SitesBLAST

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
33% identity, 93% coverage: 5:208/219 of query aligns to 4:206/207 of 4ij6A

query
sites
4ij6A

V

L

L

I

L

L

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x
A

G

A

E

E

T

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E

E

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N
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N

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V

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G

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active site: R8 (= R9), A9 (≠ H10), N15 (= N16), R58 (= R58), E82 (= E82), H150 (= H151)
binding phosphoserine: R8 (= R9), Q21 (= Q22), R58 (= R58), E82 (= E82), H85 (≠ F85), H150 (= H151), T151 (≠ G152)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
34% identity, 92% coverage: 3:204/219 of query aligns to 2:203/207 of 1h2fA

query
sites
1h2fA

T
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active site: R8 (= R9), H9 (= H10), N15 (= N16), R58 (= R58), E82 (= E82), H150 (= H151)
binding phosphate ion: T2 (= T3), T3 (= T4), G142 (= G143), E143 (≠ K144)
binding trivanadate: R8 (= R9), H9 (= H10), N15 (= N16), Q21 (= Q22), R58 (= R58), E82 (= E82), H150 (= H151), G151 (= G152), V152 (≠ G153)

Sites not aligning to the query:

binding phosphate ion: 1

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
34% identity, 92% coverage: 3:204/219 of query aligns to 2:203/207 of 1h2eA

query
sites
1h2eA

T

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active site: R8 (= R9), H9 (= H10), N15 (= N16), R58 (= R58), E82 (= E82), H150 (= H151)
binding phosphate ion: R8 (= R9), H9 (= H10), R58 (= R58), E82 (= E82), H150 (= H151)

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)
29% identity, 72% coverage: 5:162/219 of query aligns to 10:174/211 of P36623

query
sites
P36623

V

L

L

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T37 (≠ N32) modified: Phosphothreonine
S62 (= S54) modified: Phosphoserine
Y96 (≠ F85) modified: Phosphotyrosine
S166 (≠ I154) modified: Phosphoserine

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)
31% identity, 68% coverage: 5:153/219 of query aligns to 6:161/223 of P9WIC7

query
sites
P9WIC7

V

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R10 (= R9) mutation to A: Loss of phosphatase activity.
H11 (= H10) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N16) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ G46) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R58) mutation to A: Loss of phosphatase activity.
H159 (= H151) 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.

P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 69% coverage: 6:156/219 of query aligns to 9:181/271 of P36136

query
sites
P36136

L

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H

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x
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R

R12 (= R9) binding substrate; mutation to A: Impairs catalytic activity.
H13 (= H10) active site, Tele-phosphohistidine intermediate; mutation to A: Impairs catalytic activity.
T16 (= T13) mutation to A: Impairs catalytic activity.
S19 (≠ N16) mutation to A: Leads to reduced substrate affinity.
Y24 (≠ F21) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ FQ 21:22) binding substrate
S65 (= S54) mutation to A: Leads to low activity and reduced substrate affinity.
R69 (= R58) binding substrate; mutation to A: Leads to reduced substrate affinity.
E99 (= E82) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EINF 82:85) binding substrate
Y102 (≠ F85) mutation to A: Impairs catalytic activity.
W131 (= W107) mutation to A: Leads to reduced substrate affinity.
H176 (= H151) mutation to A: Impairs catalytic activity.
H178 (≠ G153) mutation to A: Leads to low activity and reduced substrate affinity.
R181 (≠ K156) binding substrate; mutation to A: Leads to reduced substrate affinity.

Sites not aligning to the query:

244 binding substrate

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
31% identity, 68% coverage: 5:153/219 of query aligns to 5:160/217 of 4pzaB

query
sites
4pzaB

V

L

L

V

L

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

E

D

W

Y

N

N

V

V

Q

G

G

S

R

R

F

M

Q

Q

G

G

C

Q

H

L

D

D

I

T

N

E

L

L

T

S

D

E

N

L

G

G

I

R

E

T

Q

Q

A

A

K

V

R

A

V

A

A

A

K

E

R

V

L

L

E

G

G

K

S

R

F

Q

D

P

C

L

-

L

V

I

Y

V

A

S

S

S

P

D

L

L

K

R

R
|
R

A

A

F

Y

N

D

T

T

A

A

K

V

L

K

I

L

A

G

S

E

T

R

K

T

G

G

I

L

S

V

P

V

I

R

I

V

E

D

D

T

D

R

L

L

R

R

E
|
E

I

T

N

H

F

L

G

G

L

D

W

W

E

Q

G

G

L

L

T

T

I

H

K

A

E

Q

M

I

K

D

S

A

K

D

F

A

P

P

K

G

E

A

F

R

D

L

I

A

W

W

R

R

N

E

D

D

T

A

E

T

D

W

G

A

P

P

L

-

C

H

G

G

D

E

L

S

S

R

I

V

K

D

R

V

A

A

S

A

I

-

R

R

V

S

E

R

H

P

A

L

V

V

L

A

K

E

I

L

V

V

-

A

-

S

-

E

-

P

-

E

-

W

-

G

N

A

D

D

N

E

K

P

G

D

K

R

N

P

I

V

V

V

V

L

V

V

A

A

H
|
H

G
|
G

G

G

active site: H10 (= H10), R59 (= R58), E83 (= E82)
binding phosphate ion: R9 (= R9), H10 (= H10), R59 (= R58), E83 (= E82), H158 (= H151), G159 (= G152)

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
28% identity, 69% coverage: 6:156/219 of query aligns to 7:179/269 of 3lg2A

query
sites
3lg2A

L

I

V

V

R
|
R

H
|
H

G

G

E

Q

T

T

E

E

W

W

N

S

V

K

Q

S

G

G

R

Q

F

Y

Q
x
T

G

G

C

L

H

T

D

D

I

L

N

P

L

L

T

T

D

P

N

Y

G

G

I

E

E

G

Q

Q

A

M

K

L

R

R

V

T

A

G

K

E

R

S

L

V

-

F

-

R

-

N

-

Q

-

F

-

L

-

N

E

P

G

D

S

N

F

I

D

T

C

Y

V

I

Y

F

A

T

S

S

P

P

L

R

K

L

R
|
R

A

A

F

R

N

Q

T

T

A

V

K

D

L

L

I

V

-

L

-

K

-

P

-

L

-

S

-

D

A

E

S

Q

T

R

K

A

G

K

I

I

S

R

P

V

I

V

E

D

D

D

L

L

R

R

E
|
E

I

W

N

E

F

Y

G

G

L

D

W

Y

E

E

G

G

L

M

T

L

I

T

K

R

E

E

M

I

-

I

-

E

-

L

-

R

K

K

S

S

K

R

F

G

-

L

-

D

-

K

P

E

K

R

E

P

F

W

D

N

I

I

W

W

R

R

N

D

D

G

T

C

E

E

D

N

G

G

P

E

L

T

C

T

G

Q

-

I

D

G

L

L

S

R

I

L

K

S

R

R

A

A

S

I

I

A

R

R

V

I

E

Q

H

N

A

L

V

H

L

R

K

K

I

H

V

Q

N

S

D

E

N

G

K

R

G

A

K

S

N

D

I

I

V

M

V

V

V

F

A

A

H
|
H

G

G

G
x
H

I

A

I

L

K
x
R

active site: H11 (= H10), R67 (= R58), E97 (= E82)
binding phosphate ion: R10 (= R9), H11 (= H10), T23 (≠ Q22), R67 (= R58), E97 (= E82), H174 (= H151), H176 (≠ G153), R179 (≠ K156)

Sites not aligning to the query:

binding phosphate ion: 242, 266

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
31% identity, 68% coverage: 5:153/219 of query aligns to 4:159/209 of 4qihA

query
sites
4qihA

V

L

L

V

L

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

E

D

W

Y

N

N

V

V

Q

G

G

S

R

R

F

M

Q
|
Q

G

G

C

Q

H

L

D

D

I

T

N

E

L

L

T

S

D

E

N

L

G

G

I

R

E

T

Q

Q

A

A

K

V

R

A

V

A

A

A

K

E

R

V

L

L

E

G

G

K

S

R

F

Q

D

P

C

L

-

L

V

I

Y

V

A

S

S

S

P

D

L

L

K

R

R
|
R

A

A

F

Y

N

D

T

T

A

A

K

V

L

K

I

L

A

G

S

E

T

R

K

T

G

G

I

L

S

V

P

V

I

R

I

V

E

D

D

T

D

R

L

L

R

R

E
|
E

I

T

N

H

F

L

G

G

L

D

W

W

E

Q

G

G

L

L

T

T

I

H

K

A

E

Q

M

I

K

D

S

A

K

D

F

A

P

P

K

G

E

A

F

R

D

L

I

A

W

W

R

R

N

E

D

D

T

A

E

T

D

W

G

A

P

P

L

-

C

H

G

G

D

E

L

S

S

R

I

V

K

D

R

V

A

A

S

A

I

-

R

R

V

S

E

R

H

P

A

L

V

V

L

A

K

E

I

L

V

V

-

A

-

S

-

E

-

P

-

E

-

W

-

G

N

A

D

D

N

E

K

P

G

D

K

R

N

P

I

V

V

V

V

L

V

V

A

A

H
|
H

G

G

active site: H9 (= H10), R58 (= R58), E82 (= E82)
binding vanadate ion: R8 (= R9), H9 (= H10), Q21 (= Q22), R58 (= R58), H157 (= H151)

1e59A E.Coli cofactor-dependent phosphoglycerate mutase complexed with vanadate (see paper)
28% identity, 86% coverage: 3:191/219 of query aligns to 2:222/239 of 1e59A

query
sites
1e59A

T

T

T

K

V

L

L

V

L

L

V

V

R
|
R

H
|
H

G

G

E

E

T

S

E

Q

W

W

N
|
N

V

K

Q

E

G

N

R

R

F
|
F

Q
x
T

G
|
G

C

W

H

Y

D

D

I

V

N

D

L

L

T

S

D

E

N

K

G

G

I

V

E

S

Q

E

A

A

K

K

R

A

V

A

A

G

K

K

R

L

L

L

-

K

-

E

E

E

G

G

-

Y

S

S

F

F

D

D

C

F

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R
|
R

A

A

F

I

N

H

T

T

A

L

K

W

-

N

-

V

L

L

I

D

A

E

S

L

T

D

K

Q

G

A

I

W

S

L

P

P

I

V

I

E

E

K

D

S

-

W

D

K

L

L

R

N

E
|
E

I

R

N

H

F
x
Y

G

G

L

A

W

L

E

Q

G

G

L

L

T

N

I
x
K

K

A

E

E

M

T

K

A

S

E

K

K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

K

I

Q

W

W

R
|
R

-
x
R

-

G

-

F

-

A

-

V

-

T

-

P

-

E

-

L

-

T

N

K

D

D

T

D

E

E

D

R

G

Y

P

P

-

G

-

H

-

D

-

P

-

R

-

Y

-

A

-

K

L

L

C

S

G

E

G

K

D

E

L

L

S

P

I

L

K

T

R

E

A

S

S

L

I

A

R

L

V

T

E

I

H

D

A

R

V

V

L

I

K

P

I

Y

V

W

N

N

D

E

N

T

-

I

-

L

-

P

-

R

-

M

-

K

K

S

G

G

K

E

N

R

I

V

V

I

V

A

A

A

H
|
H

G

G

G
x
N

I

S

I

L

K

R

A

A

A

L

L

V

I

K

A

Y

L

L

F

D

N

N

W

M

N

S

M

E

A

E

M

E

Y

I

H

L

R

E

I

L

L

N

L

I

G

P

N

T

T

G

S

V

I

P

C

L

K

V

I

Y

E

E

F

F

N

D

E

E

N

N

N

F

I

K

P

P

active site: H9 (= H10), R60 (= R58), E87 (= E82), H182 (= H151)
binding tetrametavanadate: R8 (= R9), N15 (= N16), F20 (= F21), T21 (≠ Q22), G22 (= G23), Y90 (≠ F85), K98 (≠ I93), R114 (= R108), R115 (vs. gap), N184 (≠ G153)

3ll4A Structure of the h13a mutant of ykr043c in complex with fructose-1,6- bisphosphate (see paper)
28% identity, 69% coverage: 6:156/219 of query aligns to 7:179/261 of 3ll4A

query
sites
3ll4A

L

I

V

V

R
|
R

H
x
A

G

G

E

Q

T

T

E

E

W

W

N

S

V

K

Q

S

G

G

R

Q

F
x
Y

Q
x
T

G

G

C

L

H

T

D

D

I

L

N

P

L

L

T

T

D

P

N

Y

G

G

I

E

E

G

Q

Q

A

M

K

L

R

R

V

T

A

G

K

E

R

S

L

V

-

F

-

R

-

N

-

Q

-

F

-

L

-

N

E

P

G

D

S

N

F

I

D

T

C

Y

V

I

Y

F

A

T

S

S

P

P

L

R

K

L

R
|
R

A

A

F

R

N

Q

T

T

A

V

K

D

L

L

I

V

-

L

-

K

-

P

-

L

-

S

-

D

A

E

S

Q

T

R

K

A

G

K

I

I

S

R

P

V

I

V

E

D

D

D

L

L

R

R

E
|
E

I

W

N

E

F

Y

G

G

L

D

W

Y

E

E

G

G

L

M

T

L

I

T

K

R

E

E

M

I

-

I

-

E

-

L

-

R

K

K

S

S

K

R

-

G

F

L

P

D

K

K

E

E

-

R

-

P

F

W

D

N

I

I

W

W

R

R

N

D

D

G

T

C

E

E

D

N

G

G

P

E

L

T

C

T

G

Q

-

I

D

G

L

L

S

R

I

L

K

S

R

R

A

A

S

I

I

A

R

R

V

I

E

Q

H

N

A

L

V

H

L

R

K

K

I

H

V

Q

N

S

D

E

N

G

K

R

G

A

K

S

N

D

I

I

V

M

V

V

V

F

A

A

H
|
H

G
|
G

G
x
H

I

A

I

L

K
x
R

active site: A11 (≠ H10), R67 (= R58), E97 (= E82)
binding 1,6-fructose diphosphate (linear form): R10 (= R9), Y22 (≠ F21), T23 (≠ Q22), R67 (= R58), E97 (= E82), H174 (= H151), G175 (= G152), H176 (≠ G153), R179 (≠ K156)

3oi7A Structure of the structure of the h13a mutant of ykr043c in complex with sedoheptulose-1,7-bisphosphate (see paper)
27% identity, 69% coverage: 6:156/219 of query aligns to 6:178/260 of 3oi7A

query
sites
3oi7A

L

I

V

V

R
|
R

H
x
A

G

G

E

Q

T
|
T

E

E

W

W

N

S

V

K

Q

S

G

G

R

Q

F
x
Y

Q
x
T

G

G

C

L

H

T

D

D

I

L

N

P

L

L

T

T

D

P

N

Y

G

G

I

E

E

G

Q

Q

A

M

K

L

R

R

V

T

A

G

K

E

R

S

L

V

-

F

-

R

-

N

-

Q

-

F

-

L

-

N

E

P

G

D

S

N

F

I

D

T

C

Y

V

I

Y

F

A

T

S

S

P

P

L

R

K

L

R
|
R

A

A

F

R

N

Q

T

T

A

V

K

D

L

L

I

V

-

L

-

K

-

P

-

L

-

S

-

D

A

E

S

Q

T

R

K

A

G

K

I

I

S

R

P

V

I

V

E

D

D

D

L

L

R

R

E
|
E

I

W

N

E

F
x
Y

G

G

L

D

W

Y

E

E

G

G

L

M

T

L

I

T

K

R

E

E

M

I

-

I

-

E

-

L

-

R

K

K

S

S

K

R

F

G

-

L

-

D

-

K

P

E

K

R

E

P

F

W

D

N

I

I

W

W

R

R

N

D

D

G

T

C

E

E

D

N

G

G

P

E

L

T

C

T

G

Q

-

I

D

G

L

L

S

R

I

L

K

S

R

R

A

A

S

I

I

A

R

R

V

I

E

Q

H

N

A

L

V

H

L

R

K

K

I

H

V

Q

N

S

D

E

N

G

K

R

G

A

K

S

N

D

I

I

V

M

V

V

V

F

A

A

H
|
H

G

G

G
x
H

I

A

I

L

K
x
R

active site: A10 (≠ H10), R66 (= R58), E96 (= E82)
binding magnesium ion: T13 (= T13), T22 (≠ Q22), R66 (= R58)
binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: R9 (= R9), Y21 (≠ F21), T22 (≠ Q22), R66 (= R58), E96 (= E82), Y99 (≠ F85), H173 (= H151), H175 (≠ G153), R178 (≠ K156)

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)
28% identity, 86% coverage: 3:191/219 of query aligns to 4:224/250 of P62707

query
sites
P62707

T

T

T

K

V

L

L

V

L

L

V

V

R
|
R

H
|
H

G
|
G

E
|
E

T
x
S

E
x
Q

W
|
W

N
|
N

V
x
K

Q

E

G

N

R

R

F

F

Q
x
T

G
|
G

C

W

H

Y

D

D

I

V

N

D

L

L

T

S

D

E

N

K

G

G

I

V

E

S

Q

E

A

A

K

K

R

A

V

A

A

G

K

K

R

L

L

L

-

K

-

E

E

E

G

G

-

Y

S

S

F

F

D

D

C

F

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R

R

A

A

F

I

N

H

T

T

A

L

K

W

-

N

-

V

L

L

I

D

A

E

S

L

T

D

K

Q

G

A

I

W

S

L

P

P

I

V

I

E

E

K

D

S

-

W

D

K

L

L

R

N

E
|
E

I
x
R

N
x
H

F
x
Y

G

G

L

A

W

L

E

Q

G

G

L

L

T

N

I
x
K

K

A

E

E

M

T

K

A

S

E

K
|
K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

K

I

Q

W

W

R
|
R

-
x
R

-

G

-

F

-

A

-

V

-

T

-

P

-

E

-

L

-

T

N

K

D

D

T

D

E

E

D

R

G

Y

P

P

-

G

-

H

-

D

-

P

-

R

-

Y

-

A

-

K

L

L

C

S

G

E

G

K

D

E

L

L

S

P

I

L

K

T

R

E

A

S

S

L

I

A

R

L

V

T

E

I

H

D

A

R

V

V

L

I

K

P

I

Y

V

W

N

N

D

E

N

T

-

I

-

L

-

P

-

R

-

M

-

K

K

S

G

G

K

E

N

R

I

V

V

I

V

A

A

A

H
|
H

G
|
G

G
x
N

I

S

I

L

K

R

A

A

A

L

L

V

I

K

A

Y

L

L

F

D

N

N

W

M

N

S

M

E

A

E

M

E

Y

I

H

L

R

E

I

L

L

N

L

I

G

P

N

T

T

G

S

V

I

P

C

L

K

V

I

Y

E

E

F

F

N

D

E

E

N

N

N

F

I

K

P

P

10:17 (vs. 9:16, 75% identical) binding substrate
H11 (= H10) active site, Tele-phosphohistidine intermediate
K18 (≠ V17) modified: N6-acetyllysine
TG 23:24 (≠ QG 22:23) binding substrate
E89 (= E82) active site, Proton donor/acceptor
ERHY 89:92 (≠ EINF 82:85) binding substrate
K100 (≠ I93) binding substrate; modified: N6-acetyllysine
K106 (= K99) modified: N6-acetyllysine
RR 116:117 (≠ R- 108) binding substrate
H184 (= H151) Transition state stabilizer
GN 185:186 (≠ GG 152:153) binding substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
28% identity, 70% coverage: 5:157/219 of query aligns to 4:188/229 of 3gp3A

query
sites
3gp3A

V

L

L

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

E

T

W

W

N

N

V

K

Q

E

G

N

R

R

F

F

Q
x
T

G

G

C

W

H

V

D

D

I

V

N

D

L

L

T

T

D

E

N

Q

G

G

I

N

E

R

Q

E

A

A

K

R

R

Q

V

A

A

G

K

Q

R

L

L

L

E

K

G

E

-

A

-

G

-

Y

S

T

F

F

D

D

C

I

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R
|
R

A

A

F

I

N

R

T

T

A

L

K

W

L

H

I

V

A

Q

S

D

T

Q

K

M

G

D

I

L

S

M

-

Y

-

V

P

P

I

V

E

H

D

S

-

W

D

R

L

L

R

N

E
|
E

I

R

N

H

F
x
Y

G

G

L

A

W

L

E

S

G

G

L

L

T

N

I
x
K

K

A

E

E

M

T

K

A

S

A

K

K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

L

I

V

W

W

R
|
R

N
x
R

-

S

-

Y

D

D

T

T

E

P

D

P

G

P

P

A

L

L

C

E

G

P

G

G

D

D

L

E

S

R

I

A

K

P

R

Y

A

A

S

D

I

P

R

R

V

Y

E

A

H

K

A

V

-

P

-

R

-

E

-

Q

-

L

-

P

-

L

-

T

-

E

-

C

-

L

-

K

-

D

-

T

-

V

-

A

-

R

V

V

L

L

K

P

I

L

V

W

N

N

D

E

N

S

-

I

-

A

-

P

-

A

-

V

-

K

K

A

G

G

K

K

N

Q

I

V

V

L

V

I

V

A

A

A

H
|
H

G
|
G

G
x
N

I

S

I

L

K

R

A

A

active site: H9 (= H10), R60 (= R58), E87 (= E82), H182 (= H151)
binding phosphite ion: R8 (= R9), H9 (= H10), R60 (= R58), E87 (= E82), H182 (= H151), G183 (= G152)
binding phosphoserine: T21 (≠ Q22), E87 (= E82), Y90 (≠ F85), K98 (≠ I93), R114 (= R108), R115 (≠ N109), N184 (≠ G153)

3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
28% identity, 70% coverage: 5:157/219 of query aligns to 4:188/230 of 3fdzA

query
sites
3fdzA

V

L

L

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

E

T

W

W

N
|
N

V

K

Q

E

G

N

R

R

F

F

Q
x
T

G

G

C

W

H

V

D

D

I

V

N

D

L

L

T

T

D

E

N

Q

G

G

I

N

E

R

Q

E

A

A

K

R

R

Q

V

A

A

G

K

Q

R

L

L

L

E

K

G

E

-

A

-

G

-

Y

S

T

F

F

D

D

C

I

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R
|
R

A

A

F

I

N

R

T

T

A

L

K

W

L

H

I

V

A

Q

S

D

T

Q

K

M

G

D

I

L

S

M

-

Y

-

V

P

P

I

V

E

H

D

S

-

W

D

R

L

L

R

N

E
|
E

I

R

N

H

F
x
Y

G

G

L

A

W

L

E

S

G

G

L

L

T

N

I
x
K

K

A

E

E

M

T

K

A

S

A

K

K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

L

I

V

W

W

R
|
R

N
x
R

-

S

-

Y

D

D

T

T

E

P

D

P

G

P

P

A

L

L

C

E

G

P

G

G

D

D

L

E

S

R

I

A

K

P

R

Y

A

A

S

D

I

P

R

R

V

Y

E

A

H

K

A

V

-

P

-

R

-

E

-

Q

-

L

-

P

-

L

-

T

-

E

-

C

-

L

-

K

-

D

-

T

-

V

-

A

-

R

V

V

L

L

K

P

I

L

V

W

N

N

D

E

N

S

-

I

-

A

-

P

-

A

-

V

-

K

K

A

G

G

K

K

N

Q

I

V

V

L

V

I

V

A

A

A

H
|
H

G
|
G

G
x
N

I

S

I

L

K

R

A

A

active site: H9 (= H10), R60 (= R58), E87 (= E82), H182 (= H151)
binding (2R)-2,3-diphosphoglyceric acid: R8 (= R9), H9 (= H10), N15 (= N16), T21 (≠ Q22), R60 (= R58), E87 (= E82), Y90 (≠ F85), K98 (≠ I93), R114 (= R108), R115 (≠ N109), H182 (= H151), G183 (= G152), N184 (≠ G153)

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)
28% identity, 70% coverage: 5:157/219 of query aligns to 4:188/249 of Q3JWH7

query
sites
Q3JWH7

V

L

L

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

E

T

W

W

N
|
N

V

K

Q

E

G

N

R

R

F

F

Q
x
T

G
|
G

C

W

H

V

D

D

I

V

N

D

L

L

T

T

D

E

N

Q

G

G

I

N

E

R

Q

E

A

A

K

R

R

Q

V

A

A

G

K

Q

R

L

L

L

E

K

G

E

-

A

-

G

-

Y

S

T

F

F

D

D

C

I

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R
|
R

A

A

F

I

N

R

T

T

A

L

K

W

L

H

I

V

A

Q

S

D

T

Q

K

M

G

D

I

L

S

M

-

Y

-

V

P

P

I

V

E

H

D

S

-

W

D

R

L

L

R

N

E
|
E

I

R

N

H

F
x
Y

G

G

L

A

W

L

E

S

G

G

L

L

T

N

I
x
K

K

A

E

E

M

T

K

A

S

A

K

K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

L

I

V

W

W

R
|
R

N
x
R

-

S

-

Y

D

D

T

T

E

P

D

P

G

P

P

A

L

L

C

E

G

P

G

G

D

D

L

E

S

R

I

A

K

P

R

Y

A

A

S

D

I

P

R

R

V

Y

E

A

H

K

A

V

-

P

-

R

-

E

-

Q

-

L

-

P

-

L

-

T

-

E

-

C

-

L

-

K

-

D

-

T

-

V

-

A

-

R

V

V

L

L

K

P

I

L

V

W

N

N

D

E

N

S

-

I

-

A

-

P

-

A

-

V

-

K

K

A

G

G

K

K

N

Q

I

V

V

L

V

I

V

A

A

A

H
|
H

G
|
G

G
x
N

I

S

I

L

K

R

A

A

R8 (= R9) binding (2R)-2,3-bisphosphoglycerate
H9 (= H10) active site, Tele-phosphohistidine intermediate; binding (2R)-2,3-bisphosphoglycerate
N15 (= N16) binding (2R)-2,3-bisphosphoglycerate
T21 (≠ Q22) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
G22 (= G23) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
R60 (= R58) binding (2R)-2,3-bisphosphoglycerate
E87 (= E82) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
Y90 (≠ F85) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
K98 (≠ I93) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
R114 (= R108) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
R115 (≠ N109) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate
H182 (= H151) binding (2R)-2,3-bisphosphoglycerate
G183 (= G152) binding (2R)-2,3-bisphosphoglycerate
N184 (≠ G153) binding (2R)-2,3-bisphosphoglycerate; binding (2R)-3-phosphoglycerate

3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
28% identity, 70% coverage: 5:157/219 of query aligns to 4:188/248 of 3gp5A

query
sites
3gp5A

V

L

L

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

E

T

W

W

N
|
N

V

K

Q

E

G

N

R

R

F

F

Q

T

G

G

C

W

H

V

D

D

I

V

N

D

L

L

T

T

D

E

N

Q

G

G

I

N

E

R

Q

E

A

A

K

R

R

Q

V

A

A

G

K

Q

R

L

L

L

E

K

G

E

-

A

-

G

-

Y

S

T

F

F

D

D

C

I

V

A

Y

Y

A

T

S

S

P

V

L

L

K

K

R
|
R

A

A

F

I

N

R

T

T

A

L

K

W

L

H

I

V

A

Q

S

D

T

Q

K

M

G

D

I

L

S

M

-

Y

-

V

P

P

I

V

E

H

D

S

-

W

D

R

L

L

R

N

E
|
E

I

R

N

H

F

Y

G

G

L

A

W

L

E

S

G

G

L

L

T

N

I

K

K

A

E

E

M

T

K

A

S

A

K

K

F

Y

P

G

K

D

E

E

-

Q

F

V

D

L

I

V

W

W

R

R

N

R

-

S

-

Y

D

D

T

T

E

P

D

P

G

P

P

A

L

L

C

E

G

P

G

G

D

D

L

E

S

R

I

A

K

P

R

Y

A

A

S

D

I

P

R

R

V

Y

E

A

H

K

A

V

-

P

-

R

-

E

-

Q

-

L

-

P

-

L

-

T

-

E

-

C

-

L

-

K

-

D

-

T

-

V

-

A

-

R

V

V

L

L

K

P

I

L

V

W

N

N

D

E

N

S

-

I

-

A

-

P

-

A

-

V

-

K

K

A

G

G

K

K

N

Q

I

V

V

L

V

I

V

A

A

A

H
|
H

G
|
G

G

N

I

S

I

L

K

R

A

A

active site: H9 (= H10), R60 (= R58), E87 (= E82), H182 (= H151)
binding vanadate ion: R8 (= R9), H9 (= H10), N15 (= N16), R60 (= R58), E87 (= E82), H182 (= H151), G183 (= G152)

Q9HIJ2 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (see paper)
28% identity, 89% coverage: 6:200/219 of query aligns to 5:188/200 of Q9HIJ2

query
sites
Q9HIJ2

L

I

L

L

V

I

R

R

H
|
H

G

G

E

E

T

S

E

D

W

I

N

N

V

V

Q

K

G

G

R

I

F

L

Q

S

G

D

C

T

H

I

D

D

I

N

N

N

-

M

L

L

T

T

D

E

N

K

G

G

I

M

E

R

Q

Q

A

A

K

E

R

H

V

A

A

A

K

A

R

E

L

L

E

K

G

G

-

I

S

D

F

I

D

K

C

N

V

F

Y

Y

A

S

S

S

P

P

L

I

K

K

R

R

A

A

F

F

N

D

T

T

A

A

K

Q

L

I

I

I

A

A

S

D

T

S

K

F

G

N

I

K

S

D

P

V

I

V

I

T

E

D

D

Q

D

R

L

L

R

I

E

E

I

I

N

G

F

L

G

G

L

K

W

A

E

R

G

G

L

R

T

K

I

A

K

N

E

E

M

-

K

-

S

-

K

-

F

-

P

-

K

-

E

-

F

-

D

-

I

-

W

F

R

T

N

N

D

G

T

L

E

Y

D

S

G

G

P

H

L

I

C

T

G

G

G

K

-

I

-

R

-

E

D

D

L

L

S

E

I

M

K

E

R

K

A

W

S

D

I

-

R

S

V

L

E

Q

H

K

A

R

V

V

L

V

K

E

I

A

V

I

N

A

D

S

N

R

K

E

G

G

K

I

N

N

I

-

V

V

V

Y

V

V

A

T

H

H

G

S

G

D

I

P

I

I

K

R

A

A

L

I

I

S

A

Y

L

F

F

L

N

E

W

M

N

G

M

E

A

E

M

E

Y

T

H

Y

R

G

I

L

L

S

L

I

G

K

N

N

T

A

S

S

I

M

C

T

K

V

I

I

E

D

F

V

N

-

E

-

N

-

N

E

I

I

P

G

K

R

I

I

V

L

T

T

I

L

N

G

D

A

V

I

S

S

H9 (= H10) mutation to A: Loss of activity.

Query Sequence

>WP_010966303.1 NCBI__GCF_000008765.1:WP_010966303.1
MKTTVLLVRHGETEWNVQGRFQGCHDINLTDNGIEQAKRVAKRLEGSFDCVYASPLKRAF
NTAKLIASTKGISPIIEDDLREINFGLWEGLTIKEMKSKFPKEFDIWRNDTEDGPLCGGD
LSIKRASIRVEHAVLKIVNDNKGKNIVVVAHGGIIKAALIALFNWNMAMYHRILLGNTSI
CKIEFNENNIPKIVTINDVSHLPEEYAEKDPMHDKKEIV

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