SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012411289.1 NCBI__GCF_000020025.1:WP_012411289.1 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 6 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)
35% identity, 100% coverage: 1:210/211 of query aligns to 1:217/552 of P33734

query
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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, 100% coverage: 1:210/211 of query aligns to 4:220/532 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, 100% coverage: 1:210/211 of query aligns to 4:220/538 of 1ox4B

query
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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)
28% identity, 94% coverage: 4:202/211 of query aligns to 5:196/202 of 7ac8B

query
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7ac8B

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binding glutamine: G54 (= G49), Q90 (= Q85), E98 (= E93), V142 (= V147), H143 (= H148), T144 (≠ S149), Y145 (= Y150)

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)
32% identity, 42% coverage: 21:108/211 of query aligns to 20:106/196 of P37528

query
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P37528

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GES 47:49 (≠ GAF 49:51) binding L-glutamine
E48 (≠ A50) mutation to A: No activity, disturbing interaction with PdxS.
R106 (= R108) binding L-glutamine; 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.
15 E→A: Almost no effect on glutaminase activity.
134:135 binding L-glutamine
135 R→A: No activity, disturbing interaction with PdxS.
170 H→N: No activity.

2nv2J Structure of the plp synthase complex pdx1/2 (yaad/e) from bacillus subtilis (see paper)
32% identity, 42% coverage: 21:108/211 of query aligns to 20:106/196 of 2nv2J

query
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2nv2J

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binding glutamine: G46 (= G47), G47 (= G49), S49 (≠ F51), C79 (= C81), A80 (≠ L82), I83 (≠ Q85), R106 (= R108)

Sites not aligning to the query:

binding glutamine: 134, 135

Query Sequence

>WP_012411289.1 NCBI__GCF_000020025.1:WP_012411289.1
MPVIAVVDYEMGNLHSVCKGLEKAGATPNVTYSPKELEQADAIVLPGVGAFDPAVQHLRA
RGLEQPIKDAIASGKPFLGICLGLQILFESSAEGTQPGLGIIKGKVRRFRPEPDITIPHM
GWNQLEMTQAKSILWEHLPSDPWVYFVHSYYVDPIDPLIRAATITHGTQTVTAAIAHENL
MAVQFHPEKSSNIGLQILSNFVAQVREKIPA

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