SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Synpcc7942_1481 FitnessBrowser__SynE:Synpcc7942_1481 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 7 hits to proteins with known functional sites (download)

P33734 Imidazole glycerol phosphate synthase hisHF; IGP synthase; IGPS; ImGP synthase; EC 4.3.2.10; EC 3.5.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 94% coverage: 5:207/217 of query aligns to 2:211/552 of P33734

query
sites
P33734

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Sites not aligning to the query:

239 mutation R->A,H,K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity.
258 K→A: No activity. Uncoupling of glutaminase activity from the cyclase activity.; K→R: Small reduction of activity.
360 mutation K->A,R: Almost no effect on activity.

1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
35% identity, 94% coverage: 5:207/217 of query aligns to 5:214/532 of 1ox5A

query
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1ox5A

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Sites not aligning to the query:

active site: 248, 386
binding phosphoric acid mono-[5-({[5-carbamoyl-3-(5-phosphonooxy-5-deoxy-ribofuranosyl)- 3h-imidazol-4-ylamino]-methyl}-amino)-2,3,4-trihydroxy-pentyl] ester: 283, 285, 313, 346, 347, 384, 386, 424, 451, 456, 457, 482, 505, 506

1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
35% identity, 94% coverage: 5:207/217 of query aligns to 5:214/538 of 1ox4B

query
sites
1ox4B

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Sites not aligning to the query:

active site: 248, 392
binding pyrophosphate 2-: 463, 488, 511, 512

7ac8B Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
31% identity, 92% coverage: 6:205/217 of query aligns to 4:196/202 of 7ac8B

query
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7ac8B

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binding glutamine: G54 (= G52), Q90 (= Q88), E98 (= E96), V142 (= V150), H143 (= H151), T144 (= T152), Y145 (= Y153)

2nv2J Structure of the plp synthase complex pdx1/2 (yaad/e) from bacillus subtilis (see paper)
34% identity, 45% coverage: 15:111/217 of query aligns to 11:106/196 of 2nv2J

query
sites
2nv2J

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binding glutamine: G46 (= G50), G47 (≠ A53), S49 (≠ D55), C79 (= C84), A80 (≠ L85), I83 (≠ Q88), R106 (= R111)

Sites not aligning to the query:

binding glutamine: 134, 135

P37528 Pyridoxal 5'-phosphate synthase subunit PdxT; Pdx2; Pyridoxal 5'-phosphate synthase glutaminase subunit; EC 4.3.3.6; EC 3.5.1.2 from Bacillus subtilis (strain 168) (see 2 papers)
34% identity, 45% coverage: 15:111/217 of query aligns to 11:106/196 of P37528

query
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P37528

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E15 (≠ S19) mutation to A: Almost no effect on glutaminase activity.
GES 47:49 (≠ AFD 53:55) binding
E48 (≠ F54) mutation to A: No activity, disturbing interaction with PdxS.
R106 (= R111) binding ; mutation to A: No activity, disturbing interaction with PdxS.

Sites not aligning to the query:

10 Q→A: 3-fold reduction in glutaminase activity.; Q→E: Almost no activity.; Q→N: 10-fold reduction in glutaminase activity.
134:135 binding
135 R→A: No activity, disturbing interaction with PdxS.
170 H→N: No activity.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
34% identity, 60% coverage: 75:205/217 of query aligns to 69:181/475 of 2ywcA

query
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2ywcA

T

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D

-

G

R

R

L

A

W

Y

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

K

V

S

A

-

H

A

T

K

P

A

K

G

G

L

M

Q

Q

L

I

L

L

A

E

N

N

F

F

V

L

active site: C78 (= C84), Y79 (≠ L85), H164 (= H189), E166 (= E191)

Sites not aligning to the query:

active site: 51, 53, 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 467, 471, 472, 473

Query Sequence

>Synpcc7942_1481 FitnessBrowser__SynE:Synpcc7942_1481
MASTPQIAVVDYDMGNLHSACKGLEAAGANPIVTADPATILAADGVLLPGVGAFDPAMDH
LRDRQLIEPLHQAATSGKPFLGICLGLQLLFEASEEGQSAGLGILPGRVQRFRSEPGLVI
PHMGWNQLQLQQPDCPLWQNLGADPWFYFVHTYYVVPSEPTLTAATVQHGSQPVTAAIAR
DRLWAVQFHPEKSAKAGLQLLANFVTQVAAAQLQTVA

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