SitesBLAST

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, 69% coverage: 11:168/230 of query aligns to 6:152/257 of Q7ZVE3

query
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Q7ZVE3

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H11 (= H16) active site, Tele-phosphohistidine intermediate

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
25% identity, 91% coverage: 8:216/230 of query aligns to 1:203/207 of 4ij6A

query
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active site: R8 (= R15), A9 (≠ H16), N15 (= N22), R58 (= R67), E82 (= E95), H150 (= H163)
binding phosphoserine: R8 (= R15), Q21 (= Q28), R58 (= R67), E82 (= E95), H85 (≠ F98), H150 (= H163), T151 (≠ G164)

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, 68% coverage: 11:167/230 of query aligns to 10:167/211 of P36623

query
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P36623

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T37 (= T38) modified: Phosphothreonine
S62 (= S63) modified: Phosphoserine
Y96 (≠ F98) modified: Phosphotyrosine
S166 (≠ V166) modified: Phosphoserine

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)
34% identity, 61% coverage: 11:151/230 of query aligns to 6:141/270 of Q9NQ88

query
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Q9NQ88

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H11 (= H16) 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 (≠ D108) 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.

P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 90% coverage: 11:217/230 of query aligns to 8:228/271 of P36136

query
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P36136

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R12 (= R15) binding ; mutation to A: Impairs catalytic activity.
H13 (= H16) active site, Tele-phosphohistidine intermediate; mutation to A: Impairs catalytic activity.
T16 (= T19) mutation to A: Impairs catalytic activity.
S19 (≠ N22) mutation to A: Leads to reduced substrate affinity.
Y24 (≠ F27) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ FQ 27:28) binding
S65 (= S63) mutation to A: Leads to low activity and reduced substrate affinity.
R69 (= R67) binding ; mutation to A: Leads to reduced substrate affinity.
E99 (= E95) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EQAF 95:98) binding
Y102 (≠ F98) mutation to A: Impairs catalytic activity.
W131 (= W120) mutation to A: Leads to reduced substrate affinity.
H176 (= H163) mutation to A: Impairs catalytic activity.
H178 (≠ G165) mutation to A: Leads to low activity and reduced substrate affinity.
R181 (≠ D168) binding ; mutation to A: Leads to reduced substrate affinity.

Sites not aligning to the query:

244 binding

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
25% identity, 90% coverage: 11:217/230 of query aligns to 6:226/269 of 3lg2A

query
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3lg2A

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-

R

K

Q

K

S

C

D

E

I

T

P

I

N

E

A

E

G

I

L

Q

N

N

R

V

V

K

R

S

V

Y

S

D

G

D

E

D

A

T

V

V

E

P

V

Y

L

V

D

K

W

L

A

E

D

S

V

Y

R

R

H

H

L

L

A

V

D

D

L

N

P

P

active site: H11 (= H16), R67 (= R67), E97 (= E95)
binding phosphate ion: R10 (= R15), H11 (= H16), T23 (≠ Q28), R67 (= R67), E97 (= E95), H174 (= H163), H176 (≠ G165), R179 (≠ D168)

Sites not aligning to the query:

binding phosphate ion: 242, 266

3oi7A Structure of the structure of the h13a mutant of ykr043c in complex with sedoheptulose-1,7-bisphosphate (see paper)
25% identity, 90% coverage: 11:217/230 of query aligns to 5:225/260 of 3oi7A

query
sites
3oi7A

L

C

I

I

L

I

I

V

R
|
R

H
x
A

G

G

E

Q

T
|
T

D

E

W

W

N

S

R

K

E

S

L

G

R

Q

F
x
Y

Q
x
T

G

G

H

L

V

T

D

D

V

L

P

P

L

L

N

T

A

P

T

Y

G

G

H

E

E

G

Q

Q

A

M

R

L

R

R

L

T

A

G

E

E

R

S

L

V

A

F

A

R

E

N

K

N

L

Q

V

F

V

L

D

N

-

P

-

D

-

N

-

I

-

T

H

Y

L

I

V

F

C

T

S

S

D

P

L

R

I

L

R
|
R

T

A

R

R

Q

Q

T

T

A

V

T

D

P

L

S

V

L

L

Q

K

V

P

L

L

F

S

P

D

Q

E

-

Q

-

R

A

A

S

K

I

I

D

R

T

V

L

V

T

V

D

D

S

D

A

D

L

L

R

R

E
|
E

Q

W

A

E

F
x
Y

G

G

V

D

V

Y

D

E

G

G

K

M

R

L

V

T

D

R

D

E

V

I

K

I

Q

E

-

L

-

R

-

K

-

S

-

R

-

G

-

L

D

D

H

K

A

E

D

R

A

P

W

W

N

N

Q

I

W

W

L

R

R

D

F

-

E

-

A

-

D

-

Y

-

G

G

M

C

P

E

G

N

G

G

E

E

T

T

R

Q

Q

Q

F

I

H

G

T

L

R

R

V

L

M

S

N

R

A

A

V

I

Y

A

R

R

I

I

A

Q

Q

N

Q

L

H

H

A

R

G

K

Q

H

K

Q

-

S

-

E

-

G

-

R

-

A

-

S

-

D

V

I

M

M

V

V

V

F

T

A

H
|
H

G

G

G
x
H

V

A

L

L

D
x
R

M

Y

I

F

W

A

R

A

T

I

A

W

R

F

G

G

T

L

G

G

L

V

D

Q

G

-

P

-

R

K

Q

K

S

C

D

E

I

T

P

I

N

E

A

E

G

I

L

Q

N

N

R

V

V

K

R

S

V

Y

S

D

G

D

E

D

A

T

V

V

E

P

V

Y

L

V

D

K

W

L

A

E

D

S

V

Y

R

R

H

H

L

L

A

V

D

D

L

N

P

P

active site: A10 (≠ H16), R66 (= R67), E96 (= E95)
binding magnesium ion: T13 (= T19), T22 (≠ Q28), R66 (= R67)
binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: R9 (= R15), Y21 (≠ F27), T22 (≠ Q28), R66 (= R67), E96 (= E95), Y99 (≠ F98), H173 (= H163), H175 (≠ G165), R178 (≠ D168)

3ll4A Structure of the h13a mutant of ykr043c in complex with fructose-1,6- bisphosphate (see paper)
25% identity, 90% coverage: 11:217/230 of query aligns to 6:226/261 of 3ll4A

query
sites
3ll4A

L

C

I

I

L

I

I

V

R
|
R

H
x
A

G

G

E

Q

T

T

D

E

W

W

N

S

R

K

E

S

L

G

R

Q

F
x
Y

Q
x
T

G

G

H

L

V

T

D

D

V

L

P

P

L

L

N

T

A

P

T

Y

G

G

H

E

E

G

Q

Q

A

M

R

L

R

R

L

T

A

G

E

E

R

S

L

V

A

F

A

R

E

N

K

N

L

Q

V

F

V

L

D

N

-

P

-

D

-

N

-

I

-

T

H

Y

L

I

V

F

C

T

S

S

D

P

L

R

I

L

R
|
R

T

A

R

R

Q

Q

T

T

A

V

T

D

P

L

S

V

L

L

Q

K

V

P

L

L

F

S

P

D

Q

E

-

Q

-

R

A

A

S

K

I

I

D

R

T

V

L

V

T

V

D

D

S

D

A

D

L

L

R

R

E
|
E

Q

W

A

E

F

Y

G

G

V

D

V

Y

D

E

G

G

K

M

R

L

V

T

D

R

D

E

V

I

K

I

Q

E

-

L

-

R

-

K

-

S

-

R

-

G

-

L

D

D

H

K

A

E

D

R

A

P

W

W

N

N

Q

I

W

W

L

R

R

D

F

-

E

-

A

-

D

-

Y

-

G

G

M

C

P

E

G

N

G

G

E

E

T

T

R

Q

Q

Q

F

I

H

G

T

L

R

R

V

L

M

S

N

R

A

A

V

I

Y

A

R

R

I

I

A

Q

Q

N

Q

L

H

H

A

R

G

K

Q

H

K

Q

-

S

-

E

-

G

-

R

-

A

-

S

-

D

V

I

M

M

V

V

V

F

T

A

H
|
H

G
|
G

G
x
H

V

A

L

L

D
x
R

M

Y

I

F

W

A

R

A

T

I

A

W

R

F

G

G

T

L

G

G

L

V

D

Q

G

-

P

-

R

K

Q

K

S

C

D

E

I

T

P

I

N

E

A

E

G

I

L

Q

N

N

R

V

V

K

R

S

V

Y

S

D

G

D

E

D

A

T

V

V

E

P

V

Y

L

V

D

K

W

L

A

E

D

S

V

Y

R

R

H

H

L

L

A

V

D

D

L

N

P

P

active site: A11 (≠ H16), R67 (= R67), E97 (= E95)
binding 1,6-fructose diphosphate (linear form): R10 (= R15), Y22 (≠ F27), T23 (≠ Q28), R67 (= R67), E97 (= E95), H174 (= H163), G175 (= G164), H176 (≠ G165), R179 (≠ D168)

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)
43% identity, 30% coverage: 8:77/230 of query aligns to 1:70/247 of P00950

query
sites
P00950

M
|
M

T

P

E

K

L

L

I

V

L

L

I

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

D
x
E

W
|
W

N
|
N

R

E

E

K

L

N

R

L

F

F

Q
x
T

G
|
G

H

W

V

V

D

D

V

V

P

K

L

L

N

S

A

A

T

K

G

G

H

Q

E

Q

Q

E

A

A

R

A

R

R

L

A

A

G

E

E

R

L

L

L

A

K

A

E

E

K

K

K

L

V

V

Y

V

P

D

D

H

V

L

L

V

Y

C

T

S

S

D

K

L

L

I

S

R
|
R

T

A

R

I

Q

Q

T

T

A

A

T

N

P

I

S

A

L

L

Q

E

M1 (= M8) modified: Initiator methionine, Removed
8:15 (vs. 15:22, 63% identical) binding
H9 (= H16) active site, Tele-phosphohistidine intermediate
TG 21:22 (≠ QG 28:29) binding
R60 (= R67) binding

Sites not aligning to the query:

87:90 binding
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

5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
43% identity, 30% coverage: 10:77/230 of query aligns to 2:69/234 of 5pgmE

query
sites
5pgmE

E

K

L

L

I

V

L

L

I

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

R

E

E

K

L

N

R

L

F

F

Q

T

G

G

H

W

V

V

D

D

V

V

P

K

L

L

N

S

A

A

T

K

G

G

H

Q

E

Q

Q

E

A

A

R

A

R

R

L

A

A

G

E

E

R

L

L

L

A

K

A

E

E

K

K

K

L

V

V

Y

V

P

D

D

H

V

L

L

V

Y

C

T

S

S

D

K

L

L

I

S

R
|
R

T

A

R

I

Q

Q

T

T

A

A

T

N

P

I

S

A

L

L

Q

E

active site: H8 (= H16), R59 (= R67)

Sites not aligning to the query:

active site: 86, 181
binding alanine: 231, 234

1bq4A Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate (see paper)
43% identity, 30% coverage: 10:77/230 of query aligns to 2:69/234 of 1bq4A

query
sites
1bq4A

E

K

L

L

I

V

L

L

I

V

R

R

H
|
H

G

G

E

Q

T

S

D

E

W

W

N

N

R

E

E

K

L

N

R

L

F

F

Q

T

G

G

H

W

V

V

D

D

V

V

P

K

L

L

N

S

A

A

T

K

G

G

H

Q

E

Q

Q

E

A

A

R

A

R

R

L

A

A

G

E

E

R

L

L

L

A

K

A

E

E

K

K

K

L

V

V

Y

V

P

D

D

H

V

L

L

V

Y

C

T

S

S

D

K

L

L

I

S

R
|
R

T

A

R

I

Q

Q

T

T

A

A

T

N

P

I

S

A

L

L

Q

E

active site: H8 (= H16), R59 (= R67)

Sites not aligning to the query:

active site: 86, 181
binding benzene hexacarboxylic acid: 89, 113, 114, 183, 204

1bq3A Saccharomyces cerevisiae phosphoglycerate mutase in complex with inositol hexakisphosphate (see paper)
43% identity, 30% coverage: 10:77/230 of query aligns to 2:69/234 of 1bq3A

query
sites
1bq3A

E

K

L

L

I

V

L

L

I

V

R
|
R

H
|
H

G

G

E

Q

T
x
S

D

E

W

W

N
|
N

R

E

E

K

L

N

R
x
L

F
|
F

Q
x
T

G

G

H

W

V

V

D

D

V

V

P

K

L

L

N

S

A

A

T

K

G

G

H

Q

E

Q

Q

E

A

A

R

A

R

R

L

A

A

G

E

E

R

L

L

L

A

K

A

E

E

K

K

K

L

V

V

Y

V

P

D

D

H

V

L

L

V

Y

C

T

S

S

D

K

L

L

I

S

R
|
R

T

A

R

I

Q

Q

T

T

A

A

T

N

P

I

S

A

L

L

Q

E

active site: H8 (= H16), R59 (= R67)
binding inositol hexakisphosphate: R7 (= R15), S11 (≠ T19), N14 (= N22), L18 (≠ R26), F19 (= F27), T20 (≠ Q28)

Sites not aligning to the query:

active site: 86, 181
binding inositol hexakisphosphate: 89, 97, 113

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
43% identity, 30% coverage: 10:77/230 of query aligns to 2:69/240 of 1qhfA

query
sites
1qhfA

E

K

L

L

I

V

L

L

I

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

D

E

W

W

N
|
N

R

E

E

K

L

N

R

L

F

F

Q
x
T

G

G

H

W

V

V

D

D

V

V

P

K

L

L

N

S

A

A

T

K

G

G

H

Q

E

Q

Q

E

A

A

R

A

R

R

L

A

A

G

E

E

R

L

L

L

A

K

A

E

E

K

K

K

L

V

V

Y

V

P

D

D

H

V

L

L

V

Y

C

T

S

S

D

K

L

L

I

S

R
|
R

T

A

R

I

Q

Q

T

T

A

A

T

N

P

I

S

A

L

L

Q

E

active site: H8 (= H16), R59 (= R67)
binding 3-phosphoglyceric acid: R7 (= R15), H8 (= H16), G9 (= G17), Q10 (≠ E18), S11 (≠ T19), N14 (= N22), T20 (≠ Q28), R59 (= R67)

Sites not aligning to the query:

active site: 86, 181
binding 3-phosphoglyceric acid: 207

7n3rB The ternary complex of human bisphosphoglycerate mutase with 3- phosphoglycerate and 2-phosphoglycolate (see paper)
29% identity, 59% coverage: 10:144/230 of query aligns to 3:136/239 of 7n3rB

query
sites
7n3rB

E

K

L

L

I

I

L

M

I

L

R

R

H

H

G

G

E

E

T

G

D

A

W

W

N

N

R

K

E

E

L

N

R

R

F

F

Q
x
C

G
x
S

H

W

V

V

D

D

V

Q

P

K

L

L

N

N

A

S

T

E

G

G

H

M

E

E

Q

E

A

A

R

R

R

N

L

C

A

G

E

K

R

Q

L

L

A

K

A

A

E

L

K

N

L

F

V

E

V

F

D

D

H

L

L

V

V

F

C

T

S

S

D

V

L

L

I

N

R

R

T

S

R

I

Q

H

T

T

A

A

T

W

P

L

S

I

L

L

Q

E

V

E

L

L

F

-

P

G

Q

Q

A

E

S

W

I

V

D

P

T

V

L

E

T

S

D

S

S

W

A

R

L

L

R

N

E
|
E

Q

R

A

H

F

Y

G

G

V

A

V

L

D

I

G

G

K

L

R

N

V

R

D

E

D

Q

V

M

K

A

Q

L

D

N

H

H

A

G

D

E

A

E

W

Q

N

V

Q

R

W

L

L

W

R

R

F

R

E

S

A

Y

D

N

Y

V

G

T

M

P

P

P

G

P

G

I

E

E

T

E

T

S

R

H

Q

P

F

Y

H

Y

T

Q

R

E

V

I

M

Y

N

N

binding 2-phosphoglycolic acid: C21 (≠ Q28), S22 (≠ G29), E87 (= E95)

2f90A Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and alf4- (see paper)
29% identity, 59% coverage: 10:144/230 of query aligns to 3:136/254 of 2f90A

query
sites
2f90A

E

K

L

L

I

I

L

M

I

L

R
|
R

H
|
H

G

G

E

E

T

G

D

A

W

W

N

N

R

K

E

E

L

N

R

R

F

F

Q

C

G

S

H

W

V

V

D

D

V

Q

P

K

L

L

N

N

A

S

T

E

G

G

H

M

E

E

Q

E

A

A

R

R

R

N

L

C

A

G

E

K

R

Q

L

L

A

K

A

A

E

L

K

N

L

F

V

E

V

F

D

D

H

L

L

V

V

F

C

T

S

S

D

V

L

L

I

N

R
|
R

T

S

R

I

Q

H

T

T

A

A

T

W

P

L

S

I

L

L

Q

E

V

E

L

L

F

-

P

G

Q

Q

A

E

S

W

I

V

D

P

T

V

L

E

T

S

D

S

S

W

A

R

L

L

R

N

E
|
E

Q

R

A

H

F

Y

G

G

V

A

V

L

D

I

G

G

K

L

R

N

V

R

D

E

D

Q

V

M

K

A

Q

L

D

N

H

H

A

G

D

E

A

E

W

Q

N

V

Q

R

W

L

L

W

R

R

F

R

E

S

A

Y

D

N

Y

V

G

T

M

P

P

P

G

P

G

I

E

E

T

E

T

S

R

H

Q

P

F

Y

H

Y

T

Q

R

E

V

I

M

Y

N

N

active site: H9 (= H16), R60 (= R67), E87 (= E95)
binding tetrafluoroaluminate ion: R8 (= R15), H9 (= H16), R60 (= R67), E87 (= E95)

Sites not aligning to the query:

active site: 186
binding tetrafluoroaluminate ion: 186, 187

2h4zA Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate (see paper)
29% identity, 59% coverage: 10:144/230 of query aligns to 4:137/255 of 2h4zA

query
sites
2h4zA

E

K

L

L

I

I

L

M

I

L

R
|
R

H
|
H

G

G

E

E

T

G

D

A

W

W

N

N

R

K

E

E

L

N

R

R

F

F

Q
x
C

G
x
S

H

W

V

V

D

D

V

Q

P

K

L

L

N

N

A

S

T

E

G

G

H

M

E

E

Q

E

A

A

R

R

R

N

L

C

A

G

E

K

R

Q

L

L

A

K

A

A

E

L

K

N

L

F

V

E

V

F

D

D

H

L

L

V

V

F

C

T

S

S

D

V

L

L

I

N

R
|
R

T

S

R

I

Q

H

T

T

A

A

T

W

P

L

S

I

L

L

Q

E

V

E

L

L

F

-

P

G

Q

Q

A

E

S

W

I

V

D

P

T

V

L

E

T

S

D

S

S

W

A

R

L

L

R

N

E
|
E

Q

R

A

H

F
x
Y

G

G

V

A

V

L

D

I

G

G

K

L

R

N

V
x
R

D

E

D

Q

V

M

K

A

Q

L

D

N

H

H

A

G

D

E

A

E

W

Q

N

V

Q

R

W

L

L

W

R
|
R

F
x
R

E

S

A

Y

D

N

Y

V

G

T

M

P

P

P

G

P

G

I

E

E

T

E

T

S

R

H

Q

P

F

Y

H

Y

T

Q

R

E

V

I

M

Y

N

N

active site: H10 (= H16), R61 (= R67), E88 (= E95)
binding (2R)-2,3-diphosphoglyceric acid: R9 (= R15), H10 (= H16), C22 (≠ Q28), S23 (≠ G29), R61 (= R67), E88 (= E95), Y91 (≠ F98), R99 (≠ V106), R115 (= R122), R116 (≠ F123)

Sites not aligning to the query:

active site: 187
binding (2R)-2,3-diphosphoglyceric acid: 187, 189

P07738 Bisphosphoglycerate mutase; BPGM; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; 2,3-diphosphoglycerate mutase; DPGM; BPG-dependent PGAM; EC 5.4.2.4; EC 5.4.2.11 from Homo sapiens (Human) (see 5 papers)
29% identity, 59% coverage: 10:144/230 of query aligns to 5:138/259 of P07738

query
sites
P07738

E
x
K

L

L

I

I

L

M

I

L

R
|
R

H
|
H

G
|
G

E
|
E

T
x
G

D
x
A

W
|
W

N
|
N

R
x
K

E

E

L

N

R

R

F

F

Q
x
C

G
x
S

H

W

V

V

D

D

V

Q

P
x
K

L

L

N

N

A

S

T

E

G

G

H

M

E

E

Q

E

A

A

R

R

R

N

L

C

A

G

E
x
K

R

Q

L

L

A
x
K

A

A

E

L

K

N

L

F

V

E

V

F

D

D

H

L

L

V

V

F

C

T

S

S

D

V

L

L

I

N

R
|
R

T

S

R

I

Q

H

T

T

A

A

T

W

P

L

S

I

L

L

Q

E

V

E

L

L

F

-

P

G

Q

Q

A

E

S

W

I

V

D

P

T

V

L

E

T

S

D

S

S

W

A

R

L

L

R

N

E
|
E

Q
x
R

A
x
H

F
x
Y

G

G

V

A

V

L

D

I

G

G

K

L

R

N

V
x
R

D

E

D

Q

V

M

K

A

Q

L

D

N

H

H

A

G

D

E

A

E

W

Q

N

V

Q

R

W

L

L

W

R
|
R

F
x
R

E

S

A

Y

D

N

Y

V

G

T

M

P

P

P

G

P

G

I

E

E

T

E

T

S

R

H

Q

P

F

Y

H

Y

T

Q

R

E

V

I

M

Y

N

N

K5 (≠ E10) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
10:17 (vs. 15:22, 75% identical) binding
H11 (= H16) active site, Tele-phosphohistidine intermediate
K18 (≠ R23) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
CS 23:24 (≠ QG 28:29) binding
K29 (≠ P34) Not glycated
K43 (≠ E48) modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
K46 (≠ A51) Not glycated
R62 (= R67) binding
E89 (= E95) active site, Proton donor/acceptor
ERHY 89:92 (≠ EQAF 95:98) binding
R90 (≠ Q96) to C: in ECYT8; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity; dbSNP:rs121964925
R100 (≠ V106) binding
RR 116:117 (≠ RF 122:123) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
3 modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
143 Not glycated
159 modified: carbohydrate, N-linked (Glc) (glycation) lysine
181 Not glycated
188 Transition state stabilizer
189:190 binding
197 modified: carbohydrate, N-linked (Glc) (glycation) lysine; in vitro
246 Not glycated
247 Not glycated
253 Not glycated
258 Not glycated
259 Not glycated

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)
32% identity, 50% coverage: 8:122/230 of query aligns to 3:117/250 of P62707

query
sites
P62707

M

V

T

T

E

K

L

L

I

V

L

L

I

V

R
|
R

H
|
H

G
|
G

E
|
E

T
x
S

D
x
Q

W
|
W

N
|
N

R
x
K

E

E

L

N

R

R

F

F

Q
x
T

G
|
G

H

W

V

Y

D

D

V

V

P

D

L

L

N

S

A

E

T

K

G

G

H

V

E

S

Q

E

A

A

R

K

R

A

L

A

A

G

E

K

R

L

L

L

A

K

A

E

E

E

K

G

L

Y

V

S

V

F

D

D

H

F

L

A

V

Y

C

T

S

S

D

V

L

L

I

K

R

R

T

A

R

I

Q

H

T

T

A

L

T

W

P

N

S

V

L

L

Q

D

V

E

L

L

F

-

P

D

Q

Q

A

A

S

W

I

L

D

P

T

V

L

E

T

K

D

S

S

W

A

K

L

L

R

N

E
|
E

Q
x
R

A
x
H

F
x
Y

G

G

V

A

V

L

D

Q

G

G

K

L

R

N

V
x
K

D

A

D

E

V

T

K

A

Q

E

D
x
K

H

Y

A

G

D

D

A

E

W

Q

-

V

N

K

Q

Q

W

W

L
x
R

R
|
R

10:17 (vs. 15:22, 75% identical) binding
H11 (= H16) active site, Tele-phosphohistidine intermediate
K18 (≠ R23) modified: N6-acetyllysine
TG 23:24 (≠ QG 28:29) binding
E89 (= E95) active site, Proton donor/acceptor
ERHY 89:92 (≠ EQAF 95:98) binding
K100 (≠ V106) binding ; modified: N6-acetyllysine
K106 (≠ D112) modified: N6-acetyllysine
RR 116:117 (≠ LR 121:122) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
184 Transition state stabilizer
185:186 binding

Query Sequence

>Ac3H11_4818 FitnessBrowser__acidovorax_3H11:Ac3H11_4818
MHSIIERMTELILIRHGETDWNRELRFQGHVDVPLNATGHEQARRLAERLAAEKLVVDHL
VCSDLIRTRQTATPSLQVLFPQASIDTLTDSALREQAFGVVDGKRVDDVKQDHADAWNQW
LRFEADYGMPGGETTRQFHTRVMNAVYRIAQQHAGQKVMVVTHGGVLDMIWRTARGTGLD
GPRQSDIPNAGLNRVRVSGEAVEVLDWADVRHLADLPEQPVYDQTKLVVR

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