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)
34% identity, 98% coverage: 1:213/217 of query aligns to 1:209/552 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.

1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
34% identity, 98% coverage: 1:213/217 of query aligns to 4:212/538 of 1ox4B

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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)
29% identity, 97% coverage: 4:213/217 of query aligns to 5:196/202 of 7ac8B

query
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7ac8B

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binding glutamine: G54 (= G51), Q90 (= Q86), E98 (= E94), V142 (= V159), H143 (= H160), T144 (≠ S161), Y145 (= Y162)

Query Sequence

>RR42_RS18895 FitnessBrowser__Cup4G11:RR42_RS18895
MTTIAIVDYGMGNLRSVAQALRAAAPEADVQVVDQPEAIRAADRVVLPGQGAMPDCMGAL
GASGLQQAVIEAAASKPMLGVCVGEQMLFDFSKESRTQDGSTPCLGLLPGEVIRFELEGM
TQPDGSRYKVPQMGWNRVRQVRSHPLWAGIPDESWFYFVHSYYVHAQDPAHIAGETDYGV
LFTSAVARDNIFATQFHPEKSAAMGLRLYRNFVHWNP

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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