SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_057507005.1 NCBI__GCF_001431535.1:WP_057507005.1 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)
33% identity, 98% coverage: 1:208/213 of query aligns to 2:207/207 of 4ij6A

query
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4ij6A

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active site: R8 (= R7), A9 (≠ H8), N15 (= N14), R58 (= R57), E82 (= E81), H150 (= H150)
binding phosphoserine: R8 (= R7), Q21 (= Q20), R58 (= R57), E82 (= E81), H85 (= H84), H150 (= H150), T151 (≠ D151)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
33% identity, 79% coverage: 3:171/213 of query aligns to 4:171/207 of 1h2fA

query
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1h2fA

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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R57), E82 (= E81), H150 (= H150)
binding phosphate ion: G142 (≠ D142), E143 (≠ D143)
binding trivanadate: R8 (= R7), H9 (= H8), N15 (= N14), Q21 (= Q20), R58 (= R57), E82 (= E81), H150 (= H150), G151 (≠ D151), V152 (≠ A152)

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)
33% identity, 79% coverage: 3:171/213 of query aligns to 4:171/207 of 1h2eA

query
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1h2eA

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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R57), E82 (= E81), H150 (= H150)
binding phosphate ion: R8 (= R7), H9 (= H8), R58 (= R57), E82 (= E81), H150 (= H150)

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
30% identity, 78% coverage: 2:168/213 of query aligns to 5:192/269 of 3lg2A

query
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3lg2A

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active site: H11 (= H8), R67 (= R57), E97 (= E81)
binding phosphate ion: R10 (= R7), H11 (= H8), T23 (≠ Q20), R67 (= R57), E97 (= E81), H174 (= H150), H176 (≠ A152), R179 (= R155)

Sites not aligning to the query:

binding phosphate ion: 242, 266

P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 78% coverage: 2:168/213 of query aligns to 7:194/271 of P36136

query
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P36136

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R12 (= R7) binding substrate; mutation to A: Impairs catalytic activity.
H13 (= H8) active site, Tele-phosphohistidine intermediate; mutation to A: Impairs catalytic activity.
T16 (= T11) mutation to A: Impairs catalytic activity.
S19 (≠ N14) mutation to A: Leads to reduced substrate affinity.
Y24 (= Y19) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ YQ 19:20) binding substrate
S65 (= S53) mutation to A: Leads to low activity and reduced substrate affinity.
R69 (= R57) binding substrate; mutation to A: Leads to reduced substrate affinity.
E99 (= E81) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EIAH 81:84) binding substrate
Y102 (≠ H84) mutation to A: Impairs catalytic activity.
W131 (≠ L114) mutation to A: Leads to reduced substrate affinity.
H176 (= H150) mutation to A: Impairs catalytic activity.
H178 (≠ A152) mutation to A: Leads to low activity and reduced substrate affinity.
R181 (= R155) binding substrate; mutation to A: Leads to reduced substrate affinity.

Sites not aligning to the query:

244 binding substrate

3oi7A Structure of the structure of the h13a mutant of ykr043c in complex with sedoheptulose-1,7-bisphosphate (see paper)
30% identity, 78% coverage: 2:168/213 of query aligns to 4:191/260 of 3oi7A

query
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3oi7A

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active site: A10 (≠ H8), R66 (= R57), E96 (= E81)
binding magnesium ion: T13 (= T11), T22 (≠ Q20), R66 (= R57)
binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: R9 (= R7), Y21 (= Y19), T22 (≠ Q20), R66 (= R57), E96 (= E81), Y99 (≠ H84), H173 (= H150), H175 (≠ A152), R178 (= R155)

3ll4A Structure of the h13a mutant of ykr043c in complex with fructose-1,6- bisphosphate (see paper)
30% identity, 78% coverage: 2:168/213 of query aligns to 5:192/261 of 3ll4A

query
sites
3ll4A

R

R

I

C

L

I

A

V

R
|
R

H
x
A

G

G

E

Q

T

T

P

E

W

W

N

S

A

K

E

S

G

G

R

Q

Y
|
Y

Q
x
T

G

G

Q

L

I

T

D

D

I

L

P

P

L

L

S

T

P

P

I

Y

G

G

E

E

A

G

Q

Q

A

M

Q

L

A

R

L

T

G

G

E

E

R

S

-

V

-

F

-

R

-

N

-

Q

-

F

L

L

K

N

S

P

V

D

D

N

I

I

T

T

R

Y

A

I

V

F

A

T

S

S

P

P

L

R

S

L

R
|
R

A

A

Q

R

R

Q

T

T

A

V

Q

D

L

L

A

V

L

L

G

K

A

P

R

L

A

S

D

D

-

E

-

Q

-

R

-

A

-

K

-

I

M

R

L

V

T

V

E

D

P

D

E

D

L

L

Q

R

E
|
E

I

W

A

E

H

Y

G

G

E

D

W

Y

E

E

G

G

L

M

L

L

A

T

S

R

E

E

I

I

H

I

E

E

K

L

D

R

P

K

S

S

R

R

L

G

R

L

A

D

W

-

R

K

E

E

E

R

P

P

D

W

T

N

V

I

L

W

M

R

P

D

G

G

-

C

-

E

-

N

G

G

E

E

S

T

L

T

R

Q

L

Q

V

I

L

G

D

L

R

R

S

L

W

S

R

R

G

A

L

I

A

A

R

R

-

I

-

Q

-

N

-

L

-

H

-

R

-

K

-

H

A

Q

A

S

E

E

G

G

L

R

G

A

E

S

D

D

D

-

T

-

L

I

L

M

V

V

V

F

A

A

H
|
H

D
x
G

A
x
H

V

A

N

L

R
|
R

V

Y

I

F

L

A

C

A

R

I

I

W

L

F

G

G

L

L

P

G

I

V

S

Q

R

K

active site: A11 (≠ H8), R67 (= R57), E97 (= E81)
binding 1,6-fructose diphosphate (linear form): R10 (= R7), Y22 (= Y19), T23 (≠ Q20), R67 (= R57), E97 (= E81), H174 (= H150), G175 (≠ D151), H176 (≠ A152), R179 (= R155)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
39% identity, 60% coverage: 2:128/213 of query aligns to 3:128/209 of 4qihA

query
sites
4qihA

R

R

I

L

L

V

L

M

A

L

R
|
R

H
|
H

G

G

E

Q

T

T

P

D

W

Y

N

N

A

V

E

G

G

S

R

R

Y

M

Q
|
Q

G

G

Q

Q

I

L

D

D

I

T

P

E

L

L

S

S

P

E

I

L

G

G

E

R

A

T

Q

Q

A

A

Q

V

A

A

L

A

G

A

E

E

R

V

L

L

K

G

S

K

V

R

D

Q

I

P

T

L

R

L

A

I

V

V

A

S

S

S

P

D

L

L

S

R

R
|
R

A

A

Q

Y

R

D

T

T

A

A

Q

-

L

V

A

K

L

L

G

G

A

E

R

R

A

T

D

G

M

L

L

V

-

R

T

V

E

D

P

T

E

R

L

L

Q

R

E
|
E

I

T

A

H

H

L

G

G

E

D

W

W

E

Q

G

G

L

L

L

T

A

H

S

A

E

Q

I

I

H

D

E

A

K

D

D

A

P

P

S

G

R

A

L

R

R

L

A

A

W

W

R

R

E

E

E

-

P

-

D

D

T

A

V

T

L

W

M

A

P

P

-

H

G

G

E

E

S

S

L

R

R

V

L

D

V

V

L

A

D

A

R

R

S

S

active site: H9 (= H8), R58 (= R57), E82 (= E81)
binding vanadate ion: R8 (= R7), H9 (= H8), Q21 (= Q20), R58 (= R57)

Sites not aligning to the query:

binding vanadate ion: 157

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)
39% identity, 60% coverage: 2:128/213 of query aligns to 5:130/223 of P9WIC7

query
sites
P9WIC7

R

R

I

L

L

V

L

M

A

L

R
|
R

H
|
H

G

G

E

Q

T

T

P

D

W

Y

N
|
N

A

V

E

G

G

S

R

R

Y

M

Q

Q

G

G

Q

Q

I

L

D

D

I

T

P

E

L

L

S

S

P

E

I

L

G

G

E

R

A

T

Q

Q

A

A

Q

V

A

A

L

A

G

A

E

E

R

V

L

L

K

G

S
x
K

V

R

D

Q

I

P

T

L

R

L

A

I

V

V

A

S

S

S

P

D

L

L

S

R

R
|
R

A

A

Q

Y

R

D

T

T

A

A

Q

-

L

V

A

K

L

L

G

G

A

E

R

R

A

T

D

G

M

L

L

V

-

R

T

V

E

D

P

T

E

R

L

L

Q

R

E

E

I

T

A

H

H

L

G

G

E

D

W

W

E

Q

G

G

L

L

L

T

A

H

S

A

E

Q

I

I

H

D

E

A

K

D

D

A

P

P

S

G

R

A

L

R

R

L

A

A

W

W

R

R

E

E

E

-

P

-

D

D

T

A

V

T

L

W

M

A

P

P

-

H

G

G

E

E

S

S

L

R

R

V

L

D

V

V

L

A

D

A

R

R

S

S

R10 (= R7) mutation to A: Loss of phosphatase activity.
H11 (= H8) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N14) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ S44) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R57) mutation to A: Loss of phosphatase activity.

Sites not aligning to the query:

159 H→A: About 5% of wild-type phosphatase activity.
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)
39% identity, 60% coverage: 2:128/213 of query aligns to 4:129/217 of 4pzaB

query
sites
4pzaB

R

R

I

L

L

V

L

M

A

L

R
|
R

H
|
H

G

G

E

Q

T

T

P

D

W

Y

N

N

A

V

E

G

G

S

R

R

Y

M

Q

Q

G

G

Q

Q

I

L

D

D

I

T

P

E

L

L

S

S

P

E

I

L

G

G

E

R

A

T

Q

Q

A

A

Q

V

A

A

L

A

G

A

E

E

R

V

L

L

K

G

S

K

V

R

D

Q

I

P

T

L

R

L

A

I

V

V

A

S

S

S

P

D

L

L

S

R

R
|
R

A

A

Q

Y

R

D

T

T

A

A

Q

-

L

V

A

K

L

L

G

G

A

E

R

R

A

T

D

G

M

L

L

V

-

R

T

V

E

D

P

T

E

R

L

L

Q

R

E
|
E

I

T

A

H

H

L

G

G

E

D

W

W

E

Q

G

G

L

L

L

T

A

H

S

A

E

Q

I

I

H

D

E

A

K

D

D

A

P

P

S

G

R

A

L

R

R

L

A

A

W

W

R

R

E

E

E

-

P

-

D

D

T

A

V

T

L

W

M

A

P

P

-

H

G

G

E

E

S

S

L

R

R

V

L

D

V

V

L

A

D

A

R

R

S

S

active site: H10 (= H8), R59 (= R57), E83 (= E81)
binding phosphate ion: R9 (= R7), H10 (= H8), R59 (= R57), E83 (= E81)

Sites not aligning to the query:

binding phosphate ion: 158, 159

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, 59% coverage: 3:127/213 of query aligns to 6:131/257 of Q7ZVE3

query
sites
Q7ZVE3

I

L

L

T

L

I

A

V

R

R

H
|
H

G

G

E

E

T

T

P

Q

W

Y

N

N

A

R

E

D

G

K

R

L

Y

L

Q

Q

G

G

Q

Q

-

G

I

I

D

D

I

T

P

P

L

L

S

S

P

D

I

T

G

G

E

H

A

Q

Q

Q

A

A

Q

A

A

A

L

A

G

G

E

R

R

Y

L

L

K

K

S

D

V

L

D

H

I

F

T

T

R

N

A

V

V

F

A

V

S

S

P

N

L

L

S

Q

R

R

A

A

Q

I

R

Q

T

T

A

A

Q

E

L

I

A

I

L

L

G

G

-

N

-

L

-

H

A

S

R

S

A

A

D

T

M

E

L

M

L

I

T

L

E

D

P

P

E

L

L

L

Q

R

E

E

I

R

A

G

H

F

G

G

E

V

W

A

E

E

G

G

L

R

L

P

A

K

S

E

E

H

I

L

H

K

E

N

K

M

D

A

P

N

S

A

R

A

L

G

R

Q

A

S

W

C

R

R

E

D

E

Y

P

T

D

P

T

-

V

-

L

-

M

-

P

P

G

G

E

E

S

T

L

L

R

E

L

Q

V

V

L

K

D

T

R

R

H11 (= H8) active site, Tele-phosphohistidine intermediate

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
40% identity, 45% coverage: 2:96/213 of query aligns to 3:94/196 of 6m1xC

query
sites
6m1xC

R

K

I

L

L

I

L

L

A

I

R
|
R

H
|
H

G

G

E

E

T

T

P

E

W

W

N

N

A

L

E

L

G

G

R

K

Y

I

Q
|
Q

G

G

Q

C

I

T

D

D

I

I

P

E

L

L

S

T

P

P

I

N

G

G

E

I

A

Q

Q

Q

A

A

Q

N

A

E

L

V

G

A

E

Q

R

Q

L

I

K

K

-

G

S

N

V

F

D

D

I

I

T

-

R

-

A

I

V

Y

A

S

S

S

P

P

L

L

S

H

R
|
R

A

A

Q

L

R

I

T

T

A

A

Q

Q

L

K

A

I

L

A

G

G

A

D

R

K

A

E

D

V

M

H

L

L

L

I

T

-

E

-

P

E

E

G

L

M

Q

K

E
|
E

I

I

A

P

H

F

G

G

E

T

W

W

E

E

G

G

L

H

L

T

A

F

S

E

E

E

I

L

H

N

binding 3-phosphoglyceric acid: R8 (= R7), H9 (= H8), Q21 (= Q20), R57 (= R57), E79 (= E81)

Sites not aligning to the query:

binding 3-phosphoglyceric acid: 146, 147

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)
37% identity, 57% coverage: 3:124/213 of query aligns to 6:128/270 of Q9NQ88

query
sites
Q9NQ88

I

L

L

T

L

V

A

V

R

R

H
|
H

G

G

E

E

T

T

P

R

W

F

N

N

A

K

E

E

G

K

R

I

Y

I

Q

Q

G

G

Q

Q

-

G

I

V

D

D

I

E

P

P

L

L

S

S

P

E

I

T

G

G

E

F

A

K

Q

Q

A

A

Q

A

A

A

L

A

G

G

E

I

R

F

L

L

K

N

S

N

V

V

D

K

I

F

T

T

R

H

A

A

V

F

A

S

S

S

P

D

L

L

S

M

R

R

A

T

Q

K

R

Q

T

T

A

M

Q

H

L

G

A

I

L

L

-

E

-

R

-

S

G

K

A

F

R

C

A

K

D

D

M

M

L

T

L

V

T

K

-

Y

E

D

P

S

E

R

L

L

Q

R

E

E

I

R

A

K

H

Y

G

G

E

V

W

V

E

E

G

G

L

K

L

A

A

L

S

S

E
|
E

I

L

H

R

E

-

K

-

D

-

P

-

S

A

R

M

L

A

R

K

A

A

W

A

R

R

E

E

P

C

D

P

T

V

V

F

L

T

M

P

P

P

G

G

E

E

S

T

L

L

R

D

L

Q

V

V

H11 (= H8) 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 (= E94) 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.

5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
39% identity, 45% coverage: 2:96/213 of query aligns to 3:94/198 of 5zr2C

query
sites
5zr2C

R

K

I

L

L

I

L

L

A

I

R
|
R

H

A

G

G

E

E

T

T

P

E

W

W

N

N

A

L

E

L

G

G

R

K

Y

I

Q
|
Q

G
|
G

Q

C

I

T

D

D

I

I

P

E

L

L

S

T

P

P

I

N

G

G

E

I

A

Q

Q

Q

A

A

Q

N

A

E

L

V

G

A

E

Q

R

Q

L

I

K

K

-

G

S

N

V

F

D

D

I

I

T

-

R

-

A

I

V

Y

A

S

S

S

P

P

L

L

S

H

R
|
R

A

A

Q

L

R

I

T

T

A

A

Q

Q

L

K

A

I

L

A

G

G

A

D

R

K

A

E

D

V

M

H

L

L

L

I

T

-

E

-

P

E

E

G

L

M

Q

K

E
|
E

I

I

A

P

H

F

G

G

E

T

W

W

E

E

G

G

L

H

L

T

A

F

S

E

E

E

I

L

H

N

binding phosphoserine: R8 (= R7), Q21 (= Q20), G22 (= G21), R57 (= R57), E79 (= E81)

Sites not aligning to the query:

binding phosphoserine: 146, 147

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)
34% identity, 59% coverage: 3:127/213 of query aligns to 10:139/211 of P36623

query
sites
P36623

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T37 (≠ I30) modified: Phosphothreonine
S62 (= S53) modified: Phosphoserine
Y96 (≠ H84) modified: Phosphotyrosine

Sites not aligning to the query:

166 modified: Phosphoserine

5hr5A Bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
33% identity, 75% coverage: 3:162/213 of query aligns to 226:377/424 of 5hr5A

query
sites
5hr5A

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active site: R230 (= R7), H231 (= H8), N237 (= N14), R280 (= R57), E300 (= E81), H365 (= H150)
binding 6-O-phosphono-beta-D-fructofuranose: H231 (= H8), I242 (≠ Y19), G243 (≠ Q20), E300 (= E81), Y311 (≠ A92), R325 (≠ W106), K329 (≠ P110), Y340 (≠ L121), Q366 (≠ D151), R370 (= R155)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 22, 23, 24, 25, 26, 27, 130, 141, 144, 145, 146, 402
binding citrate anion: 49, 52, 76, 103, 104, 171

P26285 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2; 6PF-2-K/Fru-2,6-P2ase 2; PFK/FBPase 2; 6PF-2-K/Fru-2,6-P2ase heart-type isozyme; EC 2.7.1.105; EC 3.1.3.46 from Bos taurus (Bovine) (see paper)
33% identity, 75% coverage: 3:162/213 of query aligns to 253:404/531 of P26285

query
sites
P26285

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Sites not aligning to the query:

467 modified: Phosphoserine; by PKA
476 modified: Phosphothreonine; by AMPK and PKC

5htkA Human heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
32% identity, 75% coverage: 3:162/213 of query aligns to 222:373/425 of 5htkA

query
sites
5htkA

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active site: R226 (= R7), H227 (= H8), N233 (= N14), R276 (= R57), E296 (= E81), H361 (= H150)
binding 6-O-phosphono-beta-D-fructofuranose: H227 (= H8), I238 (≠ Y19), G239 (≠ Q20), E296 (= E81), Y307 (≠ A92), R321 (≠ W106), K325 (≠ P110), Y336 (≠ L121), Q362 (≠ D151), R366 (= R155)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 17, 18, 19, 20, 21, 22, 140, 144, 145, 146, 397, 398
binding citrate anion: 48, 61, 72, 99, 100, 167

O60825 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2; 6PF-2-K/Fru-2,6-P2ase 2; PFK/FBPase 2; 6PF-2-K/Fru-2,6-P2ase heart-type isozyme; EC 2.7.1.105; EC 3.1.3.46 from Homo sapiens (Human) (see 2 papers)
32% identity, 75% coverage: 3:162/213 of query aligns to 252:403/505 of O60825

query
sites
O60825

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Sites not aligning to the query:

466 modified: Phosphoserine; by AMPK; S→E: Constitutively active mutant that cannot be phosphorylated and further activated by AMPK.
468 modified: Phosphothreonine
483 modified: Phosphoserine; by BRAF
486 modified: Phosphoserine
493 modified: Phosphoserine

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
28% identity, 77% coverage: 2:164/213 of query aligns to 2:195/240 of 1qhfA

query
sites
1qhfA

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I

active site: H8 (= H8), R59 (= R57), E86 (= E81), H181 (= H150)
binding 3-phosphoglyceric acid: R7 (= R7), H8 (= H8), G9 (= G9), Q10 (≠ E10), S11 (≠ T11), N14 (= N14), T20 (≠ Q20), R59 (= R57)

Sites not aligning to the query:

binding 3-phosphoglyceric acid: 207

Query Sequence

>WP_057507005.1 NCBI__GCF_001431535.1:WP_057507005.1
MRILLARHGETPWNAEGRYQGQIDIPLSPIGEAQAQALGERLKSVDITRAVASPLSRAQR
TAQLALGARADMLLTEPELQEIAHGEWEGLLASEIHEKDPSRLRAWREEPDTVLMPGGES
LRLVLDRSWRGLARAAEGLGEDDTLLVVAHDAVNRVILCRILGLPISRLWSFRQAPTTLN
LLEGPDIEQLEVVRMNDCAHHTPFFGEAKHRAL

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