SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_041097122.1 NCBI__GCF_000828635.1:WP_041097122.1 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)
28% identity, 87% coverage: 6:192/214 of query aligns to 1:187/207 of 4ij6A

query
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4ij6A

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active site: R8 (= R13), A9 (≠ H14), N15 (= N20), R58 (= R63), E82 (= E87), H150 (= H155)
binding phosphoserine: R8 (= R13), Q21 (= Q26), R58 (= R63), E82 (= E87), H85 (≠ F90), H150 (= H155), T151 (≠ G156)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
30% identity, 94% coverage: 7:208/214 of query aligns to 2:204/207 of 1h2fA

query
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1h2fA

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active site: R8 (= R13), H9 (= H14), N15 (= N20), R58 (= R63), E82 (= E87), H150 (= H155)
binding phosphate ion: T2 (= T7), T3 (≠ R8), G142 (= G147), E143 (≠ Q148)
binding trivanadate: R8 (= R13), H9 (= H14), N15 (= N20), Q21 (= Q26), R58 (= R63), E82 (= E87), H150 (= H155), G151 (= G156), V152 (≠ G157)

Sites not aligning to the query:

binding phosphate ion: 1

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
30% identity, 94% coverage: 7:208/214 of query aligns to 2:204/207 of 1h2eA

query
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1h2eA

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active site: R8 (= R13), H9 (= H14), N15 (= N20), R58 (= R63), E82 (= E87), H150 (= H155)
binding phosphate ion: R8 (= R13), H9 (= H14), R58 (= R63), E82 (= E87), H150 (= H155)

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)
34% identity, 71% coverage: 5:157/214 of query aligns to 2:161/223 of P9WIC7

query
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P9WIC7

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R10 (= R13) mutation to A: Loss of phosphatase activity.
H11 (= H14) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N20) mutation to A: About 5% of wild-type phosphatase activity.
K47 (= K50) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R63) mutation to A: Loss of phosphatase activity.
H159 (= H155) 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.

P62707 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Escherichia coli (strain K12) (see 6 papers)
38% identity, 45% coverage: 6:102/214 of query aligns to 3:104/250 of P62707

query
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P62707

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10:17 (vs. 13:20, 75% identical) binding
H11 (= H14) active site, Tele-phosphohistidine intermediate
K18 (≠ G21) modified: N6-acetyllysine
TG 23:24 (≠ QG 26:27) binding
E89 (= E87) active site, Proton donor/acceptor
ERHY 89:92 (≠ ERNF 87:90) binding
K100 (≠ V98) binding ; modified: N6-acetyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
106 modified: N6-acetyllysine
116:117 binding
184 Transition state stabilizer
185:186 binding

1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
38% identity, 45% coverage: 6:102/214 of query aligns to 1:102/239 of 1e59A

query
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1e59A

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active site: H9 (= H14), R60 (= R63), E87 (= E87)
binding tetrametavanadate: R8 (= R13), N15 (= N20), F20 (≠ I25), T21 (≠ Q26), G22 (= G27), Y90 (≠ F90), K98 (≠ V98)

Sites not aligning to the query:

active site: 182
binding tetrametavanadate: 114, 115, 184

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
34% identity, 71% coverage: 5:157/214 of query aligns to 1:160/217 of 4pzaB

query
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4pzaB

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-

A

-

E

-

L

V

V

A

A

T

S

G

E

L

P

E

E

A

W

M

G

A

G

A

A

R

D

H

E

V

P

G

D

Q

R

S

P

V

V

L

V

A

L

F

V

T

A

H
|
H

G
|
G

G

G

active site: H10 (= H14), R59 (= R63), E83 (= E87)
binding phosphate ion: R9 (= R13), H10 (= H14), R59 (= R63), E83 (= E87), H158 (= H155), G159 (= G156)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
34% identity, 70% coverage: 8:157/214 of query aligns to 3:159/209 of 4qihA

query
sites
4qihA

R

R

F

L

C

V

F

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

D

D

W

Y

N

N

G

V

E

G

K

S

R

R

I

M

Q
|
Q

G

G

Q

Q

I

L

D

D

I

T

D

E

L

L

N

S

A

E

A

L

G

G

E

R

A

T

Q

Q

A

A

R

V

A

A

V

A

G

A

V

E

G

V

L

L

A

G

K

K

H

R

S

Q

F

P

A

L

A

I

Y

V

S

S

D

D

L

L

L

R

R
|
R

A

A

W

Y

R

D

T

T

A

A

Q

V

I

K

A

L

T

G

R

E

G

R

L

T

G

G

L

L

A

V

V

V

S

R

P

V

A

D

P

T

T

R

L

L

R

R

E
|
E

R

T

N

H

F

L

G

G

V

D

L

W

Q

Q

G

G

I

L

T

T

V

H

Q

A

E

Q

A

I

S

D

V

A

Q

D

R

A

P

P

E

G

A

A

H

-

R

R

H

L

H

A

Q

W

A

R

R

E

T

D

P

A

D

T

Y

W

N

A

Y

P

E

H

S

G

G

G

E

E

S

S

L

R

I

V

A

D

F

V

A

A

R

R

-

S

-

R

-

P

-

L

-

V

-

A

-

E

-

L

V

V

A

A

T

S

G

E

L

P

E

E

A

W

M

G

A

G

A

A

R

D

H

E

V

P

G

D

Q

R

S

P

V

V

L

V

A

L

F

V

T

A

H
|
H

G

G

active site: H9 (= H14), R58 (= R63), E82 (= E87)
binding vanadate ion: R8 (= R13), H9 (= H14), Q21 (= Q26), R58 (= R63), H157 (= H155)

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)
35% identity, 64% coverage: 9:144/214 of query aligns to 6:142/257 of Q7ZVE3

query
sites
Q7ZVE3

F

L

C

T

F

I

V

V

R

R

H
|
H

G

G

E

E

T

T

D

Q

W

Y

N

N

G

R

E

D

K

K

R

L

I

L

Q

Q

G

G

Q

Q

-

G

I

I

D

D

I

T

D

P

L

L

N

S

A

D

A

T

G

G

E

H

A

Q

Q

Q

A

A

R

A

A

A

V

A

G

G

V

R

G

Y

L

L

A

K

K

D

H

L

S

H

F

F

A

T

A

N

A

V

Y

F

S

V

S

S

D

N

L

L

L

Q

R

R

A

A

W

I

R

Q

T

T

A

A

Q

E

I

I

A

I

T

L

R

-

G

G

L

N

G

N

L

L

A

H

V

S

S

S

P

A

A

T

-

E

-

M

-

I

-

L

-

D

P

P

T

L

L

L

R

R

E

E

R

R

N

G

F

F

G

G

V

V

L

A

Q

E

G

G

I

-

T

-

V

-

Q

-

E

-

A

-

S

-

V

-

Q

-

R

R

P

P

E

K

A

E

H

H

R

L

H

K

H

N

Q

M

A

A

R

N

T

A

P

A

-

G

-

Q

-

S

-

C

-

R

D

D

Y

Y

N

T

Y

P

E

P

S

G

G

G

E

E

S

T

L

L

I

E

A

Q

F

V

A

K

A

T

R

R

V

F

A

K

T

M

G

F

L

L

E

K

A

S

M

L

A

F

A

Q

R

R

H11 (= H14) active site, Tele-phosphohistidine intermediate

Q9NQ88 Fructose-2,6-bisphosphatase TIGAR; TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; EC 3.1.3.46 from Homo sapiens (Human) (see 4 papers)
39% identity, 50% coverage: 12:117/214 of query aligns to 9:119/270 of Q9NQ88

query
sites
Q9NQ88

V

V

R

R

H
|
H

G

G

E

E

T

T

D

R

W

F

N

N

G

K

E

E

K

K

R

I

I

I

Q

Q

G

G

Q

Q

-

G

I

V

D

D

I

E

D

P

L

L

N

S

A

E

A

T

G

G

E

F

A

K

Q

Q

A

A

R

A

A

A

V

A

G

G

V

I

G

F

L

L

A

N

K

N

H

V

S

K

F

F

A

T

A

H

A

A

Y

F

S

S

D

D

L

L

L

M

R

R

A

T

W

K

R

Q

T

T

A

M

Q

H

-

G

I

I

A

L

T

E

R

R

G

S

-

K

-

F

-

C

L

K

G

D

L

M

A

T

V

V

S

K

P

Y

A

D

P

S

T

R

L

L

R

R

E

E

R

R

N

K

F

Y

G

G

V

V

L

V

Q

E

G

G

I

K

T

A

V

L

Q

S

E
|
E

A

L

S

R

V

A

Q

M

R

A

P

K

E

A

A

A

H

R

R

E

H

E

H

C

Q

P

A

V

R

F

T

T

P

P

H11 (= H14) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.
E102 (= E100) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.

Sites not aligning to the query:

198 H→A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.
258:261 mutation Missing: Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.

3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
35% identity, 46% coverage: 6:104/214 of query aligns to 1:104/229 of 3gp3A

query
sites
3gp3A

I

M

T

Y

R

K

F

L

C

V

F

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

D

T

W

W

N

N

G

K

E

E

K

N

R

R

I

F

Q
x
T

G

G

Q

W

I

V

D

D

I

V

D

D

L

L

N

T

A

E

A

Q

G

G

E

N

A

R

Q

E

A

A

R

R

A

Q

V

A

G

G

V

Q

G

L

L

L

-

K

-

E

A

A

K

G

H

Y

S

T

F

F

A

D

A

I

A

A

Y

Y

S

T

S

S

D

V

L

L

L

K

R
|
R

A

A

W

I

R

R

T

T

A

L

Q

W

I

H

A

V

T

Q

R

D

G

Q

L

M

G

D

L

L

A

M

V

Y

S

V

P

P

A

V

P

V

-

H

-

S

-

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F
x
Y

G

G

V

A

L

L

Q

S

G

G

I

L

T

N

V
x
K

Q

A

E

E

A

T

S

A

V

A

Q

K

active site: H9 (= H14), R60 (= R63), E87 (= E87)
binding phosphite ion: R8 (= R13), H9 (= H14), R60 (= R63), E87 (= E87)
binding phosphoserine: T21 (≠ Q26), E87 (= E87), Y90 (≠ F90), K98 (≠ V98)

Sites not aligning to the query:

3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
35% identity, 46% coverage: 6:104/214 of query aligns to 1:104/230 of 3fdzA

query
sites
3fdzA

I

M

T

Y

R

K

F

L

C

V

F

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

D

T

W

W

N
|
N

G

K

E

E

K

N

R

R

I

F

Q
x
T

G

G

Q

W

I

V

D

D

I

V

D

D

L

L

N

T

A

E

A

Q

G

G

E

N

A

R

Q

E

A

A

R

R

A

Q

V

A

G

G

V

Q

G

L

L

L

-

K

-

E

A

A

K

G

H

Y

S

T

F

F

A

D

A

I

A

A

Y

Y

S

T

S

S

D

V

L

L

L

K

R
|
R

A

A

W

I

R

R

T

T

A

L

Q

W

I

H

A

V

T

Q

R

D

G

Q

L

M

G

D

L

L

A

M

V

Y

S

V

P

P

A

V

P

V

-

H

-

S

-

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F
x
Y

G

G

V

A

L

L

Q

S

G

G

I

L

T

N

V
x
K

Q

A

E

E

A

T

S

A

V

A

Q

K

active site: H9 (= H14), R60 (= R63), E87 (= E87)
binding (2R)-2,3-diphosphoglyceric acid: R8 (= R13), H9 (= H14), N15 (= N20), T21 (≠ Q26), R60 (= R63), E87 (= E87), Y90 (≠ F90), K98 (≠ V98)

Sites not aligning to the query:

active site: 182
binding (2R)-2,3-diphosphoglyceric acid: 114, 115, 182, 183, 184

Q3JWH7 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Burkholderia pseudomallei (strain 1710b) (see paper)
35% identity, 46% coverage: 6:104/214 of query aligns to 1:104/249 of Q3JWH7

query
sites
Q3JWH7

I

M

T

Y

R

K

F

L

C

V

F

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

D

T

W

W

N
|
N

G

K

E

E

K

N

R

R

I

F

Q
x
T

G
|
G

Q

W

I

V

D

D

I

V

D

D

L

L

N

T

A

E

A

Q

G

G

E

N

A

R

Q

E

A

A

R

R

A

Q

V

A

G

G

V

Q

G

L

L

L

-

K

-

E

A

A

K

G

H

Y

S

T

F

F

A

D

A

I

A

A

Y

Y

S

T

S

S

D

V

L

L

L

K

R
|
R

A

A

W

I

R

R

T

T

A

L

Q

W

I

H

A

V

T

Q

R

D

G

Q

L

M

G

D

L

L

A

M

V

Y

S

V

P

P

A

V

P

V

-

H

-

S

-

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F
x
Y

G

G

V

A

L

L

Q

S

G

G

I

L

T

N

V
x
K

Q

A

E

E

A

T

S

A

V

A

Q

K

R8 (= R13) binding
H9 (= H14) active site, Tele-phosphohistidine intermediate; binding
N15 (= N20) binding
T21 (≠ Q26) binding ; binding
G22 (= G27) binding ; binding
R60 (= R63) binding
E87 (= E87) binding ; binding
Y90 (≠ F90) binding ; binding
K98 (≠ V98) binding ; binding

Sites not aligning to the query:

114 binding ; binding
115 binding ; binding
182 binding
183 binding
184 binding ; binding

3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
35% identity, 46% coverage: 6:104/214 of query aligns to 1:104/248 of 3gp5A

query
sites
3gp5A

I

M

T

Y

R

K

F

L

C

V

F

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

D

T

W

W

N
|
N

G

K

E

E

K

N

R

R

I

F

Q

T

G

G

Q

W

I

V

D

D

I

V

D

D

L

L

N

T

A

E

A

Q

G

G

E

N

A

R

Q

E

A

A

R

R

A

Q

V

A

G

G

V

Q

G

L

L

L

-

K

-

E

A

A

K

G

H

Y

S

T

F

F

A

D

A

I

A

A

Y

Y

S

T

S

S

D

V

L

L

L

K

R
|
R

A

A

W

I

R

R

T

T

A

L

Q

W

I

H

A

V

T

Q

R

D

G

Q

L

M

G

D

L

L

A

M

V

Y

S

V

P

P

A

V

P

V

-

H

-

S

-

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F

Y

G

G

V

A

L

L

Q

S

G

G

I

L

T

N

V

K

Q

A

E

E

A

T

S

A

V

A

Q

K

active site: H9 (= H14), R60 (= R63), E87 (= E87)
binding vanadate ion: R8 (= R13), H9 (= H14), N15 (= N20), R60 (= R63), E87 (= E87)

Sites not aligning to the query:

active site: 182
binding vanadate ion: 182, 183

P9WIC9 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 46% coverage: 9:107/214 of query aligns to 7:110/249 of P9WIC9

query
sites
P9WIC9

F

L

C

V

F

L

V

L

R
|
R

H
|
H

G
|
G

E
|
E

T
x
S

D
|
D

W
|
W

N
|
N

G

A

E

L

K

N

R

L

I

F

Q
x
T

G
|
G

Q

W

I

V

D

D

I

V

D

G

L

L

N

T

A

D

A

K

G

G

E

Q

A

A

Q

E

A

A

R

V

A

R

V

S

G

G

V

E

G

L

L

I

A

A

K

E

H

H

S

D

F

L

A

L

-

P

-

D

A

V

A

L

Y

Y

S

T

S

S

D

L

L

L

L

R

R
|
R

A

A

W

I

R

T

T

T

A

A

Q

H

I

L

A

A

T

L

R

D

G

S

-

A

-

D

-

R

L

L

G

W

L

I

A

P

V

V

S

R

P

R

A

S

P

W

T

R

L

L

R

N

E
|
E

R
|
R

N
x
H

F
x
Y

G

G

V

A

L

L

Q

Q

G

G

I

L

T

D

V

K

Q

A

E

E

A

T

S

K

V

A

Q

R

R

Y

P

G

E

E

11:18 (vs. 13:20, 88% identical) binding
TG 24:25 (≠ QG 26:27) binding
R63 (= R63) binding
ERHY 90:93 (≠ ERNF 87:90) binding

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)
34% identity, 42% coverage: 6:95/214 of query aligns to 1:95/247 of P00950

query
sites
P00950

I
x
M

T

P

R

K

F

L

C

V

F

L

V

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

D
x
E

W
|
W

N
|
N

G

E

E

K

K

N

R

L

I

F

Q
x
T

G
|
G

Q

W

I

V

D

D

I

V

D

K

L

L

N

S

A

A

A

K

G

G

E

Q

A

Q

Q

E

A

A

R

A

A

R

V

A

G

G

V

E

G

L

L

L

A

K

K

E

H

K

S

K

F

V

A

Y

A

P

-

D

-

V

A

L

Y

Y

S

T

S

S

D

K

L

L

L

S

R
|
R

A

A

W

I

R

Q

T

T

A

A

Q

N

I

I

A

A

T

L

R

E

G

K

-

A

-

D

-

R

L

L

G

W

L

I

A

P

V

V

S

N

P

R

A

S

P

W

T

R

L

L

R

N

E
|
E

R
|
R

N
x
H

F
x
Y

G

G

V

D

L

L

Q

Q

G

G

M1 (≠ I6) modified: Initiator methionine, Removed
8:15 (vs. 13:20, 63% identical) binding
H9 (= H14) active site, Tele-phosphohistidine intermediate
TG 21:22 (≠ QG 26:27) binding
R60 (= R63) binding
ERHY 87:90 (≠ ERNF 87:90) binding

Sites not aligning to the query:

98 binding
114:115 binding
169 K→P: Causes dissociation of the homotetramer to dimers at low concentrations.
182 H→A: Reduces kcat of the mutase reaction 10000-fold.
183:184 binding

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
34% identity, 41% coverage: 8:95/214 of query aligns to 2:94/240 of 1qhfA

query
sites
1qhfA

R

K

F

L

C

V

F

L

V

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

D

E

W

W

N
|
N

G

E

E

K

K

N

R

L

I

F

Q
x
T

G

G

Q

W

I

V

D

D

I

V

D

K

L

L

N

S

A

A

A

K

G

G

E

Q

A

Q

Q

E

A

A

R

A

A

R

V

A

G

G

V

E

G

L

L

L

A

K

K

E

H

K

S

K

F

V

A

Y

A

P

-

D

-

V

A

L

Y

Y

S

T

S

S

D

K

L

L

L

S

R
|
R

A

A

W

I

R

Q

T

T

A

A

Q

N

I

I

A

A

T

L

R

E

G

K

-

A

-

D

-

R

L

L

G

W

L

I

A

P

V

V

S

N

P

R

A

S

P

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F

Y

G

G

V

D

L

L

Q

Q

G

G

active site: H8 (= H14), R59 (= R63), E86 (= E87)
binding 3-phosphoglyceric acid: R7 (= R13), H8 (= H14), G9 (= G15), Q10 (≠ E16), S11 (≠ T17), N14 (= N20), T20 (≠ Q26), R59 (= R63)

Sites not aligning to the query:

active site: 181
binding 3-phosphoglyceric acid: 207

7xb9B Phosphoglycerate mutase 1 complexed with a covalent inhibitor
34% identity, 48% coverage: 8:109/214 of query aligns to 3:109/231 of 7xb9B

query
sites
7xb9B

R

K

F

L

C

V

F

L

V

I

R

R

H

H

G

G

E

E

T

S

D

A

W

W

N

N

G

L

E

E

K

N

R

R

I
x
F

Q

S

G

G

Q

W

I

Y

D

D

I

A

D

D

L

L

N

S

A

P

A

A

G

G

E

H

A

E

Q

E

A

A

R

K

A

R

V

G

G

G

V

Q

G

A

L

L

-

R

-

D

A

A

K

G

H

Y

S

E

F

F

A

D

A

I

A

C

Y

F

S

T

S

S

D

V

L

Q

L

K

R

R

A

A

W

I

R

R

T

T

A

L

Q

W

I

T

-

V

-

L

-

D

A

A

T

I

R

D

G

Q

L

M

G

W

L

L

A

P

V

V

S

V

P

R

A

T

P

W

T

R

L

L

R

N

E

E

R
|
R

N

H

F
x
Y

G

G

V

G

L

L

Q

T

G

G

I

L

T

N

V
x
K

Q

A

E

E

A

T

S

A

V

A

Q

K

R

H

P

G

E

E

A

A

H

Q

binding 3-[[5-(cyclopenten-1-yl)-2-methoxycarbonyl-phenyl]sulfamoyl]benzenesulfonic acid: F20 (≠ I25), R88 (= R88), Y90 (≠ F90), K98 (≠ V98)

Sites not aligning to the query:

binding 3-[[5-(cyclopenten-1-yl)-2-methoxycarbonyl-phenyl]sulfamoyl]benzenesulfonic acid: 113, 114, 186

5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
34% identity, 41% coverage: 8:95/214 of query aligns to 2:94/234 of 5pgmE

query
sites
5pgmE

R

K

F

L

C

V

F

L

V

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

G

E

E

K

K

N

R

L

I

F

Q

T

G

G

Q

W

I

V

D

D

I

V

D

K

L

L

N

S

A

A

A

K

G

G

E

Q

A

Q

Q

E

A

A

R

A

A

R

V

A

G

G

V

E

G

L

L

L

A

K

K

E

H

K

S

K

F

V

A

Y

A

P

-

D

-

V

A

L

Y

Y

S

T

S

S

D

K

L

L

L

S

R
|
R

A

A

W

I

R

Q

T

T

A

A

Q

N

I

I

A

A

T

L

R

E

G

K

-

A

-

D

-

R

L

L

G

W

L

I

A

P

V

V

S

N

P

R

A

S

P

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F

Y

G

G

V

D

L

L

Q

Q

G

G

active site: H8 (= H14), R59 (= R63), E86 (= E87)

Sites not aligning to the query:

active site: 181
binding alanine: 231, 234

1bq4A Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate (see paper)
34% identity, 41% coverage: 8:95/214 of query aligns to 2:94/234 of 1bq4A

query
sites
1bq4A

R

K

F

L

C

V

F

L

V

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

G

E

E

K

K

N

R

L

I

F

Q

T

G

G

Q

W

I

V

D

D

I

V

D

K

L

L

N

S

A

A

A

K

G

G

E

Q

A

Q

Q

E

A

A

R

A

A

R

V

A

G

G

V

E

G

L

L

L

A

K

K

E

H

K

S

K

F

V

A

Y

A

P

-

D

-

V

A

L

Y

Y

S

T

S

S

D

K

L

L

L

S

R
|
R

A

A

W

I

R

Q

T

T

A

A

Q

N

I

I

A

A

T

L

R

E

G

K

-

A

-

D

-

R

L

L

G

W

L

I

A

P

V

V

S

N

P

R

A

S

P

W

T

R

L

L

R

N

E
|
E

R

R

N

H

F
x
Y

G

G

V

D

L

L

Q

Q

G

G

active site: H8 (= H14), R59 (= R63), E86 (= E87)
binding benzene hexacarboxylic acid: Y89 (≠ F90)

Sites not aligning to the query:

active site: 181
binding benzene hexacarboxylic acid: 113, 114, 183, 204

Query Sequence

>WP_041097122.1 NCBI__GCF_000828635.1:WP_041097122.1
MSTARITRFCFVRHGETDWNGEKRIQGQIDIDLNAAGEAQARAVGVGLAKHSFAAAYSSD
LLRAWRTAQIATRGLGLAVSPAPTLRERNFGVLQGITVQEASVQRPEAHRHHQARTPDYN
YESGESLIAFAARVATGLEAMAARHVGQSVLAFTHGGVLDVVYRAAAGRALDVPRDFQLP
NAAFNWLEYDDKGWRLISWADCSHLQRVLDEMLE

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