SitesBLAST

R12 (= R8) binding substrate; 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 (= S15) mutation to A: Leads to reduced substrate affinity.
Y24 (≠ H20) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ HT 20:21) 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 (= E79) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EWAY 79:82) binding substrate
Y102 (= Y82) mutation to A: Impairs catalytic activity.
W131 (= W103) mutation to A: Leads to reduced substrate affinity.
H176 (= H143) mutation to A: Impairs catalytic activity.
H178 (= H145) mutation to A: Leads to low activity and reduced substrate affinity.
R181 (= R148) binding substrate; mutation to A: Leads to reduced substrate affinity.

Sites not aligning to the query:

244 binding substrate

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
34% identity, 70% coverage: 5:157/218 of query aligns to 7:188/269 of 3lg2A

query
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3lg2A

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active site: H11 (= H9), R67 (= R58), E97 (= E79)
binding phosphate ion: R10 (= R8), H11 (= H9), T23 (= T21), R67 (= R58), E97 (= E79), H174 (= H143), H176 (= H145), R179 (= R148)

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)
33% identity, 70% coverage: 5:157/218 of query aligns to 6:187/260 of 3oi7A

query
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3oi7A

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active site: A10 (≠ H9), R66 (= R58), E96 (= E79)
binding magnesium ion: T13 (= T12), T22 (= T21), R66 (= R58)
binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: R9 (= R8), Y21 (≠ H20), T22 (= T21), R66 (= R58), E96 (= E79), Y99 (= Y82), H173 (= H143), H175 (= H145), R178 (= R148)

3ll4A Structure of the h13a mutant of ykr043c in complex with fructose-1,6- bisphosphate (see paper)
33% identity, 70% coverage: 5:157/218 of query aligns to 7:188/261 of 3ll4A

query
sites
3ll4A

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active site: A11 (≠ H9), R67 (= R58), E97 (= E79)
binding 1,6-fructose diphosphate (linear form): R10 (= R8), Y22 (≠ H20), T23 (= T21), R67 (= R58), E97 (= E79), H174 (= H143), G175 (= G144), H176 (= H145), R179 (= R148)

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
27% identity, 89% coverage: 1:193/218 of query aligns to 1:196/196 of 6m1xC

query
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6m1xC

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binding 3-phosphoglyceric acid: R8 (= R8), H9 (= H9), Q21 (≠ T21), R57 (= R58), E79 (= E79), H146 (= H143), G147 (= G144)

5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
27% identity, 89% coverage: 1:194/218 of query aligns to 1:197/198 of 5zr2C

query
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5zr2C

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binding phosphoserine: R8 (= R8), Q21 (≠ T21), G22 (≠ S22), R57 (= R58), E79 (= E79), H146 (= H143), G147 (= G144)

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
27% identity, 89% coverage: 1:193/218 of query aligns to 1:200/207 of 4ij6A

query
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4ij6A

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L

L

active site: R8 (= R8), A9 (≠ H9), N15 (≠ S15), R58 (= R58), E82 (= E79), H150 (= H143)
binding phosphoserine: R8 (= R8), Q21 (≠ T21), R58 (= R58), E82 (= E79), H85 (≠ Y82), H150 (= H143), T151 (≠ G144)

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)
30% identity, 64% coverage: 4:142/218 of query aligns to 6:153/257 of Q7ZVE3

query
sites
Q7ZVE3

I

L

V

T

L

I

I

V

R

R

H
|
H

G

G

E

E

T

T

K

Q

W

Y

S

N

K

R

-

D

-

K

-

L

T

Q

G

G

Q

Q

H

-

T

-

S

-

T

G

T

I

D

D

L

T

Q

P

L

L

T

S

E

D

V

T

G

G

A

H

Q

Q

A

A

Q

A

G

A

I

A

A

G

Q

R

L

Y

L

L

R

K

H

D

W

L

D

H

I

F

R

T

T

N

V

V

W

F

S

V

S

S

P

N

R

L

T

Q

R

R

A

A

I

I

N

Q

T

T

A

A

E

E

L

I

-

I

-

L

-

G

-

N

-

L

-

H

S

S

G

S

L

A

T

T

I

E

D

M

R

I

I

L

R

D

P

P

D

L

L

L

A

R

E

E

W

R

A

G

Y

F

G

G

D

V

A

A

E

E

G

G

K

R

T

P

R

K

Q

E

Q

H

I

L

D

K

E

N

S

M

D

A

P

N

G

A

W

A

S

G

L

Q

W

S

A

C

D

R

G

D

G

Y

I

T

G

P

P

P

G

G

E

E

T

T

V

L

E

E

S

Q

V

V

T

K

N

T

R

R

V

F

D

K

R

M

L

F

L

L

A

K

E

S

A

L

-

F

E

Q

P

R

L

M

L

L

E

E

S

E

G

H

D

G

V

S

A

A

L

L

V

S

S

S

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)
26% identity, 88% coverage: 1:191/218 of query aligns to 1:222/247 of P00950

query
sites
P00950

M
|
M

G

P

E

K

I

L

V

V

L

L

I

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

K
x
E

W
|
W

S
x
N

K

E

T

K

G

N

Q

L

H

F

T
|
T

S
x
G

T

W

T

V

D

D

L

V

Q

K

L

L

T

S

E

A

V

K

G

G

A

Q

Q

Q

Q

E

A

A

Q

A

G

R

I

A

A

G

Q

E

L

L

R

K

H

E

W

K

D

K

I

V

R

Y

-

P

-

D

T

V

V

L

W

Y

S

T

S

S

P

K

R

L

T

S

R
|
R

A

A

I

I

N

Q

T

T

A

A

E

N

L

I

S

A

G

L

L

E

T

K

I

A

D

D

R

R

I

L

-

W

R

I

P

P

-

V

-

N

-

R

-

S

-

W

D

R

L

L

A

N

E
|
E

W
x
R

A
x
H

Y
|
Y

G

G

D

D

A

L

E

Q

G

G

K

K

T

D

R
x
K

Q

A

Q

E

-

T

-

L

-

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-
x
R

-

S

-

F

-

D

-

V

-

P

I

I

D

D

E

A

S

S

D

S

P

P

G

F

W

S

S

Q

-

K

-

G

-

D

-

E

-

R

-

Y

L

K

W

Y

A

V

D

D

G

P

G

N

I

V

G

L

P

P

G

E

G

T

E

E

T

S

V

L

E

A

S

L

V

V

T

-

N

-

R

-

V

I

D

D

R

R

L

L

A

P

E

Y

-

W

-

Q

-

D

-

V

-

I

A

A

E
x
K

P

D

L

L

E

S

S

G

G

K

D

T

V

V

A

M

L

I

V

A

S

A

H
|
H

G
|
G

H
x
N

L

S

C

L

R

R

V

G

I

L

A

V

A

K

R

H

W

L

I

E

G

G

L

I

E

S

A

D

G

A

-

D

-

I

A

A

G

K

M

L

N

N

F

I

S

P

I

T

G

G

T

I

A

P

A

L

V

V

A

-

G

-

L

-

G

-

Y

F

E

E

Y

L

D

D

E

E

R

-

S

-

I

-

G

-

L

-

W

-

N

N

L

L

T

K

P

P

M1 (= M1) modified: Initiator methionine, Removed
8:15 (vs. 8:15, 50% identical) binding substrate
H9 (= H9) active site, Tele-phosphohistidine intermediate
TG 21:22 (≠ TS 21:22) binding substrate
R60 (= R58) binding substrate
ERHY 87:90 (≠ EWAY 79:82) binding substrate
K98 (≠ R90) binding substrate
RR 114:115 (vs. gap) binding substrate
K169 (≠ E130) mutation to P: Causes dissociation of the homotetramer to dimers at low concentrations.
H182 (= H143) mutation to A: Reduces kcat of the mutase reaction 10000-fold.
GN 183:184 (≠ GH 144:145) binding substrate

5hr5A Bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
30% identity, 72% coverage: 4:161/218 of query aligns to 226:381/424 of 5hr5A

query
sites
5hr5A

I

I

V

Y

L

L

I

C

R
|
R

H
|
H

G

G

E

E

T

S

K

E

W

F

S
x
N

K

L

T

L

G

G

Q

K

H
x
I

T
x
G

S

G

T

D

T

S

D

G

L

L

Q

S

L

V

T

R

E

-

V

-

G

G

A

K

Q

Q

Q

F

A

A

Q

Q

G

A

I

L

A

R

Q

K

L

F

L

L

R

E

H

E

W

Q

D

E

I

I

-

A

-

D

R

L

T

K

V

V

W

W

S

T

S

S

P

Q

R

L

T

K

R
|
R

A

T

I

I

N

Q

T

T

A

A

E

E

L

S

S

L

G

G

L

V

T

T

I

Y

D

E

R

Q

I

W

R

K

P

I

D

-

L

L

A

N

E
|
E

W

I

A

D

Y

A

G

G

D

V

A

C

E

E

G

E

K

M

T

T

R
x
Y

Q

A

Q

E

I

I

D

Q

E

E

S

Q

D

Y

P

P

G

D

W

E

S

F

L

A

W

L

A
x
R

D

D

G

E

I
x
K

-

Y

-

L

-

Y

-

R

G

Y

P

P

G

G

E

E

T

S

V
x
Y

E

Q

S

D

V

L

T

V

N

Q

R

R

V

L

D

E

R

P

L

V

L

I

A

M

E

E

A

L

E

E

P

-

L

-

E

R

S

Q

G

G

D

N

V

V

A

L

L

V

V

I

S

S

H
|
H

G
x
Q

H

A

L

V

C

M

R
|
R

V

C

I

L

A

L

A

A

R

Y

W

F

I

-

G

-

L

L

E

D

A

K

G

G

A

A

active site: R230 (= R8), H231 (= H9), N237 (≠ S15), R280 (= R58), E300 (= E79), H365 (= H143)
binding 6-O-phosphono-beta-D-fructofuranose: H231 (= H9), I242 (≠ H20), G243 (≠ T21), E300 (= E79), Y311 (≠ R90), R325 (≠ A104), K329 (≠ I108), Y340 (≠ V115), Q366 (≠ G144), R370 (= R148)

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)
29% identity, 70% coverage: 4:155/218 of query aligns to 253:404/531 of P26285

query
sites
P26285

I

I

V

Y

L

L

I

C

R

R

H

H

G

G

E

E

T

S

K

E

W

F

S

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K

L

T

L

G

G

Q

K

H

I

T

G

S

G

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D

T

S

D

G

L

L

Q

S

L

V

T

R

E

-

V

-

G

G

A

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Q

Q

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A

A

Q

Q

G

A

I

L

A

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Q

K

L

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L

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Q

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E

I

I

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A

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D

-

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R

A

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N

Q

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A

A

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E

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S

L

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G

L

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T

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K

P

I

D

-

L

L

A

N

E

E

W

I

A

D

Y

A

G

G

D

V

A

C

E

E

G

E

K

M

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T

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Y

Q

A

Q

E

I

I

D

Q

E

E

S

Q

D

Y

P

P

G

D

W

E

S

F

L

A

W

L

A

R

D

D

G

E

I

K

-

Y

-

L

-

Y

-

R

G

Y

P

P

G

G

E

E

T

S

V

Y

E

Q

S

D

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L

T

V

N

Q

R

R

V

L

D

E

R

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L

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L

I

A

M

E

E

A

L

E

E

P

-

L

-

E

R

S

Q

G

G

D

N

V

V

A

L

L

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V

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S

H

H

G

Q

H

A

L

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C

M

R

R

V

C

I

L

A

L

A

A

R

Y

W

F

I

L

Sites not aligning to the query:

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

1qhfA Yeast phosphoglycerate mutase-3pg complex structure to 1.7 a (see paper)
26% identity, 87% coverage: 3:191/218 of query aligns to 2:221/240 of 1qhfA

query
sites
1qhfA

E

K

I

L

V

V

L

L

I

V

R
|
R

H
|
H

G
|
G

E
x
Q

T
x
S

K

E

W

W

S
x
N

K

E

T

K

G

N

Q

L

H

F

T
|
T

S

G

T

W

T

V

D

D

L

V

Q

K

L

L

T

S

E

A

V

K

G

G

A

Q

Q

Q

Q

E

A

A

Q

A

G

R

I

A

A

G

Q

E

L

L

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H

E

W

K

D

K

I

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R

Y

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P

-

D

T

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V

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Y

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S

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K

R

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R
|
R

A

A

I

I

N

Q

T

T

A

A

E

N

L

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A

G

L

L

E

T

K

I

A

D

D

R

R

I

L

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W

R

I

P

P

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V

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N

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R

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D

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L

A

N

E
|
E

W

R

A

H

Y

Y

G

G

D

D

A

L

E

Q

G

G

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K

T

D

R

K

Q

A

Q

E

-

T

-

L

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K

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F

-

G

-

E

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K

-

F

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N

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F

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-

V

-

P

I

I

D

D

E

A

S

S

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S

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P

G

F

W

S

S

Q

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K

-

G

-

D

-

E

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R

-

Y

L

K

W

Y

A

V

D

D

G

P

G

N

I

V

G

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P

P

G

E

G

T

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L

E

A

S

L

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V

T

-

N

-

R

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D

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R

L

L

A

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E

Y

-

W

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D

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-

I

A

A

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K

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D

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L

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S

G

G

K

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V

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M

L

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A

S

A

H
|
H

G

G

H

N

L

S

C

L

R

R

V

G

I

L

A

V

A

K

R

H

W

L

I

E

G

G

L

I

E

S

A

D

G

A

-

D

-

I

A

A

G

K

M

L

N

N

F

I

S

P

I
x
T

G

G

T

I

A

P

A

L

V

V

A

-

G

-

L

-

G

-

Y

F

E

E

Y

L

D

D

E

E

R

-

S

-

I

-

G

-

L

-

W

-

N

N

L

L

T

K

P

P

active site: H8 (= H9), R59 (= R58), E86 (= E79), H181 (= H143)
binding 3-phosphoglyceric acid: R7 (= R8), H8 (= H9), G9 (= G10), Q10 (≠ E11), S11 (≠ T12), N14 (≠ S15), T20 (= T21), R59 (= R58), T207 (≠ I167)

5pgmE Saccharomyces cerevisiae phosphoglycerate mutase (see paper)
26% identity, 87% coverage: 3:191/218 of query aligns to 2:221/234 of 5pgmE

query
sites
5pgmE

E

K

I

L

V

V

L

L

I

V

R

R

H
|
H

G

G

E

Q

T

S

K

E

W

W

S

N

K

E

T

K

G

N

Q

L

H

F

T

T

S

G

T

W

T

V

D

D

L

V

Q

K

L

L

T

S

E

A

V

K

G

G

A

Q

Q

Q

Q

E

A

A

Q

A

G

R

I

A

A

G

Q

E

L

L

R

K

H

E

W

K

D

K

I

V

R

Y

-

P

-

D

T

V

V

L

W

Y

S

T

S

S

P

K

R

L

T

S

R
|
R

A

A

I

I

N

Q

T

T

A

A

E

N

L

I

S

A

G

L

L

E

T

K

I

A

D

D

R

R

I

L

-

W

R

I

P

P

-

V

-

N

-

R

-

S

-

W

D

R

L

L

A

N

E
|
E

W

R

A

H

Y

Y

G

G

D

D

A

L

E

Q

G

G

K

K

T

D

R

K

Q

A

Q

E

-

T

-

L

-

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-

R

-

S

-

F

-

D

-

V

-

P

I

I

D

D

E

A

S

S

D

S

P

P

G

F

W

S

S

Q

-

K

-

G

-

D

-

E

-

R

-

Y

L

K

W

Y

A

V

D

D

G

P

G

N

I

V

G

L

P

P

G

E

G

T

E

E

T

S

V

L

E

A

S

L

V

V

T

-

N

-

R

-

V

I

D

D

R

R

L

L

A

P

E

Y

-

W

-

Q

-

D

-

V

-

I

A

A

E

K

P

D

L

L

E

S

S

G

G

K

D

T

V

V

A

M

L

I

V

A

S

A

H
|
H

G

G

H

N

L

S

C

L

R

R

V

G

I

L

A

V

A

K

R

H

W

L

I

E

G

G

L

I

E

S

A

D

G

A

-

D

-

I

A

A

G

K

M

L

N

N

F

I

S

P

I

T

G

G

T

I

A

P

A

L

V

V

A

-

G

-

L

-

G

-

Y

F

E

E

Y

L

D

D

E

E

R

-

S

-

I

-

G

-

L

-

W

-

N

N

L

L

T

K

P

P

active site: H8 (= H9), R59 (= R58), E86 (= E79), H181 (= H143)

Sites not aligning to the query:

binding alanine: 231, 234

1bq4A Saccharomyces cerevisiae phosphoglycerate mutase in complex with benzene hexacarboxylate (see paper)
26% identity, 87% coverage: 3:191/218 of query aligns to 2:221/234 of 1bq4A

query
sites
1bq4A

E

K

I

L

V

V

L

L

I

V

R

R

H
|
H

G

G

E

Q

T

S

K

E

W

W

S

N

K

E

T

K

G

N

Q

L

H

F

T

T

S

G

T

W

T

V

D

D

L

V

Q

K

L

L

T

S

E

A

V

K

G

G

A

Q

Q

Q

Q

E

A

A

Q

A

G

R

I

A

A

G

Q

E

L

L

R

K

H

E

W

K

D

K

I

V

R

Y

-

P

-

D

T

V

V

L

W

Y

S

T

S

S

P

K

R

L

T

S

R
|
R

A

A

I

I

N

Q

T

T

A

A

E

N

L

I

S

A

G

L

L

E

T

K

I

A

D

D

R

R

I

L

-

W

R

I

P

P

-

V

-

N

-

R

-

S

-

W

D

R

L

L

A

N

E
|
E

W

R

A

H

Y
|
Y

G

G

D

D

A

L

E

Q

G

G

K

K

T

D

R

K

Q

A

Q

E

-

T

-

L

-

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-
x
R

-

S

-

F

-

D

-

V

-

P

I

I

D

D

E

A

S

S

D

S

P

P

G

F

W

S

S

Q

-

K

-

G

-

D

-

E

-

R

-

Y

L

K

W

Y

A

V

D

D

G

P

G

N

I

V

G

L

P

P

G

E

G

T

E

E

T

S

V

L

E

A

S

L

V

V

T

-

N

-

R

-

V

I

D

D

R

R

L

L

A

P

E

Y

-

W

-

Q

-

D

-

V

-

I

A

A

E

K

P

D

L

L

E

S

S

G

G

K

D

T

V

V

A

M

L

I

V

A

S

A

H
|
H

G

G

H
x
N

L

S

C

L

R

R

V

G

I

L

A

V

A

K

R

H

W

L

I

E

G

G

L

I

E

S

A

D

G

A

-

D

-

I

A

A

G

K

M

L

N
|
N

F

I

S

P

I

T

G

G

T

I

A

P

A

L

V

V

A

-

G

-

L

-

G

-

Y

F

E

E

Y

L

D

D

E

E

R

-

S

-

I

-

G

-

L

-

W

-

N

N

L

L

T

K

P

P

active site: H8 (= H9), R59 (= R58), E86 (= E79), H181 (= H143)
binding benzene hexacarboxylic acid: Y89 (= Y82), R113 (vs. gap), R114 (vs. gap), N183 (≠ H145), N204 (= N164)

1bq3A Saccharomyces cerevisiae phosphoglycerate mutase in complex with inositol hexakisphosphate (see paper)
26% identity, 87% coverage: 3:191/218 of query aligns to 2:221/234 of 1bq3A

query
sites
1bq3A

E

K

I

L

V

V

L

L

I

V

R
|
R

H
|
H

G

G

E

Q

T
x
S

K

E

W

W

S
x
N

K

E

T

K

G

N

Q
x
L

H
x
F

T
|
T

S

G

T

W

T

V

D

D

L

V

Q

K

L

L

T

S

E

A

V

K

G

G

A

Q

Q

Q

Q

E

A

A

Q

A

G

R

I

A

A

G

Q

E

L

L

R

K

H

E

W

K

D

K

I

V

R

Y

-

P

-

D

T

V

V

L

W

Y

S

T

S

S

P

K

R

L

T

S

R
|
R

A

A

I

I

N

Q

T

T

A

A

E

N

L

I

S

A

G

L

L

E

T

K

I

A

D

D

R

R

I

L

-

W

R

I

P

P

-

V

-

N

-

R

-

S

-

W

D

R

L

L

A

N

E
|
E

W

R

A

H

Y
|
Y

G

G

D

D

A

L

E

Q

G

G

K

K

T

D

R
x
K

Q

A

Q

E

-

T

-

L

-

K

-

F

-

G

-

E

-

K

-

F

-

N

-

T

-

Y

-
x
R

-

R

-

S

-

F

-

D

-

V

-

P

I

I

D

D

E

A

S

S

D

S

P

P

G

F

W

S

S

Q

-

K

-

G

-

D

-

E

-

R

-

Y

L

K

W

Y

A

V

D

D

G

P

G

N

I

V

G

L

P

P

G

E

G

T

E

E

T

S

V

L

E

A

S

L

V

V

T

-

N

-

R

-

V

I

D

D

R

R

L

L

A

P

E

Y

-

W

-

Q

-

D

-

V

-

I

A

A

E

K

P

D

L

L

E

S

S

G

G

K

D

T

V

V

A

M

L

I

V

A

S

A

H
|
H

G

G

H

N

L

S

C

L

R

R

V

G

I

L

A

V

A

K

R

H

W

L

I

E

G

G

L

I

E

S

A

D

G

A

-

D

-

I

A

A

G

K

M

L

N

N

F

I

S

P

I

T

G

G

T

I

A

P

A

L

V

V

A

-

G

-

L

-

G

-

Y

F

E

E

Y

L

D

D

E

E

R

-

S

-

I

-

G

-

L

-

W

-

N

N

L

L

T

K

P

P

active site: H8 (= H9), R59 (= R58), E86 (= E79), H181 (= H143)
binding inositol hexakisphosphate: R7 (= R8), S11 (≠ T12), N14 (≠ S15), L18 (≠ Q19), F19 (≠ H20), T20 (= T21), Y89 (= Y82), K97 (≠ R90), R113 (vs. gap)

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, 65% coverage: 3:144/218 of query aligns to 5:160/223 of P9WIC7

query
sites
P9WIC7

E

R

I

L

V

V

L

M

I

L

R
|
R

H
|
H

G

G

E

Q

T

T

K

D

W

Y

S
x
N

K

V

T

G

G

S

Q

R

H

M

T

Q

S

G

T

Q

T

L

D

D

L

T

Q

E

L

L

T

S

E

E

V

L

G

G

A

R

Q

T

Q

Q

A

A

Q

V

G

A

I

A

A

A

Q

E

L

V

L

L

R

G

H
x
K

W

R

D

Q

I

P

R

L

T

L

V

I

W

V

S

S

P

D

R

L

T

R

R
|
R

A

A

I

Y

N

D

T

T

A

A

-

V

-

K

-

L

-

G

E

E

L

R

S

T

G

G

L

L

T

V

I

V

D

-

R

R

I

V

R

D

P

T

D

R

L

L

A

R

E

E

W

T

A

H

Y

L

G

G

D

D

A

W

E

Q

G

G

K

L

T

T

R

H

Q

A

Q

Q

I

I

D

D

E

A

S

D

D

A

P

P

G

G

W

A

S

R

L

L

-

A

W

W

-

R

A

E

D

D

G

A

G

T

I

W

G

A

P

P

-

H

G

G

E

E

T

S

V

R

E

V

S

D

V

V

T

A

N

A

R

R

V

S

D

R

R

P

L

L

L

V

A

A

E

E

-

L

-

V

-

A

A

S

E

E

P

P

L

E

L

W

E

G

S

G

G

A

D

D

-

E

-

P

-

D

-

R

-

P

V

V

A

V

L

L

V

V

S

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 (≠ S15) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ H45) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R58) mutation to A: Loss of phosphatase activity.
H159 (= H143) 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.

5htkA Human heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
27% identity, 72% coverage: 4:161/218 of query aligns to 222:377/425 of 5htkA

query
sites
5htkA

I

I

V

Y

L

L

I

C

R
|
R

H
|
H

G

G

E

E

T

S

K

E

W

F

S
x
N

K

L

T

L

G

G

Q

K

H
x
I

T
x
G

S

G

T

D

T

S

D

G

L

L

Q

S

L

V

T

R

E

-

V

-

G

G

A

K

Q

Q

Q

F

A

A

Q

Q

G

A

I

L

A

R

Q

K

L

F

L

L

R

E

H

E

W

Q

D

E

I

I

R

T

-

D

-

L

T

K

V

V

W

W

S

T

S

S

P

Q

R

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T

K

R
|
R

A

T

I

I

N

Q

T

T

A

A

E

E

L

S

S

L

G

G

L

V

T

P

I

Y

D

E

-

Q

-

W

R

K

I

I

R

L

P

N

D
x
E

L

I

-

D

-

A

-

G

-

V

-

C

A

E

E

E

W

M

A

T

Y
|
Y

G

A

D

E

A

I

E

E

G

K

K

R

T

Y

R

P

Q

E

I

F

D

A

E

L

S
x
R

D

D

P

Q

G

E

W
x
K

S

Y

L

L

W

Y

A

R

D

-

G

-

I

-

G

Y

P

P

G

G

E

E

T

S

V
x
Y

E

Q

S

D

V

L

T

V

N

Q

R

R

V

L

D

E

R

P

L

V

L

I

A

M

E

E

A

L

E

E

P

-

L

-

E

R

S

Q

G

G

D

N

V

V

A

L

L

V

V

I

S

S

H
|
H

G
x
Q

H

A

L

V

C

M

R
|
R

V

C

I

L

A

L

A

A

R

Y

W

F

I

-

G

-

L

L

E

D

A

K

G

G

A

A

active site: R226 (= R8), H227 (= H9), N233 (≠ S15), R276 (= R58), E296 (≠ D76), H361 (= H143)
binding 6-O-phosphono-beta-D-fructofuranose: H227 (= H9), I238 (≠ H20), G239 (≠ T21), E296 (≠ D76), Y307 (= Y82), R321 (≠ S96), K325 (≠ W100), Y336 (≠ V115), Q362 (≠ G144), R366 (= R148)

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

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
34% identity, 65% coverage: 3:144/218 of query aligns to 3:158/209 of 4qihA

query
sites
4qihA

E

R

I

L

V

V

L

M

I

L

R
|
R

H
|
H

G

G

E

Q

T

T

K

D

W

Y

S

N

K

V

T

G

G

S

Q

R

H

M

T
x
Q

S

G

T

Q

T

L

D

D

L

T

Q

E

L

L

T

S

E

E

V

L

G

G

A

R

Q

T

Q

Q

A

A

Q

V

G

A

I

A

A

A

Q

E

L

V

L

L

R

G

H

K

W

R

D

Q

I

P

R

L

T

L

V

I

W

V

S

S

P

D

R

L

T

R

R
|
R

A

A

I

Y

N

D

T

T

A

A

-

V

-

K

-

L

-

G

E

E

L

R

S

T

G

G

L

L

T

V

I

V

D

-

R

R

I

V

R

D

P

T

D

R

L

L

A

R

E
|
E

W

T

A

H

Y

L

G

G

D

D

A

W

E

Q

G

G

K

L

T

T

R

H

Q

A

Q

Q

I

I

D

D

E

A

S

D

D

A

P

P

G

G

W

A

S

R

L

L

-

A

W

W

-

R

A

E

D

D

G

A

G

T

I

W

G

A

P

P

-

H

G

G

E

E

T

S

V

R

E

V

S

D

V

V

T

A

N

A

R

R

V

S

D

R

R

P

L

L

L

V

A

A

E

E

-

L

-

V

-

A

A

S

E

E

P

P

L

E

L

W

E

G

S

G

G

A

D

D

-

E

-

P

-

D

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R

-

P

V

V

A

V

L

L

V

V

S

A

H
|
H

G

G

active site: H9 (= H9), R58 (= R58), E82 (= E79)
binding vanadate ion: R8 (= R8), H9 (= H9), Q21 (≠ T21), R58 (= R58), H157 (= H143)

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
34% identity, 65% coverage: 3:144/218 of query aligns to 4:159/217 of 4pzaB

query
sites
4pzaB

E

R

I

L

V

V

L

M

I

L

R
|
R

H
|
H

G

G

E

Q

T

T

K

D

W

Y

S

N

K

V

T

G

G

S

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H

M

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T

Q

T

L

D

D

L

T

Q

E

L

L

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S

E

E

V

L

G

G

A

R

Q

T

Q

Q

A

A

Q

V

G

A

I

A

A

A

Q

E

L

V

L

L

R

G

H

K

W

R

D

Q

I

P

R

L

T

L

V

I

W

V

S

S

P

D

R

L

T

R

R
|
R

A

A

I

Y

N

D

T

T

A

A

-

V

-

K

-

L

-

G

E

E

L

R

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T

G

G

L

L

T

V

I

V

D

-

R

R

I

V

R

D

P

T

D

R

L

L

A

R

E
|
E

W

T

A

H

Y

L

G

G

D

D

A

W

E

Q

G

G

K

L

T

T

R

H

Q

A

Q

Q

I

I

D

D

E

A

S

D

D

A

P

P

G

G

W

A

S

R

L

L

-

A

W

W

-

R

A

E

D

D

G

A

G

T

I

W

G

A

P

P

-

H

G

G

E

E

T

S

V

R

E

V

S

D

V

V

T

A

N

A

R

R

V

S

D

R

R

P

L

L

L

V

A

A

E

E

-

L

-

V

-

A

A

S

E

E

P

P

L

E

L

W

E

G

S

G

G

A

D

D

-

E

-

P

-

D

-

R

-

P

V

V

A

V

L

L

V

V

S

A

H
|
H

G
|
G

active site: H10 (= H9), R59 (= R58), E83 (= E79)
binding phosphate ion: R9 (= R8), H10 (= H9), R59 (= R58), E83 (= E79), H158 (= H143), G159 (= G144)

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)
27% identity, 72% coverage: 4:161/218 of query aligns to 252:407/505 of O60825

query
sites
O60825

I

I

V

Y

L

L

I

C

R

R

H

H

G

G

E

E

T

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K

E

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H

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S

L

V

T

R

E

-

V

-

G

G

A

K

Q

Q

Q

F

A

A

Q

Q

G

A

I

L

A

R

Q

K

L

F

L

L

R

E

H

E

W

Q

D

E

I

I

R

T

-

D

-

L

T

K

V

V

W

W

S

T

S

S

P

Q

R

L

T

K

R

R

A

T

I

I

N

Q

T

T

A

A

E

E

L

S

S

L

G

G

L

V

T

P

I

Y

D

E

-

Q

-

W

R

K

I

I

R

L

P

N

D

E

L

I

-

D

-

A

-

G

-

V

-

C

A

E

E

E

W

M

A

T

Y

Y

G

A

D

E

A

I

E

E

G

K

K

R

T

Y

R

P

Q

E

I

F

D

A

E

L

S

R

D

D

P

Q

G

E

W

K

S

Y

L

L

W

Y

A

R

D

-

G

-

I

-

G

Y

P

P

G

G

E

E

T

S

V

Y

E

Q

S

D

V

L

T

V

N

Q

R

R

V

L

D

E

R

P

L

V

L

I

A

M

E

E

A

L

E

E

P

-

L

-

E

R

S

Q

G

G

D

N

V

V

A

L

L

V

V

I

S

S

H

H

G

Q

H

A

L

V

C

M

R

R

V

C

I

L

A

L

A

A

R

Y

W

F

I

-

G

-

L

L

E

D

A

K

G

G

A

A

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

Query Sequence

>WP_025272194.1 NCBI__GCF_000527155.1:WP_025272194.1
MGEIVLIRHGETKWSKTGQHTSTTDLQLTEVGAQQAQGIAQLLRHWDIRTVWSSPRTRAI
NTAELSGLTIDRIRPDLAEWAYGDAEGKTRQQIDESDPGWSLWADGGIGPGGETVESVTN
RVDRLLAEAEPLLESGDVALVSHGHLCRVIAARWIGLEAGAGMNFSIGTAAVAGLGYEYD
ERSIGLWNLTPRLLGPPPTPSSEPDDWGGDNAFGGDVA

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