Comparing WP_010964257.1 NCBI__GCF_000008765.1:WP_010964257.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
7ac8B Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
35% identity, 99% coverage: 1:201/203 of query aligns to 1:197/202 of 7ac8B
1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
37% identity, 96% coverage: 5:199/203 of query aligns to 7:211/538 of 1ox4B
Sites not aligning to the query:
1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
37% identity, 96% coverage: 5:199/203 of query aligns to 7:211/532 of 1ox5A
Sites not aligning to the query:
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)
37% identity, 96% coverage: 5:199/203 of query aligns to 4:208/552 of P33734
Sites not aligning to the query:
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
27% identity, 62% coverage: 75:199/203 of query aligns to 97:206/693 of P49915
Sites not aligning to the query:
2vxoB Human gmp synthetase in complex with xmp (see paper)
27% identity, 62% coverage: 75:199/203 of query aligns to 75:181/658 of 2vxoB
Sites not aligning to the query:
>WP_010964257.1 NCBI__GCF_000008765.1:WP_010964257.1
MNKKIAIIDYDMGNLLSVKKAFDYIGANSFITSDSKEIEKSDAIILPGVGAFPDAMSSLK
ENGIDKTIINEAKNGKPFAGICLGMQLLFDESEEVTNTKGLGLIGGKIRKMKTEFKIPHM
GWNSLNIPRECNILKGVSKGSYVYFVHSYYAELADKNNLNAYCDYGTKLPAVVSYKNIFG
IQFHPEKSGEIGLTILKNFWELI
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory