M

V

V

H

H

C

G

D

E

T

T

P

S

S

T

G

G

M

R

L

I

N

H

N

P

V

L

G

K

A

A

I

I

C

G

K

E

L

A

L

C

K

R

K

T

K

E

G

D

I

A

M

L

T

F

V

I

V

V

D

D

S

A

V

V

S

A

A

T

M

I

G

G

E

C

E

E

L

V

K

K

V

V

D

D

E

E

W

W

D

K

I

I

D

D

I

A

V

A

I

I

G

G

S

T

Q

Q

K
|
K

C

C

I

L

S

S

A

V

P

P

P

S

G

G

L

M

T

A

I

P

V

I

S

T

I

Y

S

N

D

E

D

R

A

V

F

A

S

D

A

V

M

I

K

A

N

A

R

R

K

K

-

K

-

V

-

E

-

R

-

G

-

I

-

A

-

T

-

Q

-

A

-

D

-

R

-

A

-

L

-

S

-

G

-

N

T

R

P

P

I

I

A

T

S

S

F

N

Y

Y

C

F

N

D

L

L

L

S

V

Q

W

L

E

E

D

D

Y

Y

Y

W

N

S

K

E

K

R

W

R

F

L

-
x
N

P

H

Y

H

T

T

P

E

P

A

I

T

S

T

D

M

I

L

V

Y

A

A

L

L

R

R

K

E

A

G

V

V

E

R

N

L

I

V

L

L

E

E

-

G

-

L

K

E

D

T

I

R

I

F

A

E

R

R

H

H

D

R

K

H

I

H

A

E

S

A

A

A

T

L

R

A

A

A

A

G

V

I

V

K

L

A

G

M

G

G

L

L

E

R

I

L

Y

F

I

G

E

D

D

D

G

S

F

C

S

K

-

M

N

P

T

V

V

V

T

T

V

C

I

V

K

E

V

I

P

P

H

G

G

G

M

I

N

D

D

G

D

E

K

S

I

V

L

R

S

D

Y

M

M

L

K

L

E

A

N

Q

Y

F

N

G

V

I

M

E

I

I

A

A

G

S

A

S

F

F

D

G

Y

P

L

L

K

A

G

G

K

K

V

I

L

W

R

R

I

I

G

G

H

T

M

M

G

G

E

Y

N

S

A

C

Y

R

V

K

D

E

K

N

V

V

S

L

Y

F

T

V

L

L

F

A

A

G

L

L

Q

E

R

A

T

V

L

L

Q37 (≠ D30) mutation to H: 5-fold decrease in transamination activity.
K198 (= K191) modified: N6-(pyridoxal phosphate)lysine
N264 (vs. gap) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.

Query Sequence

>WP_010963544.1 NCBI__GCF_000008765.1:WP_010963544.1
MKVPIIMTPGPTSVRENVRLSRAEKTTNPDLDMDFYDFYKKTTEKIGKFLKTKNEVRILS
GEGILGLEAACASLTEKGDRVLVIENGIFGEGFADFVKMYGGEPFFFRGNKKCSINIEEL
ERFLDSDSEFKYATVVHCDTPSGMLNNVGAICKLLKKKGIMTVVDSVSAMGGEELKVDEW
DIDIVIGGSQKCISAPPGLTIVSISDDAFSAMKNRKTPIASFYCNLLVWEDYYNKKWFPY
TPPISDIVALRKAVENILEEKDIIARHDKIASATRAAVVLGGLEIYIEDGFSNTVTVIKV
PHGMNDDKILSYMKENYNVMIAGAFDYLKGKVLRIGHMGENAYVDKVSYTLFALQRTLEH
YGFEFKRDMVKVFLEKV

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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