SitesBLAST

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
31% identity, 85% coverage: 1:168/197 of query aligns to 1:161/207 of 4ij6A

query
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4ij6A

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active site: R8 (= R8), A9 (≠ H9), N15 (= N15), R58 (= R62), E82 (= E89), H150 (= H154)
binding phosphoserine: R8 (= R8), Q21 (= Q21), R58 (= R62), E82 (= E89), H85 (≠ T92), H150 (= H154), T151 (≠ G155)

5hr5A Bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
28% identity, 83% coverage: 3:165/197 of query aligns to 225:376/424 of 5hr5A

query
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5hr5A

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active site: R230 (= R8), H231 (= H9), N237 (= N15), R280 (= R62), E300 (= E89), H365 (= H154)
binding 6-O-phosphono-beta-D-fructofuranose: H231 (= H9), I242 (≠ V20), G243 (≠ H23), E300 (= E89), Y311 (≠ K100), R325 (≠ E114), K329 (≠ H118), Y340 (≠ H129), Q366 (≠ G155), R370 (= R159)

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)
28% identity, 83% coverage: 3:165/197 of query aligns to 252:403/531 of P26285

query
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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)
29% identity, 83% coverage: 3:165/197 of query aligns to 221:372/425 of 5htkA

query
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5htkA

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active site: R226 (= R8), H227 (= H9), N233 (= N15), R276 (= R62), E296 (= E89), H361 (= H154)
binding 6-O-phosphono-beta-D-fructofuranose: H227 (= H9), I238 (≠ V20), G239 (≠ H23), E296 (= E89), Y307 (≠ K100), R321 (≠ E114), K325 (≠ H118), Y336 (≠ H129), Q362 (≠ G155), R366 (= R159)

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)
29% identity, 83% coverage: 3:165/197 of query aligns to 251:402/505 of O60825

query
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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

1bifA 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase bifunctional enzyme complexed with atp-g-s and phosphate (see paper)
27% identity, 83% coverage: 3:165/197 of query aligns to 214:365/432 of 1bifA

query
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active site: R219 (= R8), H220 (= H9), N226 (= N15), R269 (= R62), E289 (= E89), H354 (= H154)
binding phosphate ion: R219 (= R8), H220 (= H9), R269 (= R62), E289 (= E89), Y300 (≠ K100), R314 (≠ E114), K318 (≠ H118), Y329 (≠ H129), H354 (= H154), R359 (= R159)

Sites not aligning to the query:

binding phosphothiophosphoric acid-adenylate ester: 11, 12, 13, 14, 15, 16, 17, 131, 134, 136, 184, 210, 391

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, 77% coverage: 4:155/197 of query aligns to 6:160/223 of P9WIC7

query
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P9WIC7

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P

T

K

H

A

A

E

Q

L

I

A

D

A

A

R

D

H

A

P

P

G

G

M

A

L

R

E

L

G

A

E

W

G

R

L

E

D

D

H

A

W

-

V

T

F

W

R

A

C

P

P

H

G

G

E

E

S

S

H

R

H

V

D

D

V

V

A

A

S

A

R

R

L

S

A

R

H

P

W

L

L

V

A

A

D

E

L

L

A

V

-

A

-

S

-

E

-

P

-

E

-

W

-

G

-

A

-

D

-

E

P

P

G

D

D

R

K

P

V

V

I

V

A

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 (= N15) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ D49) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R62) mutation to A: Loss of phosphatase activity.
H159 (= H154) 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.

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
34% identity, 77% coverage: 4:155/197 of query aligns to 5:159/217 of 4pzaB

query
sites
4pzaB

V

L

I

V

L

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

V

D

W

Y

N

N

R

V

E

G

G

S

R

R

V

M

Q

Q

G

G

H

Q

G

L

D

D

S

T

P

E

L

L

T

S

P

E

K

L

G

G

A

R

A

T

Q

Q

A

A

R

V

A

A

Y

A

G

A

R

-

K

-

L

-

R

-

Q

E

M

V

L

L

G

G

D

K

A

R

G

Q

G

P

W

L

R

L

V

I

V

V

S

S

P

D

L

L

G

R

R
|
R

C

A

A

Y

Q

D

T

T

T

A

G

V

I

K

L

L

C

G

E

E

V

R

A

T

E

G

L

L

D

V

F

V

R

R

S

-

I

-

T

-

F

V

D

D

D

T

R

R

L

L

R

R

E
|
E

V

T

H

H

T

L

G

G

Q

D

W

W

S

Q

G

G

L

L

P

T

K

H

A

A

E

Q

L

I

A

D

A

A

R

D

H

A

P

P

G

G

M

A

L

R

E

L

G

A

E

W

G

R

L

E

D

D

H

A

W

-

V

T

F

W

R

A

C

P

P

H

G

G

E

E

S

S

H

R

H

V

D

D

V

V

A

A

S

A

R

R

L

S

A

R

H

P

W

L

L

V

A

A

D

E

L

L

A

V

-

A

-

S

-

E

-

P

-

E

-

W

-

G

-

A

-

D

-

E

P

P

G

D

D

R

K

P

V

V

I

V

A

L

V

V

S

A

H
|
H

G
|
G

active site: H10 (= H9), R59 (= R62), E83 (= E89)
binding phosphate ion: R9 (= R8), H10 (= H9), R59 (= R62), E83 (= E89), H158 (= H154), G159 (= G155)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
34% identity, 77% coverage: 4:155/197 of query aligns to 4:158/209 of 4qihA

query
sites
4qihA

V

L

I

V

L

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

V

D

W

Y

N

N

R

V

E

G

G

S

R

R

V

M

Q
|
Q

G

G

H

Q

G

L

D

D

S

T

P

E

L

L

T

S

P

E

K

L

G

G

A

R

A

T

Q

Q

A

A

R

V

A

A

Y

A

G

A

R

-

K

-

L

-

R

-

Q

E

M

V

L

L

G

G

D

K

A

R

G

Q

G

P

W

L

R

L

V

I

V

V

S

S

P

D

L

L

G

R

R
|
R

C

A

A

Y

Q

D

T

T

T

A

G

V

I

K

L

L

C

G

E

E

V

R

A

T

E

G

L

L

D

V

F

V

R

R

S

-

I

-

T

-

F

V

D

D

D

T

R

R

L

L

R

R

E
|
E

V

T

H

H

T

L

G

G

Q

D

W

W

S

Q

G

G

L

L

P

T

K

H

A

A

E

Q

L

I

A

D

A

A

R

D

H

A

P

P

G

G

M

A

L

R

E

L

G

A

E

W

G

R

L

E

D

D

H

A

W

-

V

T

F

W

R

A

C

P

P

H

G

G

E

E

S

S

H

R

H

V

D

D

V

V

A

A

S

A

R

R

L

S

A

R

H

P

W

L

L

V

A

A

D

E

L

L

A

V

-

A

-

S

-

E

-

P

-

E

-

W

-

G

-

A

-

D

-

E

P

P

G

D

D

R

K

P

V

V

I

V

A

L

V

V

S

A

H
|
H

G

G

active site: H9 (= H9), R58 (= R62), E82 (= E89)
binding vanadate ion: R8 (= R8), H9 (= H9), Q21 (= Q21), R58 (= R62), H157 (= H154)

3fdzA Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b with bound 2,3-diphosphoglyceric acid and 3- phosphoglyceric acid (see paper)
37% identity, 54% coverage: 1:107/197 of query aligns to 1:105/230 of 3fdzA

query
sites
3fdzA

M

M

P

Y

T

K

V

L

I

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

V

T

W

W

N
|
N

R

K

E

E

G

N

R

R

V

F

Q
x
T

G

G

H

W

G

V

D

D

S

V

P

D

L

L

T

T

P

E

K

Q

G

G

A

N

A

R

Q

E

A

A

R

R

A

Q

Y

A

G

G

R

-

K

-

L

-

R

-

Q

Q

M

L

L

L

G

K

D

E

A

A

G

G

G

Y

W

T

R

F

V

D

V

I

-

A

-

Y

S

T

S

S

P

V

L

L

G

K

R
|
R

C

A

A

I

Q

R

T

T

T

L

G

W

I

H

L

V

C

Q

E

D

V

Q

A

M

E

D

L

L

D

M

F

Y

R

V

S

P

I

V

T

V

F

H

D

S

D

W

R

R

L

L

R

N

E
|
E

V

R

H

H

T
x
Y

G

G

Q

A

W

L

S

S

G

G

L

L

P

N

K
|
K

A

A

E

E

L

T

A

A

R

K

H

Y

active site: H9 (= H9), R60 (= R62), E87 (= E89)
binding (2R)-2,3-diphosphoglyceric acid: R8 (= R8), H9 (= H9), N15 (= N15), T21 (≠ Q21), R60 (= R62), E87 (= E89), Y90 (≠ T92), K98 (= K100)

Sites not aligning to the query:

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

3gp5A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 3-phosphoglyceric acid and vanadate (see paper)
37% identity, 54% coverage: 1:107/197 of query aligns to 1:105/248 of 3gp5A

query
sites
3gp5A

M

M

P

Y

T

K

V

L

I

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

V

T

W

W

N
|
N

R

K

E

E

G

N

R

R

V

F

Q

T

G

G

H

W

G

V

D

D

S

V

P

D

L

L

T

T

P

E

K

Q

G

G

A

N

A

R

Q

E

A

A

R

R

A

Q

Y

A

G

G

R

-

K

-

L

-

R

-

Q

Q

M

L

L

L

G

K

D

E

A

A

G

G

G

Y

W

T

R

F

V

D

V

I

-

A

-

Y

S

T

S

S

P

V

L

L

G

K

R
|
R

C

A

A

I

Q

R

T

T

T

L

G

W

I

H

L

V

C

Q

E

D

V

Q

A

M

E

D

L

L

D

M

F

Y

R

V

S

P

I

V

T

V

F

H

D

S

D

W

R

R

L

L

R

N

E
|
E

V

R

H

H

T

Y

G

G

Q

A

W

L

S

S

G

G

L

L

P

N

K

K

A

A

E

E

L

T

A

A

R

K

H

Y

active site: H9 (= H9), R60 (= R62), E87 (= E89)
binding vanadate ion: R8 (= R8), H9 (= H9), N15 (= N15), R60 (= R62), E87 (= E89)

Sites not aligning to the query:

active site: 182
binding vanadate ion: 182, 183

3gp3A Crystal structure of phosphoglyceromutase from burkholderia pseudomallei with 2-phosphoserine (see paper)
37% identity, 54% coverage: 1:107/197 of query aligns to 1:105/229 of 3gp3A

query
sites
3gp3A

M

M

P

Y

T

K

V

L

I

V

L

L

V

I

R
|
R

H
|
H

G

G

E

E

T

S

V

T

W

W

N

N

R

K

E

E

G

N

R

R

V

F

Q
x
T

G

G

H

W

G

V

D

D

S

V

P

D

L

L

T

T

P

E

K

Q

G

G

A

N

A

R

Q

E

A

A

R

R

A

Q

Y

A

G

G

R

-

K

-

L

-

R

-

Q

Q

M

L

L

L

G

K

D

E

A

A

G

G

G

Y

W

T

R

F

V

D

V

I

-

A

-

Y

S

T

S

S

P

V

L

L

G

K

R
|
R

C

A

A

I

Q

R

T

T

T

L

G

W

I

H

L

V

C

Q

E

D

V

Q

A

M

E

D

L

L

D

M

F

Y

R

V

S

P

I

V

T

V

F

H

D

S

D

W

R

R

L

L

R

N

E
|
E

V

R

H

H

T
x
Y

G

G

Q

A

W

L

S

S

G

G

L

L

P

N

K
|
K

A

A

E

E

L

T

A

A

R

K

H

Y

active site: H9 (= H9), R60 (= R62), E87 (= E89)
binding phosphite ion: R8 (= R8), H9 (= H9), R60 (= R62), E87 (= E89)
binding phosphoserine: T21 (≠ Q21), E87 (= E89), Y90 (≠ T92), K98 (= K100)

Sites not aligning to the query:

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)
37% identity, 54% coverage: 1:107/197 of query aligns to 1:105/249 of Q3JWH7

query
sites
Q3JWH7

M

M

P

Y

T

K

V

L

I

V

L

L

V

I

R
|
R

H
|
H

G
|
G

E
|
E

T
x
S

V
x
T

W
|
W

N
|
N

R

K

E

E

G

N

R

R

V

F

Q
x
T

G
|
G

H

W

G

V

D

D

S

V

P

D

L

L

T

T

P

E

K

Q

G

G

A

N

A

R

Q

E

A

A

R

R

A

Q

Y

A

G

G

R

-

K

-

L

-

R

-

Q

Q

M

L

L

L

G

K

D

E

A

A

G

G

G

Y

W

T

R

F

V

D

V

I

-

A

-

Y

S

T

S

S

P

V

L

L

G

K

R
|
R

C

A

A

I

Q

R

T

T

T

L

G

W

I

H

L

V

C

Q

E

D

V

Q

A

M

E

D

L

L

D

M

F

Y

R

V

S

P

I

V

T

V

F

H

D

S

D

W

R

R

L

L

R

N

E
|
E

V
x
R

H
|
H

T
x
Y

G

G

Q

A

W

L

S

S

G

G

L

L

P

N

K
|
K

A

A

E

E

L

T

A

A

R

K

H

Y

8:15 (vs. 8:15, 75% identical) binding
H9 (= H9) active site, Tele-phosphohistidine intermediate
TG 21:22 (≠ QG 21:22) binding
R60 (= R62) binding
ERHY 87:90 (≠ EVHT 89:92) binding
K98 (= K100) binding

Sites not aligning to the query:

114:115 binding
183:184 binding

P36136 Sedoheptulose 1,7-bisphosphatase; EC 3.1.3.37 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 71% coverage: 2:141/197 of query aligns to 6:153/271 of P36136

query
sites
P36136

P

P

T

R

V

C

I

I

L

I

V

V

R
|
R

H
|
H

G

G

E

Q

T
|
T

V

E

W

W

N
x
S

R

K

E

S

G

G

R

Q

V
x
Y

Q
x
T

G

G

H

L

G

T

D

D

S

L

P

P

L

L

T

T

P

P

K

Y

G

G

A

E

A

G

Q

Q

A

M

R

L

A

R

Y

T

G

G

R

E

K

S

L

V

-

F

-

R

-

N

R

N

Q

Q

M

F

L

L

G

N

D

P

A

D

G

N

G

I

W

T

R

Y

V

I

V

F

S

T

S
|
S

P

P

L

R

G

L

R
|
R

C

A

A

R

Q

Q

T

T

T

V

G

D

I

L

L

V

C

L

E

K

V

P

A

L

E

S

L

D

D

E

F

Q

R

R

S

A

-

K

-

I

-

R

I

V

T

V

F

V

D

D

R

D

L

L

R

R

E
|
E

V
x
W

H
x
E

T
x
Y

G

G

Q

D

W

Y

S

E

G

G

L

M

P

L

K

T

A

R

E

E

L

I

A

I

A

E

R

-

H

-

P

-

G

-

M

L

L

R

E

K

G

S

E

R

G

G

L

L

D

D

H

K

-

E

-

R

-

P

-

W

-

N

-

I

W
|
W

V

R

F

D

R

G

C

C

P

E

G

N

G

G

E

E

S

T

H

T

H

Q

D

Q

V

I

A

G

S

L

R

R

L

L

A

S

H

R

W

A

L

I

A

A

R12 (= R8) binding ; 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 (≠ N15) mutation to A: Leads to reduced substrate affinity.
Y24 (≠ V20) mutation to A: Leads to low activity and reduced substrate affinity.
YT 24:25 (≠ VQ 20:21) binding
S65 (= S58) mutation to A: Leads to low activity and reduced substrate affinity.
R69 (= R62) binding ; mutation to A: Leads to reduced substrate affinity.
E99 (= E89) mutation to A: Impairs catalytic activity.
EWEY 99:102 (≠ EVHT 89:92) binding
Y102 (≠ T92) mutation to A: Impairs catalytic activity.
W131 (= W119) mutation to A: Leads to reduced substrate affinity.

Sites not aligning to the query:

176 H→A: Impairs catalytic activity.
178 H→A: Leads to low activity and reduced substrate affinity.
181 binding ; R→A: Leads to reduced substrate affinity.
244 binding

3lg2A A ykr043c/ fructose-1,6-bisphosphate product complex following ligand soaking (see paper)
29% identity, 71% coverage: 2:141/197 of query aligns to 4:151/269 of 3lg2A

query
sites
3lg2A

P

P

T

R

V

C

I

I

L

I

V

V

R
|
R

H
|
H

G

G

E

Q

T

T

V

E

W

W

N

S

R

K

E

S

G

G

R

Q

V

Y

Q
x
T

G

G

H

L

G

T

D

D

S

L

P

P

L

L

T

T

P

P

K

Y

G

G

A

E

A

G

Q

Q

A

M

R

L

A

R

Y

T

G

G

R

E

K

S

L

V

-

F

-

R

-

N

R

N

Q

Q

M

F

L

L

G

N

D

P

A

D

G

N

G

I

W

T

R

Y

V

I

V

F

S

T

S

S

P

P

L

R

G

L

R
|
R

C

A

A

R

Q

Q

T

T

T

V

G

D

I

L

L

V

C

L

E

K

V

P

A

L

E

S

L

D

D

E

F

Q

R

R

S

A

-

K

-

I

-

R

I

V

T

V

F

V

D

D

R

D

L

L

R

R

E
|
E

V

W

H

E

T

Y

G

G

Q

D

W

Y

S

E

G

G

L

M

P

L

K

T

A

R

E

E

L

I

A

I

A

E

R

-

H

-

P

-

G

-

M

L

L

R

E

K

G

S

E

R

G

G

L

L

D

D

H

K

-

E

-

R

-

P

-

W

-

N

-

I

W

W

V

R

F

D

R

G

C

C

P

E

G

N

G

G

E

E

S

T

H

T

H

Q

D

Q

V

I

A

G

S

L

R

R

L

L

A

S

H

R

W

A

L

I

A

A

active site: H11 (= H9), R67 (= R62), E97 (= E89)
binding phosphate ion: R10 (= R8), H11 (= H9), T23 (≠ Q21), R67 (= R62), E97 (= E89)

Sites not aligning to the query:

binding phosphate ion: 174, 176, 179, 242, 266

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
30% identity, 79% coverage: 1:155/197 of query aligns to 1:147/196 of 6m1xC

query
sites
6m1xC

M

M

P

T

T

K

V

L

I

I

L

L

V

I

R
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R

H
|
H

G

G

E

E

T

T

V

E

W

W

N

N

R

L

E

L

G

G

R

K

V

I

Q
|
Q

G

G

H

C

G

T

D

D

S

I

P

E

L

L

T

T

P

P

K

N

G

G

A

I

A

Q

Q

Q

A

A

R

N

A

E

Y

V

G

A

R

Q

K

Q

L

I

R

K

Q

-

M

-

L

-

G

-

D

-

A

-

G

G

G

N

W

F

R

D

V

I

-

Y

S

S

P

P

L

L

G

H

R
|
R

C

A

A

L

Q

I

T

T

T

A

G

Q

I

K

L

I

C

A

E

G

V

D

A

K

E

E

L

-

D

-

F

-

R

-

S

-

I

V

T

H

F

L

D

I

D

E

R

G

L

M

R

K

E
|
E

V

I

H

P

T

F

G

G

Q

T

W

W

S

E

G

G

L

H

P

T

K

F

A

E

E

E

L

L

A

N

A

G

-

D

-

I

R

N

H

Y

P

K

G

K

M

F

L

L

E

S

G

G

E

E

G

D

L

-

D

-

H

-

W

-

V

-

F

-

R

G

C

C

P

P

G

F

G

D

E

S

S

T

H

G

H

M

D

S

V

I

A

A

S

S

-

W

-

S

-

K

R

K

L

N

A

A

H

Q

W

L

L

L

A

L

D

D

L

L

A

C

P

K

G

Q

D

N

K

E

-

N

-

K

-

T

V

I

I

V

A

C

V

V

S

S

H
|
H

G
|
G

binding 3-phosphoglyceric acid: R8 (= R8), H9 (= H9), Q21 (= Q21), R57 (= R62), E79 (= E89), H146 (= H154), G147 (= G155)

P25114 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4; 6PF-2-K/Fru-2,6-P2ase 4; PFK/FBPase 4; 6PF-2-K/Fru-2,6-P2ase testis-type isozyme; EC 2.7.1.105; EC 3.1.3.46 from Rattus norvegicus (Rat) (see 2 papers)
26% identity, 83% coverage: 3:165/197 of query aligns to 251:402/469 of P25114

query
sites
P25114

T

S

V

I

I

Y

L

L

V

C

R

R

H
|
H

G

G

E

E

T

S

V

E

W

L

N

N

R

L

E

K

G

G

R

R

V

I

Q

-

G

-

H
x
G

G

G

D

D

S

P

P

G

L

L

T

S

P

P

K

R

G

G

A

-

Q

-

A

-

R

R

A

E

Y

F

G

S

R

K

K

H

L

L

R

A

Q

Q

M

F

L

I

G

S

D

D

A

Q

G

N

-

I

-

K

G

D

W

L

R

K

V

V

V

W

S

T

S

S

P

Q

L

M

G

K

R

R

C

T

A

I

Q

Q

T

T

T

A

G

E

I

A

L

L

C

-

E

-

V

-

A

-

E

-

L

-

D

-

F

-

R

-

S

S

I

V

T

P

F

Y

D

E

D

Q

-

W

-

K

R

V

L

L

R

N

E
|
E

V

I

H

D

T

A

G

G

Q

V

W

C

S

E

G

E

L

M

P

T

K
x
Y

A

E

E

E

L

I

A

Q

A

D

R

H

H

Y

P

P

G

L

M

E

L

F

E

A

G

L

E
x
R

G

D

L

Q

D

D

H
x
K

W

Y

V

R

F

Y

R

R

C

Y

P

P

G

K

G

G

E

E

S

S

H
x
Y

H

E

D

D

V

L

A

V

S

Q

R

R

L

L

A

E

H

P

W

V

L

I

A

M

D

E

L

L

A

E

P

R

G

Q

D

E

K

N

V

V

I

L

A

V

V

I

S

C

H

H

G
x
Q

I

A

A

V

G

M

R
|
R

V

C

L

L

R

L

G

A

L

Y

Y

F

H257 (= H9) active site, Tele-phosphohistidine intermediate
G269 (≠ H23) binding
E326 (= E89) active site, Proton donor/acceptor
Y337 (≠ K100) binding
R351 (≠ E114) binding
K355 (≠ H118) binding
Y366 (≠ H129) binding
Q392 (≠ G155) binding
R396 (= R159) binding

Sites not aligning to the query:

46:54 binding
79 binding
131 binding
137 binding
168:173 binding
198 binding
428 binding

3oi7A Structure of the structure of the h13a mutant of ykr043c in complex with sedoheptulose-1,7-bisphosphate (see paper)
28% identity, 71% coverage: 2:141/197 of query aligns to 3:150/260 of 3oi7A

query
sites
3oi7A

P

P

T

R

V

C

I

I

L

I

V

V

R
|
R

H
x
A

G

G

E

Q

T
|
T

V

E

W

W

N

S

R

K

E

S

G

G

R

Q

V
x
Y

Q
x
T

G

G

H

L

G

T

D

D

S

L

P

P

L

L

T

T

P

P

K

Y

G

G

A

E

A

G

Q

Q

A

M

R

L

A

R

Y

T

G

G

R

E

K

S

L

V

-

F

-

R

-

N

R

N

Q

Q

M

F

L

L

G

N

D

P

A

D

G

N

G

I

W

T

R

Y

V

I

V

F

S

T

S

S

P

P

L

R

G

L

R
|
R

C

A

A

R

Q

Q

T

T

T

V

G

D

I

L

L

V

C

L

E

K

V

P

A

L

E

S

L

D

D

E

F

Q

R

R

S

A

-

K

-

I

-

R

I

V

T

V

F

V

D

D

R

D

L

L

R

R

E
|
E

V

W

H

E

T
x
Y

G

G

Q

D

W

Y

S

E

G

G

L

M

P

L

K

T

A

R

E

E

L

I

A

I

A

E

R

-

H

-

P

-

G

-

M

L

L

R

E

K

G

S

E

R

G

G

L

L

D

D

H

K

-

E

-

R

-

P

-

W

-

N

-

I

W

W

V

R

F

D

R

G

C

C

P

E

G

N

G

G

E

E

S

T

H

T

H

Q

D

Q

V

I

A

G

S

L

R

R

L

L

A

S

H

R

W

A

L

I

A

A

active site: A10 (≠ H9), R66 (= R62), E96 (= E89)
binding magnesium ion: T13 (= T12), T22 (≠ Q21), R66 (= R62)
binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: R9 (= R8), Y21 (≠ V20), T22 (≠ Q21), R66 (= R62), E96 (= E89), Y99 (≠ T92)

Sites not aligning to the query:

binding 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose: 173, 175, 178

Query Sequence

>WP_011386726.1 NCBI__GCF_000009985.1:WP_011386726.1
MPTVILVRHGETVWNREGRVQGHGDSPLTPKGAAQARAYGRKLRQMLGDAGGWRVVSSPL
GRCAQTTGILCEVAELDFRSITFDDRLREVHTGQWSGLPKAELAARHPGMLEGEGLDHWV
FRCPGGESHHDVASRLAHWLADLAPGDKVIAVSHGIAGRVLRGLYSRLDPDLAMRGDSPQ
DVLFLMSKGCIERIGSE

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