SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012968296.1 NCBI__GCF_000025465.1:WP_012968296.1 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)

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
31% identity, 96% coverage: 1:202/210 of query aligns to 1:200/207 of 4ij6A

query
sites
4ij6A

M

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x
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active site: R8 (= R8), A9 (≠ H9), N15 (= N15), R58 (= R60), E82 (= E84), H150 (= H152)
binding phosphoserine: R8 (= R8), Q21 (= Q21), R58 (= R60), E82 (= E84), H85 (≠ F87), H150 (= H152), T151 (≠ G153)

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
30% identity, 96% coverage: 1:202/210 of query aligns to 1:196/196 of 6m1xC

query
sites
6m1xC

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binding 3-phosphoglyceric acid: R8 (= R8), H9 (= H9), Q21 (= Q21), R57 (= R60), E79 (= E84), H146 (= H152), G147 (= G153)

5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
30% identity, 97% coverage: 1:203/210 of query aligns to 1:197/198 of 5zr2C

query
sites
5zr2C

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binding phosphoserine: R8 (= R8), Q21 (= Q21), G22 (= G22), R57 (= R60), E79 (= E84), H146 (= H152), G147 (= G153)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
28% identity, 79% coverage: 6:171/210 of query aligns to 6:169/207 of 1h2fA

query
sites
1h2fA

L

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active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R60), E82 (= E84), H150 (= H152)
binding phosphate ion: G142 (≠ H144), E143 (≠ Q145)
binding trivanadate: R8 (= R8), H9 (= H9), N15 (= N15), Q21 (= Q21), R58 (= R60), E82 (= E84), H150 (= H152), G151 (= G153), V152 (≠ Q154)

Sites not aligning to the query:

binding phosphate ion: 1, 2, 3

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
28% identity, 79% coverage: 6:171/210 of query aligns to 6:169/207 of 1h2eA

query
sites
1h2eA

L

L

V

T

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H

A

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active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R60), E82 (= E84), H150 (= H152)
binding phosphate ion: R8 (= R8), H9 (= H9), R58 (= R60), E82 (= E84), H150 (= H152)

P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
23% identity, 90% coverage: 4:193/210 of query aligns to 10:205/211 of P36623

query
sites
P36623

V

L

I

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T

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T37 (≠ R31) modified: Phosphothreonine
S62 (= S56) modified: Phosphoserine
Y96 (≠ F87) modified: Phosphotyrosine
S166 (≠ V155) modified: Phosphoserine

Q7ZVE3 Fructose-2,6-bisphosphatase TIGAR B; TP53-induced glycolysis and apoptosis regulator B; EC 3.1.3.46 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
31% identity, 64% coverage: 4:138/210 of query aligns to 6:139/257 of Q7ZVE3

query
sites
Q7ZVE3

V

L

I

T

L

I

V

V

R

R

H
|
H

A

G

E

E

T

T

E

Q

W

Y

N

N

I

R

K

D

G

K

I

L

Q

Q

G

G

Q

Q

S

G

-

I

D

D

S

T

A

P

L

L

T

S

P

D

R

T

G

G

E

H

R

Q

Q

Q

T

A

S

A

A

A

L

-

A

A

A

G

F

R

A

Y

A

L

S

K

D

D

Y

L

R

H

V

F

D

T

C

N

V

V

Y

F

T

V

S

S

P

N

L

L

G

Q

R

R

A

A

W

I

Q

Q

M

T

G

A

Q

E

R

I

L

I

A

L

G

G

H

N

-

N

-

L

-

H

-

S

F

S

R

A

C

T

P

E

L

M

I

I

A

L

E

D

P

P

A

L

L

L

K

R

E

E

Q

R

A

G

F

F

G

G

Q

V

F

A

E

E

G

G

M

R

L

P

T

K

S

E

Q

H

L

L

M

K

Q

N

Q

M

R

-

P

-

H

-

D

-

A

A

H

N

A

A

L

A

F

G

T

Q

H

S

D

C

A

R

E

D

Y

Y

C

T

P

P

Q

G

G

G

E

E

S

T

L

L

A

E

Q

Q

A

V

T

K

R

T

R

R

V

F

T

K

G

M

F

F

I

L

H

K

N

S

L

L

H11 (= H9) active site, Tele-phosphohistidine intermediate

P00950 Phosphoglycerate mutase 1; PGAM 1; BPG-dependent PGAM 1; MPGM 1; Phosphoglyceromutase 1; EC 5.4.2.11 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 7 papers)
23% identity, 89% coverage: 1:186/210 of query aligns to 1:216/247 of P00950

query
sites
P00950

M
|
M

M

P

Q

K

V

L

I

V

L

L

V

V

R
|
R

H
|
H

A
x
G

E
x
Q

T
x
S

E
|
E

W
|
W

N
|
N

I

E

K

K

G

N

I

L

I

F

Q
x
T

G
|
G

Q

W

S

V

D

D

S

V

A

K

L

L

T

S

P

A

R

K

G

G

E

Q

R

Q

Q

E

T

A

S

A

A

R

L

A

L

G

A

E

A

L

F

L

A

K

A

E

S

K

D

K

Y

V

R

Y

V

P

D

D

C

V

V

L

Y

Y

T

T

S

S

P

K

L

L

G

S

R
|
R

A

A

W

I

Q

Q

M

T

G

A

Q

N

-

I

-

A

-

L

R

E

L

K

A

A

G

D

H

R

F

L

R

W

C

I

P

P

L

V

I

N

A

R

E

S

P

W

A

R

L

L

K

N

E
|
E

Q
x
R

A
x
H

F
x
Y

G

G

Q

D

F

L

E

Q

G

G

M

K

L

D

T
x
K

S

A

Q

E

L

T

M

L

Q

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-
x
R

-

S

-

F

-

D

-

V

-

P

R

P

P

P

H

I

D

D

A

A

H

S

A

S

L

P

F

F

T

S

H

Q

-

K

-

G

D

D

A

E

E

R

Y

Y

-

K

-

Y

-

V

-

D

-

P

-

N

C

V

P

L

P

P

Q

E

G

T

E

E

S

S

L

L

A

A

Q

L

A

V

T

I

R

D

R

R

V

L

T

L

G

P

F

Y

I

W

H

Q

N

D

L

V

-

I

-

A

P
x
K

E

D

A

L

T

L

E

S

H

G

Q

K

R

T

I

V

C

M

I

I

V

A

T

A

H
|
H

G
|
G

Q
x
N

V

S

S

L

Q

R

G

G

V

L

L

V

A

K

V

H

L

L

K

-

E

E

G

G

T

I

I

S

D

D

-

A

N

D

F

I

S

A

R

K

Y

L

A

N

H

I

P

P

N

T

A

G

S

I

Y

P

S

L

V

V

F

F

D

E

F

L

M1 (= M1) modified: Initiator methionine, Removed
8:15 (vs. 8:15, 63% identical) binding
H9 (= H9) active site, Tele-phosphohistidine intermediate
TG 21:22 (≠ QG 21:22) binding
R60 (= R60) binding
ERHY 87:90 (≠ EQAF 84:87) binding
K98 (≠ T95) binding
RR 114:115 (vs. gap) binding
K169 (≠ P139) mutation to P: Causes dissociation of the homotetramer to dimers at low concentrations.
H182 (= H152) mutation to A: Reduces kcat of the mutase reaction 10000-fold.
GN 183:184 (≠ GQ 153:154) binding

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
26% identity, 72% coverage: 3:153/210 of query aligns to 3:158/209 of 4qihA

query
sites
4qihA

Q

R

V

L

I

V

L

M

V

L

R
|
R

H
|
H

A

G

E

Q

T

T

E

D

W

Y

N

N

I

V

K

G

G

S

I

R

I

M

Q
|
Q

G

G

Q

Q

S

L

D

D

S

T

A

E

L

L

T

S

P

E

R

L

G

G

E

-

R

-

Q

R

T

T

S

Q

A

A

L

V

L

A

A

A

F

E

A

V

A

L

S

G

D

K

Y

R

R

Q

V

P

D

L

C

L

V

I

Y

V

T

S

S

S

P

D

L

L

G

R

R
|
R

A

A

W

Y

Q

D

M

T

G

A

Q

V

R

K

L

L

A

G

G

E

H

R

F

T

R

G

C

L

P

V

L

V

I

R

A

V

E

D

P

T

A

R

L

L

K

R

E
|
E

Q

T

A

H

F

L

G

G

Q

D

F

W

E

Q

G

G

M

L

L

T

T

H

S

A

Q

Q

L

I

M

D

Q

A

Q

D

R

A

P

P

H

-

D

G

A

A

H

R

A

L

L

A

F

W

T

R

H

E

D

D

A

A

E

T

Y

W

C

A

P

P

P

H

Q

G

G

G

E

E

S

S

L

R

A

V

Q

D

A

V

T

A

R

A

R

R

-

S

-

R

-

P

-

L

V

V

T

A

G

E

F

L

I

V

H

A

N

S

L

E

P

P

E

E

-

W

-

G

A

A

T

D

E

E

H

P

Q

D

R

R

-

P

I

V

C

V

I

L

V

V

T

A

H
|
H

G

G

active site: H9 (= H9), R58 (= R60), E82 (= E84)
binding vanadate ion: R8 (= R8), H9 (= H9), Q21 (= Q21), R58 (= R60), H157 (= H152)

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
23% identity, 88% coverage: 3:186/210 of query aligns to 2:215/240 of 1qhfA

query
sites
1qhfA

Q

K

V

L

I

V

L

L

V

V

R
|
R

H
|
H

A
x
G

E
x
Q

T
x
S

E

E

W

W

N
|
N

I

E

K

K

G

N

I

L

I

F

Q
x
T

G

G

Q

W

S

V

D

D

S

V

A

K

L

L

T

S

P

A

R

K

G

G

E

Q

R

Q

Q

E

T

A

S

A

A

R

L

A

L

G

A

E

A

L

F

L

A

K

A

E

S

K

D

K

Y

V

R

Y

V

P

D

D

C

V

V

L

Y

Y

T

T

S

S

P

K

L

L

G

S

R
|
R

A

A

W

I

Q

Q

M

T

G

A

Q

N

-

I

-

A

-

L

R

E

L

K

A

A

G

D

H

R

F

L

R

W

C

I

P

P

L

V

I

N

A

R

E

S

P

W

A

R

L

L

K

N

E
|
E

Q

R

A

H

F

Y

G

G

Q

D

F

L

E

Q

G

G

M

K

L

D

T

K

S

A

Q

E

L

T

M

L

Q

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-

R

-

S

-

F

-

D

-

V

-

P

R

P

P

P

H

I

D

D

A

A

H

S

A

S

L

P

F

F

T

S

H

Q

-

K

-

G

D

D

A

E

E

R

Y

Y

-

K

-

Y

-

V

-

D

-

P

-

N

C

V

P

L

P

P

Q

E

G

T

E

E

S

S

L

L

A

A

Q

L

A

V

T

I

R

D

R

R

V

L

T

L

G

P

F

Y

I

W

H

Q

N

D

L

V

-

I

-

A

P

K

E

D

A

L

T

L

E

S

H

G

Q

K

R

T

I

V

C

M

I

I

V

A

T

A

H
|
H

G

G

Q

N

V

S

S

L

Q

R

G

G

V

L

L

V

A

K

V

H

L

L

K

-

E

E

G

G

T

I

I

S

D

D

-

A

N

D

F

I

S

A

R

K

Y

L

A

N

H

I

P

P

N
x
T

A

G

S

I

Y

P

S

L

V

V

F

F

D

E

F

L

active site: H8 (= H9), R59 (= R60), E86 (= E84), H181 (= H152)
binding 3-phosphoglyceric acid: R7 (= R8), H8 (= H9), G9 (≠ A10), Q10 (≠ E11), S11 (≠ T12), N14 (= N15), T20 (≠ Q21), R59 (= R60), T207 (≠ N178)

P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
26% identity, 72% coverage: 3:153/210 of query aligns to 5:160/223 of P9WIC7

query
sites
P9WIC7

Q

R

V

L

I

V

L

M

V

L

R
|
R

H
|
H

A

G

E

Q

T

T

E

D

W

Y

N
|
N

I

V

K

G

G

S

I

R

I

M

Q

Q

G

G

Q

Q

S

L

D

D

S

T

A

E

L

L

T

S

P

E

R

L

G

G

E

-

R

-

Q

R

T

T

S

Q

A

A

L

V

L

A

A

A

F

E

A

V

A

L

S

G

D
x
K

Y

R

R

Q

V

P

D

L

C

L

V

I

Y

V

T

S

S

S

P

D

L

L

G

R

R
|
R

A

A

W

Y

Q

D

M

T

G

A

Q

V

R

K

L

L

A

G

G

E

H

R

F

T

R

G

C

L

P

V

L

V

I

R

A

V

E

D

P

T

A

R

L

L

K

R

E

E

Q

T

A

H

F

L

G

G

Q

D

F

W

E

Q

G

G

M

L

L

T

T

H

S

A

Q

Q

L

I

M

D

Q

A

Q

D

R

A

P

P

H

G

D

-

A

A

H

R

A

L

L

A

F

W

T

R

H

E

D

D

A

A

E

T

Y

W

C

A

P

P

P

H

Q

G

G

G

E

E

S

S

L

R

A

V

Q

D

A

V

T

A

R

A

R

R

-

S

-

R

-

P

-

L

V

V

T

A

G

E

F

L

I

V

H

A

N

S

L

E

P

P

E

E

-

W

-

G

A

A

T

D

E

E

H

P

Q

D

R

R

-

P

I

V

C

V

I

L

V

V

T

A

H
|
H

G

G

R10 (= R8) mutation to A: Loss of phosphatase activity.
H11 (= H9) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N15) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ D47) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R60) mutation to A: Loss of phosphatase activity.
H159 (= H152) mutation to A: About 5% of wild-type phosphatase activity.

Sites not aligning to the query:

209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
26% identity, 72% coverage: 3:153/210 of query aligns to 4:159/217 of 4pzaB

query
sites
4pzaB

Q

R

V

L

I

V

L

M

V

L

R
|
R

H
|
H

A

G

E

Q

T

T

E

D

W

Y

N

N

I

V

K

G

G

S

I

R

I

M

Q

Q

G

G

Q

Q

S

L

D

D

S

T

A

E

L

L

T

S

P

E

R

L

G

G

E

-

R

-

Q

R

T

T

S

Q

A

A

L

V

L

A

A

A

F

E

A

V

A

L

S

G

D

K

Y

R

R

Q

V

P

D

L

C

L

V

I

Y

V

T

S

S

S

P

D

L

L

G

R

R
|
R

A

A

W

Y

Q

D

M

T

G

A

Q

V

R

K

L

L

A

G

G

E

H

R

F

T

R

G

C

L

P

V

L

V

I

R

A

V

E

D

P

T

A

R

L

L

K

R

E
|
E

Q

T

A

H

F

L

G

G

Q

D

F

W

E

Q

G

G

M

L

L

T

T

H

S

A

Q

Q

L

I

M

D

Q

A

Q

D

R

A

P

P

H

-

D

G

A

A

H

R

A

L

L

A

F

W

T

R

H

E

D

D

A

A

E

T

Y

W

C

A

P

P

P

H

Q

G

G

G

E

E

S

S

L

R

A

V

Q

D

A

V

T

A

R

A

R

R

-

S

-

R

-

P

-

L

V

V

T

A

G

E

F

L

I

V

H

A

N

S

L

E

P

P

E

E

-

W

-

G

A

A

T

D

E

E

H

P

Q

D

R

R

-

P

I

V

C

V

I

L

V

V

T

A

H
|
H

G
|
G

active site: H10 (= H9), R59 (= R60), E83 (= E84)
binding phosphate ion: R9 (= R8), H10 (= H9), R59 (= R60), E83 (= E84), H158 (= H152), G159 (= G153)

5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
23% identity, 88% coverage: 3:186/210 of query aligns to 2:215/234 of 5pgmE

query
sites
5pgmE

Q

K

V

L

I

V

L

L

V

V

R

R

H
|
H

A

G

E

Q

T

S

E

E

W

W

N

N

I

E

K

K

G

N

I

L

I

F

Q

T

G

G

Q

W

S

V

D

D

S

V

A

K

L

L

T

S

P

A

R

K

G

G

E

Q

R

Q

Q

E

T

A

S

A

A

R

L

A

L

G

A

E

A

L

F

L

A

K

A

E

S

K

D

K

Y

V

R

Y

V

P

D

D

C

V

V

L

Y

Y

T

T

S

S

P

K

L

L

G

S

R
|
R

A

A

W

I

Q

Q

M

T

G

A

Q

N

-

I

-

A

-

L

R

E

L

K

A

A

G

D

H

R

F

L

R

W

C

I

P

P

L

V

I

N

A

R

E

S

P

W

A

R

L

L

K

N

E
|
E

Q

R

A

H

F

Y

G

G

Q

D

F

L

E

Q

G

G

M

K

L

D

T

K

S

A

Q

E

L

T

M

L

Q

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-

R

-

S

-

F

-

D

-

V

-

P

R

P

P

P

H

I

D

D

A

A

H

S

A

S

L

P

F

F

T

S

H

Q

-

K

-

G

D

D

A

E

E

R

Y

Y

-

K

-

Y

-

V

-

D

-

P

-

N

C

V

P

L

P

P

Q

E

G

T

E

E

S

S

L

L

A

A

Q

L

A

V

T

I

R

D

R

R

V

L

T

L

G

P

F

Y

I

W

H

Q

N

D

L

V

-

I

-

A

P

K

E

D

A

L

T

L

E

S

H

G

Q

K

R

T

I

V

C

M

I

I

V

A

T

A

H
|
H

G

G

Q

N

V

S

S

L

Q

R

G

G

V

L

L

V

A

K

V

H

L

L

K

-

E

E

G

G

T

I

I

S

D

D

-

A

N

D

F

I

S

A

R

K

Y

L

A

N

H

I

P

P

N

T

A

G

S

I

Y

P

S

L

V

V

F

F

D

E

F

L

active site: H8 (= H9), R59 (= R60), E86 (= E84), H181 (= H152)

Sites not aligning to the query:

binding alanine: 231, 234

1bifA 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bifunctional enzyme complexed with atp-g-s and phosphate (see paper)
31% identity, 75% coverage: 4:161/210 of query aligns to 215:363/432 of 1bifA

query
sites
1bifA

V

I

I

Y

L

L

V

C

R
|
R

H
|
H

A

G

E

E

T

S

E

E

W

L

N
|
N

I

L

K

K

G

G

I

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

P

A

G

L

L

T

S

P

P

R

R

G

G

E

-

R

R

Q

E

T

F

S

S

A

K

L

H

L

L

A

A

A

Q

F

F

A

I

A

S

S

D

D

Q

Y

N

R

I

V

K

D

D

C

L

-

K

V

V

Y

F

T

T

S

S

P

Q

L

M

G

K

R
|
R

A

T

W

I

Q

Q

M

T

G

A

Q

E

R

A

L

L

A

S

G

-

H

-

F

-

R

-

C

V

P

P

L

Y

I

E

A

Q

E

F

P

K

A

V

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

M

L

T

T
x
Y

S

E

Q

E

L

I

M

Q

Q

D

Q

H

R

Y

P

P

H

L

D

E

A

-

H

F

A

A

L

L

F
x
R

T

D

H

Q

D

D

A
x
K

-

Y

E

R

Y

Y

C

R

P

Y

P

P

Q

K

G

G

E

E

S

S

L
x
Y

A

E

Q

D

A

L

T

V

R

Q

R

R

V

L

T

E

G

P

F

V

I

I

H

M

N

E

L

L

P

-

E

-

A

-

T

E

E

R

H

Q

Q

E

R

N

I

V

C

L

I

V

V

I

T

C

H
|
H

G

Q

Q

A

V

V

S

M

Q
x
R

G

C

V

L

L

L

A

A

active site: R219 (= R8), H220 (= H9), N226 (= N15), R269 (= R60), E289 (= E84), H354 (= H152)
binding phosphate ion: R219 (= R8), H220 (= H9), R269 (= R60), E289 (= E84), Y300 (≠ T95), R314 (≠ F110), K318 (≠ A114), Y329 (≠ L124), H354 (= H152), R359 (≠ Q157)

Sites not aligning to the query:

binding phosphothiophosphoric acid-adenylate ester: 11, 12, 13, 14, 15, 16, 17, 131, 134, 136, 184, 210, 391

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
31% identity, 47% coverage: 5:102/210 of query aligns to 7:115/269 of 3lg2A

query
sites
3lg2A

I

I

L

I

V

V

R
|
R

H
|
H

A

G

E

Q

T

T

E

E

W

W

N

S

I

K

K

S

G

G

I

Q

I

Y

Q
x
T

G

G

Q

L

S

T

D

D

S

L

A

P

L

L

T

T

P

P

R

Y

G

G

E

E

R

G

Q

Q

T

M

-

L

S

R

A

T

L

G

L

E

A

S

A

V

F

F

A

R

A

N

S

N

D

Q

Y

F

-

L

-

N

-

P

-

D

R

N

V

I

D

T

C

Y

V

I

Y

F

T

T

S

S

P

P

L

R

G

L

R
|
R

A

A

W

R

Q

Q

-

T

-

V

-

D

-

L

M

V

G

L

Q

K

R

P

L

L

A

S

G

D

H

E

F

Q

R

R

C

A

P

K

L

I

-

R

-

V

I

V

A

V

E

D

P

D

A

D

L

L

K

R

E
|
E

Q

W

A

E

F

Y

G

G

Q

D

F

Y

E

E

G

G

M

M

L

L

T

T

S

R

Q

E

L

I

M

I

Q

E

Q

L

R

R

active site: H11 (= H9), R67 (= R60), E97 (= E84)
binding phosphate ion: R10 (= R8), H11 (= H9), T23 (≠ Q21), R67 (= R60), E97 (= E84)

Sites not aligning to the query:

binding phosphate ion: 174, 176, 179, 242, 266

P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 47% coverage: 5:102/210 of query aligns to 9:117/271 of P36136

query
sites
P36136

I

I

L

I

V

V

R
|
R

H
|
H

A

G

E

Q

T
|
T

E

E

W

W

N
x
S

I

K

K

S

G

G

I

Q

I
x
Y

Q
x
T

G

G

Q

L

S

T

D

D

S

L

A

P

L

L

T

T

P

P

R

Y

G

G

E

E

R

G

Q

Q

T

M

-

L

S

R

A

T

L

G

L

E

A

S

A

V

F

F

A

R

A

N

S

N

D

Q

Y

F

-

L

-

N

-

P

-

D

R

N

V

I

D

T

C

Y

V

I

Y

F

T

T

S
|
S

P

P

L

R

G

L

R
|
R

A

A

W

R

Q

Q

-

T

-

V

-

D

-

L

M

V

G

L

Q

K

R

P

L

L

A

S

G

D

H

E

F

Q

R

R

C

A

P

K

L

I

-

R

-

V

I

V

A

V

E

D

P

D

A

D

L

L

K

R

E
|
E

Q
x
W

A
x
E

F
x
Y

G

G

Q

D

F

Y

E

E

G

G

M

M

L

L

T

T

S

R

Q

E

L

I

M

I

Q

E

Q

L

R

R

R12 (= R8) binding ; mutation to A: Impairs catalytic activity.
H13 (= H9) active site, Tele-phosphohistidine intermediate; mutation to A: Impairs catalytic activity.
T16 (= T12) mutation to A: Impairs catalytic activity.
S19 (≠ N15) mutation to A: Leads to reduced substrate affinity.
Y24 (≠ I20) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ IQ 20:21) binding
S65 (= S56) mutation to A: Leads to low activity and reduced substrate affinity.
R69 (= R60) binding ; mutation to A: Leads to reduced substrate affinity.
E99 (= E84) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EQAF 84:87) binding
Y102 (≠ F87) mutation to A: Impairs catalytic activity.

Sites not aligning to the query:

131 W→A: Leads to reduced substrate affinity.
176 H→A: Impairs catalytic activity.
178 H→A: Leads to low activity and reduced substrate affinity.
181 binding ; R→A: Leads to reduced substrate affinity.
244 binding

P16118 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; 6PF-2-K/Fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/Fru-2,6-P2ase liver isozyme; EC 2.7.1.105; EC 3.1.3.46 from Homo sapiens (Human) (see paper)
28% identity, 80% coverage: 4:171/210 of query aligns to 254:412/471 of P16118

query
sites
P16118

V

I

I

Y

L

L

V

C

R

R

H

H

A

G

E

E

T

S

E

E

W

L

N

N

I

I

K

R

G

G

I

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

S

A

G

L

L

T

S

P

V

R

R

G

G

E

K

R

Q

Q

Y

T

A

S

Y

A

A

L

L

L

A

A

N

A

F

F

I

A

Q

A

S

S

Q

D

G

Y

I

R

S

V

S

D

L

C

K

V

V

Y

W

T

T

S

S

P

H

L

M

G

K

R

R

A

T

W

I

Q

Q

M

T

G

A

Q

E

R

A

L

L

A

G

G

-

H

-

F

-

R

-

C

V

P

P

L

Y

I

E

A

Q

E

W

P

K

A

A

L

L

K

N

E

E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

M

L

T

T

Y

S

E

Q

E

L

I

M

Q

Q

E

Q

H

R

Y

P

P

H

E

D

E

A

-

H

F

A

A

L

L

F

R

T

D

H

Q

D

D

A

K

-

Y

E

R

Y

Y

C

R

P

Y

P

P

Q

K

G

G

E

E

S

S

L

Y

A

E

Q

D

A

L

T

V

R

Q

R

R

V

L

T

E

G

P

F

V

I

I

H

M

N

E

L

L

P

-

E

-

A

-

T

E

E

R

H

Q

Q

E

R

N

I

V

C

L

I

V

V

I

T

C

H

H

G

Q

Q

A

V

V

S

M

Q

R

G

C

V

L

L

L

A

A

V

Y

L

F

K

L

E

D

G

K

T

S

I

S

D

D

N

E

F

L

Sites not aligning to the query:

49:57 binding
170:175 binding
430 binding

5y65C Phosphoglycerate mutase 1 complexed with a small molecule inhibitor kh2
22% identity, 77% coverage: 3:164/210 of query aligns to 3:196/239 of 5y65C

query
sites
5y65C

Q

K

V

L

I

V

L

L

V

I

R

R

H
|
H

A

G

E

E

T

S

E

A

W

W

N

N

I

L

K

E

G
x
N

I
x
R

I
x
F

Q

S

G

G

Q

W

S

Y

D

D

S

A

A

D

L

L

T

S

P

P

R

A

G

G

E

H

R

E

Q

E

T

A

S

K

A

R

L

G

A

Q

A

A

F

L

A

R

A

D

S

A

D

G

Y

Y

R

E

V

F

D

D

C

I

V

C

Y

F

T

T

S

S

P

V

L

Q

G

K

R
|
R

A

A

-

I

-

R

-

T

-

L

W

W

Q

T

M

V

G

L

Q

D

R

A

L

I

A

-

G

D

H

Q

F

M

R

W

C

L

P

P

L

V

I

V

A

R

E

T

P

W

A

R

L

L

K

N

E
|
E

Q
x
R

A

H

F

Y

G

G

Q

G

F

L

E

T

G

G

M

L

L

N

T
x
K

S

A

Q

E

L

T

-

A

-

K

-

H

-

G

-

E

-

A

-

Q

-

V

-

K

M

I

Q
x
W

Q
x
R

R

R

P

S

H

Y

D

D

A

V

-

P

-

M

-

E

-

P

-

D

-

H

-

P

-

F

H

Y

A

S

L

N

F

I

T

S

H

K

D

D

A

R

E

R

Y

Y

C

A

P

D

-

L

-

T

-

E

-

D

-

Q

-

L

P

P

Q

S

G

C

E

E

S

S

L

L

A

K

Q

D

A

T

T

I

R

A

R

R

V

A

T

L

G

P

F

F

I

W

H

N

N

E

-

E

-

I

L

V

P

P

E

Q

A

I

T

K

E

E

H

G

Q

K

R

R

I

V

C

L

I

I

V

A

T

A

H
|
H

G

G

Q

N

V

S

S

L

Q

R

G

G

V

I

L

V

A

K

V

H

L

L

K

E

active site: H9 (= H9), R60 (= R60), E87 (= E84), H184 (= H152)
binding ~{N}-[3,4-bis(oxidanyl)-9,10-bis(oxidanylidene)anthracen-2-yl]-4-(dimethylamino)benzenesulfonamide: N18 (≠ G18), R19 (≠ I19), F20 (≠ I20), R88 (≠ Q85), K98 (≠ T95), W113 (≠ Q100), R114 (≠ Q101)

8it4A Phosphoglycerate mutase 1 complexed with a covalent inhibitor
22% identity, 77% coverage: 3:164/210 of query aligns to 3:196/233 of 8it4A

query
sites
8it4A

Q

K

V

L

I

V

L

L

V

I

R

R

H

H

A

G

E

E

T

S

E

A

W

W

N

N

I

L

K

E

G

N

I

R

I
x
F

Q

S

G

G

Q

W

S

Y

D

D

S

A

A

D

L

L

T

S

P

P

R

A

G

G

E

H

R

E

Q

E

T

A

S

K

A

R

L

G

A

Q

A

A

F

L

A

R

A

D

S

A

D

G

Y

Y

R

E

V

F

D

D

C

I

V

C

Y

F

T

T

S

S

P

V

L

Q

G

K

R

R

A

A

-

I

-

R

-

T

-

L

W

W

Q

T

M

V

G

L

Q

D

R

A

L

I

A

-

G

D

H

Q

F

M

R

W

C

L

P

P

L

V

I

V

A

R

E

T

P

W

A

R

L

L

K

N

E

E

Q
x
R

A

H

F
x
Y

G

G

Q

G

F

L

E

T

G

G

M

L

L

N

T
x
K

S

A

Q

E

L

T

-

A

-

K

-

H

-

G

-

E

-

A

-

Q

-
x
V

-

K

M

I

Q
x
W

Q
x
R

R

R

P

S

H

Y

D

D

A

V

-

P

-

M

-

E

-

P

-

D

-

H

-

P

-

F

H

Y

A

S

L

N

F

I

T

S

H

K

D

D

A

R

E

R

Y

Y

C

A

P

D

-

L

-

T

-

E

-

D

-

Q

-

L

P

P

Q

S

G

C

E

E

S

S

L

L

A

K

Q

D

A

T

T

I

R

A

R

R

V

A

T

L

G

P

F

F

I

W

H

N

N

E

-

E

-

I

L

V

P

P

E

Q

A

I

T

K

E

E

H

G

Q

K

R

R

I

V

C

L

I

I

V

A

T

A

H

H

G

G

Q

N

V

S

S

L

Q

R

G

G

V

I

L

V

A

K

V

H

L

L

K

E

binding 3-[[5-(4-chlorophenyl)-2-methoxycarbonyl-thiophen-3-yl]sulfamoyl]benzenesulfonic acid: F20 (≠ I20), R88 (≠ Q85), Y90 (≠ F87), K98 (≠ T95), V110 (vs. gap), W113 (≠ Q100), R114 (≠ Q101)

5y2iB Phosphoglycerate mutase 1 (pgam1) complexed with its inhibitor pgmi- 004a
22% identity, 77% coverage: 3:164/210 of query aligns to 3:196/233 of 5y2iB

query
sites
5y2iB

Q

K

V

L

I

V

L

L

V

I

R

R

H
|
H

A

G

E

E

T

S

E

A

W

W

N

N

I

L

K
x
E

G
x
N

I

R

I
x
F

Q

S

G

G

Q

W

S

Y

D

D

S

A

A

D

L

L

T

S

P

P

R

A

G

G

E

H

R

E

Q

E

T

A

S

K

A

R

L

G

A

Q

A

A

F

L

A

R

A

D

S

A

D

G

Y

Y

R

E

V

F

D

D

C

I

V

C

Y

F

T

T

S

S

P

V

L

Q

G

K

R
|
R

A

A

-

I

-

R

-

T

-

L

W

W

Q

T

M

V

G

L

Q

D

R

A

L

I

A

-

G

D

H

Q

F

M

R

W

C

L

P

P

L

V

I

V

A

R

E

T

P

W

A

R

L

L

K

N

E
|
E

Q
x
R

A

H

F

Y

G

G

Q

G

F
x
L

E

T

G

G

M

L

L

N

T

K

S

A

Q

E

L

T

-

A

-

K

-

H

-

G

-

E

-

A

-

Q

-

V

-

K

M

I

Q
x
W

Q
x
R

R

R

P

S

H

Y

D

D

A

V

-

P

-
x
P

-

P

-

M

-

E

-

P

-

D

-

H

-

P

-

F

H

Y

A

S

L

N

F

I

T

S

H

K

D

D

A

R

E

R

Y

Y

C

A

P

D

-

L

-

T

-

E

-

D

-

Q

-

L

P

P

Q

S

G

C

E

E

S

S

L

L

A

K

Q

D

A

T

T

I

R

A

R

R

V

A

T

L

G

P

F

F

I

W

H

N

N

E

-

E

-

I

L

V

P

P

E

Q

A

I

T

K

E

E

H

G

Q

K

R

R

I

V

C

L

I

I

V

A

T

A

H
|
H

G

G

Q

N

V

S

S

L

Q

R

G

G

V

I

L

V

A

K

V

H

L

L

K

E

active site: H9 (= H9), R60 (= R60), E87 (= E84), H184 (= H152)
binding 3,4-bis(oxidanyl)-9,10-bis(oxidanylidene)-~{N}-[4-(trifluoromethyl)phenyl]anthracene-2-sulfonamide: E17 (≠ K17), N18 (≠ G18), F20 (≠ I20), R88 (≠ Q85), L93 (≠ F90), W113 (≠ Q100), R114 (≠ Q101), P121 (vs. gap)

Query Sequence

>WP_012968296.1 NCBI__GCF_000025465.1:WP_012968296.1
MMQVILVRHAETEWNIKGIIQGQSDSALTPRGERQTSALLAAFAASDYRVDCVYTSPLGR
AWQMGQRLAGHFRCPLIAEPALKEQAFGQFEGMLTSQLMQQRPHDAHALFTHDAEYCPPQ
GESLAQATRRVTGFIHNLPEATEHQRICIVTHGQVSQGVLAVLKEGTIDNFSRYAHPNAS
YSVFDFRDGKCLAIRWGIATHLLQLERQNA

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