SitesBLAST

Q0S7P9 Cholesterol ring-cleaving hydrolase IpdA subunit; (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA hydrolase alpha subunit; COCHEA-CoA hydrolase alpha subunit; EC 4.1.99.- from Rhodococcus jostii (strain RHA1) (see paper)
26% identity, 66% coverage: 97:286/286 of query aligns to 98:296/296 of Q0S7P9

query
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Q0S7P9

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E105 (≠ H104) mutation E->A,D: Loss of activity.

6co9A Crystal structure of rhodococcus jostii rha1 ipdab cochea-coa complex (see paper)
26% identity, 66% coverage: 97:286/286 of query aligns to 97:295/295 of 6co9A

query
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6co9A

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binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (5R,10R)-7-hydroxy-10-methyl-2-oxo-1-oxaspiro[4.5]dec-6-ene-6-carbothioate (non-preferred name): E104 (≠ H104)

Sites not aligning to the query:

binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (5R,10R)-7-hydroxy-10-methyl-2-oxo-1-oxaspiro[4.5]dec-6-ene-6-carbothioate (non-preferred name): 28, 84

6lp1C Crystal structure of acetate:succinate coa transferase (asct) from trypanosoma brucei. (see paper)
25% identity, 78% coverage: 1:222/286 of query aligns to 3:232/469 of 6lp1C

query
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6lp1C

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binding calcium ion: Q202 (≠ R192), D230 (≠ T220)

Query Sequence

>SM_b20587 FitnessBrowser__Smeli:SM_b20587
MARIMSLAEAVEENVRDGDTVAMEGFTHLIPYAAGHEVIRQGRKDLFLVRMTPDILYDQL
IGVGAARGMKFSWGGNPGVGSLHRFRDAVENQWPRPLEIEEHSHAAMANAYEAGAGNLPF
AAFRGYIGADLPKVNLNIRSVTCPFTGEVLAAVPAIRPDVTIIHAQRADRNGNVLIEGIV
GVQKEAVLAARRSIVTVEEIVDELSPPSPNSVVLPGWAVTAVAHVPGGAFPSYAHGYYPR
SNAFYIRWDEIARDRETFTAWIRENVLAAKPEDFARHAAKTAAKVA

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