SitesBLAST

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)
31% identity, 96% coverage: 5:207/212 of query aligns to 3:209/552 of P33734

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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)
31% identity, 96% coverage: 5:207/212 of query aligns to 6:212/532 of 1ox5A

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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

7ac8B Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
27% identity, 95% coverage: 6:207/212 of query aligns to 5:196/202 of 7ac8B

query
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7ac8B

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binding glutamine: G54 (= G54), Q90 (= Q89), E98 (= E97), V142 (= V153), H143 (= H154), T144 (≠ S155), Y145 (= Y156)

Query Sequence

>WP_019557253.1 NCBI__GCF_000381085.1:WP_019557253.1
MDQKLVAVIDYGMGNLRSVAKAAEHVAPDNVHILVTNNPEEVACADAIIFPGQGAAKACM
QALHDTGMIHPIQKAAQEKPFLGICMGLQVLMSHSDENQGINCLNVIPGHVKHFELEENS
PLKIPHMGWNQIHQEQDHALWQNIPQDSRFYFVHSYYVQPENQAMITGTTTHGITFPAVL
SHKNVFAIQAHPEKSAEHGLQLFNNFLAWDGQ

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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