SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS22635 FitnessBrowser__Pedo557:CA265_RS22635 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)

3kd3A Crystal structure of a phosphoserine phosphohydrolase-like protein from francisella tularensis subsp. Tularensis schu s4
31% identity, 48% coverage: 9:217/433 of query aligns to 5:211/216 of 3kd3A

query
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3kd3A

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active site: D7 (= D11), F8 (= F12), D9 (= D13), G103 (= G109), D173 (= D179)
binding magnesium ion: D7 (= D11), D9 (= D13), D169 (= D175)

6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
26% identity, 48% coverage: 11:218/433 of query aligns to 16:216/217 of 6q6jB

query
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6q6jB

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binding calcium ion: D16 (= D11), D18 (= D13), D175 (= D175)
binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D11), V17 (≠ F12), D18 (= D13), F54 (= F57), S105 (= S108), G106 (= G109), G107 (= G110), K154 (= K157), T178 (≠ S178)

6hyjB Psph human phosphoserine phosphatase (see paper)
26% identity, 48% coverage: 11:218/433 of query aligns to 20:220/223 of 6hyjB

query
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6hyjB

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binding calcium ion: D20 (= D11), D22 (= D13), D179 (= D175)
binding phosphoserine: F131 (≠ Y130), K168 (≠ E167)
binding serine: E29 (= E20), R202 (= R200)

1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
26% identity, 48% coverage: 11:218/433 of query aligns to 17:217/222 of 1l8oA

query
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1l8oA

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active site: D17 (= D11), V18 (≠ F12), D19 (= D13), G107 (= G109), K155 (= K157), D180 (= D179)
binding phosphate ion: D17 (= D11), D19 (= D13), S106 (= S108), K155 (= K157)
binding serine: G177 (= G176), T179 (≠ S178), R199 (= R200)

1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
26% identity, 48% coverage: 11:218/433 of query aligns to 17:217/222 of 1l8lA

query
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1l8lA

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active site: D17 (= D11), V18 (≠ F12), D19 (= D13), G107 (= G109), K155 (= K157), D180 (= D179)
binding d-2-amino-3-phosphono-propionic acid: D17 (= D11), D19 (= D13), G107 (= G109), K155 (= K157), D176 (= D175), G177 (= G176), T179 (≠ S178)

6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
26% identity, 48% coverage: 11:218/433 of query aligns to 16:216/221 of 6hyyA

query
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6hyyA

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A

E

E

E

S

G

G

K
|
K

V

G

K

K

L

V

L

I

Q

K

H

L

L

L

K

K

L

E

E

K

-

F

-

H

-

F

G

K

E

K

L

I

F

I

G

M

I

I

G

G

D
|
D

G

G

Y

A

S

T

D

D

F

M

Q

E

L

A

R

C

E

P

S

P

G

A

I

-

N

D

K

A

F

F

F

I

A

G

F

F

T

G

E

G

N

N

I

V

A

I

R

R

E

Q

S

Q

I

V

V

K

S

D

K

N

A

A

D

K

H

W

V

Y

T

I

P

T

S

D

F

F

D

V

E

E

F

L

L

L

binding magnesium ion: D16 (= D11), D18 (= D13), D175 (= D175)
binding serine: D16 (= D11), V17 (≠ F12), D18 (= D13), S105 (= S108), G106 (= G109), K154 (= K157)

P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
26% identity, 48% coverage: 11:218/433 of query aligns to 20:220/225 of P78330

query
sites
P78330

D
|
D

F
x
V

D
|
D

S
|
S

T

T

F

V

T

I

Q

R

V

E

E
|
E

A

G

L

I

D
|
D

E

E

L

L

A
|
A

R

K

I

I

S

C

L

-

K

-

N

-

H

-

P

-

D

-

K

-

E

-

A

G

I

V

F

E

Q

D

K

A

I

V

E

S

D

E

Y

M

T

T

N

R

F

R

A

A

M
|
M

E
x
G

G

G

K

A

L

V

S

P

F

F

S

K

E

A

S

A

L

L

A

T

Q

E

R
|
R

V

L

K

A

L

L

L

I

E

Q

A

P

N

S

E

R

D

E

H

Q

L

V

K

Q

Q

R

L

L

I

I

K

A

H

E

L

Q

K

P

K

H

V

L

S

T

T

P

S

G

F

I

S

R

R

E

N

L

A

V

E

S

F

R

F

L

K

Q

K

E

H

R

A

N

D

V

E

Q

V

V

L

F

I

L

V

I

S
|
S

G
|
G

F

F

K

R

E

S

F

I

I

V

T

E

P

H

V

V

V

A

S

S

Q

K

Y

L

H

N

I

I

K

P

K

A

E

T

N

N

I

V

Y

F

A

A

N
|
N

T

R

F

L

V

K

T

F

T

Y

G

F

D

N

G

G

K

E

I

Y

I

A

D

G

Y

F

D

D

H

E

A

T

N

Q

P

P

L

T

S

A

E

E

E

S

G

G

K
|
K

V

G

K

K

L

V

L

I

Q

K

H

L

L

L

K

K

L

E

E

K

-

F

-

H

-

F

G

K

E

K

L

I

F

I

G

M

I

I

G

G

D
|
D

G

G

Y

A

S
x
T

D

D

F

M

Q

E

L

A

R

C

E

P

S

P

G

A

I

-

N

D

K

A

F

F

F

I

A

G

F

F

T

G

E

G

N

N

I

V

A

I

R
|
R

E

Q

S

Q

I

V

V

K

S

D

K

N

A

A

D

K

H

W

V

Y

T

I

P

T

S

D

F

F

D

V

E

E

F

L

L

L

D20 (= D11) binding Mg(2+)
DVD 20:22 (≠ DFD 11:13) binding L-serine
D22 (= D13) binding Mg(2+)
S23 (= S14) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
E29 (= E20) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
D32 (= D23) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
A35 (= A26) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
M52 (= M51) binding O-phospho-L-serine; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
G53 (≠ E52) binding phosphate
R65 (= R64) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
SGG 109:111 (= SGG 108:110) binding L-serine; binding O-phospho-L-serine
N133 (= N132) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
K158 (= K157) binding L-serine; binding O-phospho-L-serine
D179 (= D175) binding Mg(2+)
T182 (≠ S178) binding O-phospho-L-serine; binding phosphate; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
R202 (= R200) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.

P0A9T0 D-3-phosphoglycerate dehydrogenase; PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 24% coverage: 332:433/433 of query aligns to 308:410/410 of P0A9T0

query
sites
P0A9T0

I

V

P

A

K

G

R

K

V

L

A

I

D

K

F

Y

M

S

N

D

T

N

G

G

A

S

T

T

Y

L

L

S

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

P

K

-

I

L

E

H

K

G

S

G

H

R

R

R

L

L

I

M

H

H

I

I

H

H

K

E

N

N

V

R

P

P

G

G

I

V

M

L

A

T

K

A

I

L

N

N

T

K

V

I

F

F

A

A

K

E

H

Q

D

G

I

V

N

N

I

I

V

A

S

A

Q

Q

F

Y

L

L

M

Q

T

T

N

S

P

A

E

Q

I

M

G

G

Y

Y

A

V

I

V

T

I

D

D

I

I

N

E

A

A

E

D

Y

E

D

D

-

V

-

A

K

E

Q

K

L

A

F

L

K

Q

S

A

L

M

K

K

K

A

I

I

E

P

H

G

T

T

I

I

K

R

F

A

R

R

V

L

L

L

Y

Y

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
161:162 binding NAD(+)
181 binding NAD(+)
238:240 binding NAD(+)
264 binding NAD(+)
292:295 binding NAD(+)

1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
35% identity, 24% coverage: 332:433/433 of query aligns to 304:406/406 of 1ybaA

query
sites
1ybaA

I

V

P

A

K

G

R

K

V

L

A

I

D

K

F

Y

M

S

N

D

T

N

G

G

A

S

T

T

Y

L

L

S

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

P

K

-

I

L

E

H

K

G

S

G

H

R

R

R

L

L

I

M

H

H

I

I

H

H

K

E

N

N

V

R

P

P

G

G

I

V

M

L

A

T

K

A

I

L

N

N

T

K

V

I

F

F

A

A

K

E

H

Q

D

G

I

V

N

N

I

I

V

A

S

A

Q

Q

F

Y

L

L

M

Q

T

T

N

S

P

A

E

Q

I

M

G

G

Y

Y

A

V

I

V

T

I

D

D

I

I

N

E

A

A

E

D

Y

E

D

D

-

V

-

A

K

E

Q

K

L

A

F

L

K

Q

S

A

L

M

K

K

K

A

I

I

E

P

H

G

T

T

I

I

K

R

F

A

R

R

V

L

L

L

Y

Y

Sites not aligning to the query:

active site: 104, 236, 260, 265, 288
binding 2-oxoglutaric acid: 56, 57, 79, 80
binding nicotinamide-adenine-dinucleotide: 80, 102, 108, 154, 156, 157, 158, 176, 177, 178, 181, 206, 207, 208, 234, 235, 236, 288, 290
binding phosphate ion: 81, 83

1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
35% identity, 24% coverage: 332:433/433 of query aligns to 282:384/384 of 1sc6D

query
sites
1sc6D

I

V

P

A

K

G

R

K

V

L

A

I

D

K

F

Y

M

S

N

D

T

N

G

G

A

S

T

T

Y

L

L

S

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

P

K

-

I

L

E

H

K

G

S

G

H

R

R

R

L

L

I

M

H

H

I

I

H

H

K

E

N

N

V

R

P

P

G

G

I

V

M

L

A

T

K

A

I

L

N

N

T

K

V

I

F

F

A

A

K

E

H

Q

D

G

I

V

N

N

I

I

V

A

S

A

Q

Q

F

Y

L

L

M

Q

T

T

N

S

P

A

E

Q

I

M

G

G

Y

Y

A

V

I

V

T

I

D

D

I

I

N

E

A

A

E

D

Y

E

D

D

-

V

-

A

K

E

Q

K

L

A

F

L

K

Q

S

A

L

M

K

K

K

A

I

I

E

P

H

G

T

T

I

I

K

R

F

A

R

R

V

L

L

L

Y

Y

Sites not aligning to the query:

active site: 102, 228, 252
binding nicotinamide-adenine-dinucleotide: 99, 100, 102, 103, 146, 148, 149, 150, 168, 169, 170, 198, 199, 200, 204, 205, 227

1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
35% identity, 24% coverage: 332:433/433 of query aligns to 302:404/404 of 1psdA

query
sites
1psdA

I

V

P

A

K

G

R

K

V

L

A

I

D

K

F

Y

M

S

N

D

T

N

G

G

A

S

T

T

Y

L

L

S

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

P

K

-

I

L

E

H

K

G

S

G

H

R

R

R

L

L

I

M

H

H

I

I

H
|
H

K

E

N
|
N

V
x
R

P

P

G

G

I
x
V

M

L

A

T

K

A

I

L

N

N

T

K

V

I

F

F

A

A

K

E

H

Q

D

G

I

V

N

N

I

I

V

A

S

A

Q

Q

F

Y

L

L

M

Q

T

T

N

S

P

A

E

Q

I

M

G

G

Y

Y

A

V

I

V

T

I

D

D

I

I

N

E

A

A

E

D

Y

E

D

D

-

V

-

A

K

E

Q

K

L

A

F

L

K

Q

S

A

L

M

K

K

K

A

I

I

E

P

H

G

T

T

I

I

K

R

F

A

R

R

V

L

L

L

Y

Y

binding serine: H338 (= H369), N340 (= N371), R341 (≠ V372), V344 (≠ I375)

Sites not aligning to the query:

active site: 102, 234, 258, 263, 286
binding nicotinamide-adenine-dinucleotide: 102, 155, 156, 175, 176, 179, 204, 205, 206, 232, 233, 234, 286

2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
35% identity, 24% coverage: 332:433/433 of query aligns to 304:406/406 of 2p9eA

query
sites
2p9eA

I

V

P

A

K

G

R

K

V

L

A

I

D

K

F

Y

M

S

N

D

T

N

G

G

A

S

T

T

Y

L

L

S

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

P

K

-

I

L

E

H

K

V

S

G

H

R

R

R

L

L

I

M

H

H

I

I

H

H

K

E

N

N

V

R

P

P

G

G

I

V

M

L

A

T

K

A

I

L

N

N

T

K

V

I

F

F

A

A

K

E

H

Q

D

G

I

V

N

N

I

I

V

A

S

A

Q

Q

F

Y

L

L

M

Q

T

T

N

S

P

A

E

Q

I

M

G

G

Y

Y

A

V

I

V

T

I

D

D

I

I

N

E

A

A

E

D

Y

E

D

D

-

V

-

A

K

E

Q

K

L

A

F

L

K

Q

S

A

L

M

K

K

K

A

I

I

E

P

H

G

T

T

I

I

K

R

F

A

R

R

V

L

L

L

Y

Y

Sites not aligning to the query:

active site: 104, 236, 260, 265, 288
binding 1,4-dihydronicotinamide adenine dinucleotide: 156, 157, 158, 176, 177, 178, 206, 207, 208, 212, 234, 235, 236, 288, 290

Q58989 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see 3 papers)
28% identity, 45% coverage: 1:193/433 of query aligns to 1:186/211 of Q58989

query
sites
Q58989

M

M

P

E

K

K

Q

K

K

K

A

K

Y

L

Y

I

I

L

I

F

D
|
D

F

F

D
|
D

S

S

T

T

F

L

T

V

Q

N

V

N

E
|
E

A

T

L

I

D

D

E

E

L

I

A

A

R

R

I

-

S

-

L

-

K

-

N

-

H

-

P

-

D

-

K

E

E

A

A

G

I

V

F

E

Q

E

K

E

I

V

E

K

D

K

Y

I

T

T

N

K

F

E

A

A

M

M

E

E

G

G

K

K

L

L

S

N

F

F

S

E

E

Q

S

S

L

L

A

R

Q

K

R
|
R

V

V

K

S

L

L

E

-

A

-

N

K

E

D

D

L

H

P

L

I

K

E

Q

K

L

V

I

E

K

K

H

A

L

I

K

K

K

R

K

I

V

T

S

P

T

T

S

E

F

G

S

A

R

E

N

E

A

T

-

I

E

K

F

E

F

L

K

K

K

N

H

R

A

G

D

Y

E

V

V

V

L

A

I

V

V

V

S
|
S

G
|
G

G

G

F

F

K

D

E

I

F

A

I

V

T

N

P

K

V

I

V

K

S

E

Q

K

Y

L

H

G

I

L

K

-

E

D

N

Y

I

A

Y

F

A

A

N

N

T

R

F

L

V

I

T

V

T

K

G

-

D

D

G

G

K

K

I

L

I

T

D

G

Y

-

D

D

H

V

A

E

N

G

P

E

L

V

S

L

E

K

E

E

G

N

G

A

K
|
K

V

G

K

E

L

I

L

L

Q

E

H

K

L

I

-

A

K

K

L

I

E

E

G

G

-

I

-

N

-

L

-

E

E

D

L

T

F

V

G

A

I

V

G

G

D
|
D

G

G

Y

A

S
x
N

D

D

F

I

Q

S

L

M

-

F

R

K

E

K

S

A

G

G

I

L

I

K

N

I

K

A

F

F

F

C

A

A

D11 (= D11) active site, Nucleophile; binding Mg(2+); mutation to N: Loss of activity.
D13 (= D13) active site, Proton donor; binding Mg(2+)
E20 (= E20) binding substrate
R56 (= R64) binding substrate
SG 99:100 (= SG 108:109) binding substrate
K144 (= K157) binding substrate
D167 (= D175) binding Mg(2+)
N170 (≠ S178) binding substrate

1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
28% identity, 44% coverage: 3:193/433 of query aligns to 2:185/210 of 1f5sA

query
sites
1f5sA

K

K

Q

K

K

K

A

K

Y

L

Y

I

I

L

I

F

D
|
D

F
|
F

D
|
D

S

S

T

T

F

L

T

V

Q

N

V

N

E

E

A

T

L

I

D

D

E

E

L

I

A

A

R

R

I

-

S

-

L

-

K

-

N

-

H

-

P

-

D

-

K

E

E

A

A

G

I

V

F

E

Q

E

K

E

I

V

E

K

D

K

Y

I

T

T

N

K

F

E

A

A

M

M

E

E

G

G

K

K

L

L

S

N

F

F

S

E

E

Q

S

S

L

L

A

R

Q

K

R

R

V

V

K

S

L

L

E

-

A

-

N

K

E

D

D

L

H

P

L

I

K

E

Q

K

L

V

I

E

K

K

H

A

L

I

K

K

K

R

K

I

V

T

S

P

T

T

S

E

F

G

S

A

R

E

N

E

A

T

-

I

E

K

F

E

F

L

K

K

K

N

H

R

A

G

D

Y

E

V

V

V

L

A

I

V

V

V

S
|
S

G
|
G

G

G

F

F

K

D

E

I

F

A

I

V

T

N

P

K

V

I

V

K

S

E

Q

K

Y

L

H

G

I

L

K

-

E

D

N

Y

I

A

Y

F

A

A

N

N

T

R

F

L

V

I

T

V

T

K

G

-

D

D

G

G

K

K

I

L

I

T

D

G

Y

-

D

D

H

V

A

E

N

G

P

E

L

V

S

L

E

K

E

E

G

N

G

A

K
|
K

V

G

K

E

L

I

L

L

Q

E

H

K

L

I

-

A

K

K

L

I

E

E

G

G

-

I

-

N

-

L

-

E

E

D

L

T

F

V

G

A

I

V

G

G

D
|
D

G

G

Y

A

S

N

D
|
D

F

I

Q

S

L

M

-

F

R

K

E

K

S

A

G

G

I

L

I

K

N

I

K

A

F

F

F

C

A

A

active site: D10 (= D11), F11 (= F12), D12 (= D13), G99 (= G109), K143 (= K157), D170 (= D179)
binding magnesium ion: D10 (= D11), D12 (= D13), D166 (= D175)
binding phosphate ion: D10 (= D11), F11 (= F12), D12 (= D13), S98 (= S108), G99 (= G109), K143 (= K157)

1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
28% identity, 44% coverage: 3:193/433 of query aligns to 1:184/209 of 1l7nA

query
sites
1l7nA

K

K

Q

K

K

K

A

K

Y

L

Y

I

I

L

I

F

D
|
D

F
|
F

D
|
D

S

S

T

T

F

L

T

V

Q

N

V

N

E

E

A

T

L

I

D

D

E

E

L

I

A

A

R

R

I

-

S

-

L

-

K

-

N

-

H

-

P

-

D

-

K

E

E

A

A

G

I

V

F

E

Q

E

K

E

I

V

E

K

D

K

Y

I

T

T

N

K

F

E

A

A

M

M

E

E

G

G

K

K

L

L

S

N

F

F

S

E

E

Q

S

S

L

L

A

R

Q

K

R

R

V

V

K

S

L

L

E

K

A

-

N

-

E

D

D

L

H

P

L

I

K

E

Q

K

L

V

I

E

K

K

H

A

L

I

K

K

K

R

K

I

V

T

S

P

T

T

S

E

F

G

S

A

R

E

N

E

A

T

-

I

E

K

F

E

F

L

K

K

K

N

H

R

A

G

D

Y

E

V

V

V

L

A

I

V

V

V

S
|
S

G
|
G

G

G

F

F

K

D

E

I

F

A

I

V

T

N

P

K

V

I

V

K

S

E

Q

K

Y

L

H

G

I

L

K

-

E

D

N

Y

I

A

Y

F

A

A

N

N

T

R

F

L

V

I

T

V

T

K

G

-

D

D

G

G

K

K

I

L

I

T

D

G

Y

-

D

D

H

V

A

E

N

G

P

E

L

V

S

L

E

K

E

E

G

N

G

A

K
|
K

V

G

K

E

L

I

L

L

Q

E

H

K

L

I

-

A

K

K

L

I

E

E

G

G

-

I

-

N

-

L

-

E

E

D

L

T

F

V

G

A

I

V

G

G

D
|
D

G

G

Y

A

S
x
N

D
|
D

F

I

Q

S

L

M

-

F

R

K

E

K

S

A

G

G

I

L

I

K

N

I

K

A

F

F

F

C

A

A

active site: D9 (= D11), F10 (= F12), D11 (= D13), G98 (= G109), K142 (= K157), D169 (= D179)
binding aluminum fluoride: D9 (= D11), F10 (= F12), D11 (= D13), S97 (= S108), K142 (= K157)
binding tetrafluoroaluminate ion: D9 (= D11), F10 (= F12), D11 (= D13), S97 (= S108), G98 (= G109), K142 (= K157), N168 (≠ S178)
binding magnesium ion: D9 (= D11), D11 (= D13), D165 (= D175)

6iuyA Structure of dsgpdh of dunaliella salina (see paper)
26% identity, 28% coverage: 97:218/433 of query aligns to 100:220/585 of 6iuyA

query
sites
6iuyA

F

L

K

K

K

A

H

R

A

G

D

V

E

E

V

V

L

F

I

L

V

I

S

S

G

G

F

F

K

R

E

E

F

M

I

A

T

L

P

P

V

I

V

A

S

S

Q

H

Y

L

H

K

I

I

K

P

K

A

E

K

N

N

I

V

Y

F

A

C

N

N

T

T

F

M

V

S

T

W

T

Q

G

L

D

D

G

-

K

-

I

-

D

-

Y

-

D

D

H

H

A

G

N

E

P

P

L

V

S

R

E

L

E

S

G

H

G

F

K

K

V

S

K

R

L

A

L

I

Q

E

H

R

L

I

K

R

L

R

E

K

-

Y

-

P

-

Y

G

N

E

N

L

I

F

I

G

M

I

V

G

G

D
|
D

G

G

Y

F

S

S

D

D

F

L

Q

E

L

A

R

M

E

Q

S

G

G

S

I

P

-

D

-

G

I

A

N

D

K

A

F

F

F

I

A

C

F

F

T

G

E

G

N

V

I

M

A

Q

R

R

E

P

S

A

I

V

V

A

S

S

K

Q

A

A

D

D

H

W

V

F

T

V

P

R

S

S

F

Y

D

D

E

E

F

L

L

M

binding magnesium ion: D175 (= D175)

Sites not aligning to the query:

binding magnesium ion: 20, 22
binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532

1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
27% identity, 44% coverage: 4:193/433 of query aligns to 1:183/208 of 1l7pA

query
sites
1l7pA

Q

K

K

K

A

K

Y

L

Y

I

I

L

I

F

D
x
N

F
|
F

D
|
D

S

S

T

T

F

L

T

V

Q

N

V

N

E
|
E

A

T

L

I

D

D

E

E

L

I

A

A

R

R

I

-

S

-

L

-

K

-

N

-

H

-

P

-

D

-

K

E

E

A

A

G

I

V

F

E

Q

E

K

E

I

V

E

K

D

K

Y

I

T

T

N

K

F

E

A

A

M
|
M

E

E

G

G

K

K

L

L

S

N

F
|
F

S

E

E

Q

S

S

L

L

A

R

Q

K

R
|
R

V

V

K

S

L

L

E

K

A

-

N

-

E

D

D

L

H

P

L

I

K

E

Q

K

L

V

I

E

K

K

H

A

L

I

K

K

K

R

K

I

V

T

S

P

T

T

S

E

F

G

S

A

R

E

N

E

A

T

-

I

E

K

F

E

F

L

K

K

K

N

H

R

A

G

D

Y

E

V

V

V

L

A

I

V

V

V

S
|
S

G
|
G

G

G

F

F

K

D

E

I

F

A

I

V

T

N

P

K

V

I

V

K

S

E

Q

K

Y

L

H

G

I

L

K

-

E

D

N

Y

I

A

Y

F

A

A

N

N

T

R

F

L

V

I

T

V

T

K

G

-

D

D

G

G

K

K

I

L

I

T

D

G

Y

-

D

D

H

V

A

E

N

G

P

E

L

V

S

L

E

K

E

E

G

N

G

A

K
|
K

V

G

K

E

L

I

L

L

Q

E

H

K

L

I

-

A

K

K

L

I

E

E

G

G

-

I

-

N

-

L

-

E

E

D

L

T

F

V

G

A

I

V

G

G

D

D

G

G

Y

A

S

N

D
|
D

F

I

Q

S

L

M

-

F

R

K

E

K

S

A

G

G

I

L

I

K

N

I

K

A

F

F

F

C

A

A

active site: N8 (≠ D11), F9 (= F12), D10 (= D13), G97 (= G109), K141 (= K157), D168 (= D179)
binding phosphoserine: N8 (≠ D11), F9 (= F12), D10 (= D13), E17 (= E20), M40 (= M51), F46 (= F57), R53 (= R64), S96 (= S108), G97 (= G109), K141 (= K157)

8q4sA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with ap4 and magnesium.
26% identity, 43% coverage: 3:187/433 of query aligns to 78:258/295 of 8q4sA

query
sites
8q4sA

K

R

Q

R

K

K

A

K

Y

I

Y

L

I

I

I

A

D
|
D

F
x
M

D
|
D

S

S

T

T

F

M

T

I

Q

G

V

Q

E
|
E

A

C

L

I

D

D

E

E

L

L

A

A

-

E

R

E

I

A

S

G

L

L

K

R

N

D

H

H

P

-

D

-

K

-

E

-

A

-

I

-

F

-

Q

-

K

-

I

V

E

A

D

A

Y

I

T

T

N

A

F

R

A

A

M
|
M

E

N

G

G

K

E

L

I

S

A

F
|
F

S

E

E

P

S

A

L

L

A

R

Q

E

R
|
R

V

V

K

A

L

L

E

K

A

G

N

L

E

P

D

L

H

S

L

V

K

I

Q

D

L

K

I

V

K

I

H

S

L

T

K

R

K

I

K

T

V

L

S

T

T

P

S

G

F

G

S

P

R

Q

N

L

A

V

E

R

F

T

F

M

K

R

K

K

H

H

A

G

D

A

E

Y

V

T

L

A

I

L

V

V

S
|
S

G
|
G

F

F

K

T

E

S

F

F

I

T

T

R

P

R

V

I

V

A

S

E

Q

M

Y

I

H

G

I

F

K

N

K

E

E

E

N

R

I

-

Y

-

A

A

N

N

T

R

F

L

V

I

T

D

T

-

G

-

D

D

G

G

K

T

I

R

I

L

D

T

Y

G

D

T

H

V

A

A

N

E

P

P

L

I

S

L

E

G

E

R

G

E

G

A

K

K

V

V

-

E

K

K

L

L

L

V

Q

E

H

I

L

A

K

E

L

R

E

V

G

G

-

L

-

T

-

P

-

E

E

D

L

A

F

I

G

A

I

V

G

G

D
|
D

G

G

Y

A

S

N

D

D

F

L

-

G

-

M

-

I

Q

Q

L

L

R

A

E

G

S

T

G

G

I

V

binding (2S)-2-amino-4-phosphonobutanoic acid: D86 (= D11), M87 (≠ F12), D88 (= D13), E95 (= E20), M118 (= M51), F124 (= F57), R131 (= R64), S175 (= S108), G176 (= G109), G177 (= G110)
binding magnesium ion: D86 (= D11), D88 (= D13), D243 (= D175)

P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 24% coverage: 332:433/433 of query aligns to 360:466/466 of P87228

query
sites
P87228

I

V

P

S

K

E

R

A

V

L

A

T

D

R

F

Y

M

I

N

N

T

E

G

G

A

N

T

S

Y

I

L

G

S

A

S

V

N

N

F

F

P

P

N

E

L

V

Q

S

L

L

P

R

K

S

I

L

E

T

K

E

S

A

-

D

-

R

-

N

-

A

H

A

R

R

L

V

I

L

H

F

I

V

H

H

K

R

N

N

V

V

P

P

G

G

I

V

M

L

A

R

K

Q

I

V

N

N

T

E

V

L

F

F

A

I

K

D

H

H

D

-

I

-

N

N

I

I

V

K

S

S

Q

Q

F

F

L

S

M

D

T

S

N

R

P

G

E

D

I

I

G

A

Y

Y

A

L

I

V

T

A

D

D

I

I

N

S

A

D

E

C

Y

T

D

P

-

G

-

S

-

L

K

E

Q

A

L

L

F

H

K

Q

S

K

L

L

K

E

K

S

I

L

E

P

H

C

T

K

I

I

K

N

F

T

R

R

V

L

L

L

Y

Y

Sites not aligning to the query:

87 modified: Phosphoserine
258 modified: Phosphoserine

O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
25% identity, 21% coverage: 237:325/433 of query aligns to 10:102/533 of O43175

query
sites
O43175

L

L

V

I

I

S

G

D

D

S

V

L

D

D

P

P

L

C

T

C

I

R

A

K

I

I

L

L

K

Q

N

D

D

G

G

G

L

L

S

Q

I

V

R

V

H

E

K

K

T

Q

S

N

F

L

E

S

D

K

K

E

Y

E

V

L

-

I

-

A

-

E

-

L

K

Q

D

D

V

C

G

E

I

G

I

L

L

I

L

V

A

R

D

S

G

A

E

T

K

K

I

V

N

T

K

A

E

D

Q

V

L

I

K

N

N

A

A

A

A

E

K

K

L

L

K

Q

T

V

I

V

G

G

Y

R

L

A

G

G

N
x
T

A

G

K

V

N

D

K

N

I

V

D

D

L

L

D

E

L

A

C

A

T

T

K

R

Q

K

G

G

I

I

V

L

V

V

F

M

D

N

D

T

P

P

K

N

N

G

N

N

T78 (≠ N301) binding NAD(+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
135 R → W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
155:156 binding NAD(+)
175 binding NAD(+)
207 binding NAD(+)
234:236 binding NAD(+)
260 binding NAD(+)
261 V → M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
283:286 binding NAD(+)
373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987

Query Sequence

>CA265_RS22635 FitnessBrowser__Pedo557:CA265_RS22635
MPKQKAYYIIDFDSTFTQVEALDELARISLKNHPDKEAIFQKIEDYTNFAMEGKLSFSES
LAQRVKLLEANEDHLKQLIKHLKKKVSTSFSRNAEFFKKHADEVLIVSGGFKEFITPVVS
QYHIKKENIYANTFVTTGDGKIIDYDHANPLSEEGGKVKLLQHLKLEGELFGIGDGYSDF
QLRESGIINKFFAFTENIARESIVSKADHVTPSFDEFLYVNDLPRAISYPKNRILCLVIG
DVDPLTIAILKNDGLSIRHKTSFEDKYVKDVGIILLADGEKINKEQLKNAAKLKTIGYLG
NAKNKIDLDLCTKQGIVVFDDPKNNPRNIDFIPKRVADFMNTGATYLSSNFPNLQLPKIE
KSHRLIHIHKNVPGIMAKINTVFAKHDINIVSQFLMTNPEIGYAITDINAEYDKQLFKSL
KKIEHTIKFRVLY

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