Comparing WP_012043673.1 NCBI__GCF_000015165.1:WP_012043673.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
35% identity, 97% coverage: 7:508/519 of query aligns to 1:491/506 of 8pn7A
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
34% identity, 94% coverage: 7:493/519 of query aligns to 1:479/506 of 3n6rB
Q168G2 Propionyl-CoA carboxylase beta chain; EC 6.4.1.3 from Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) (see paper)
34% identity, 94% coverage: 7:493/519 of query aligns to 5:483/510 of Q168G2
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
33% identity, 97% coverage: 1:504/519 of query aligns to 1:499/515 of 1vrgA
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
33% identity, 98% coverage: 6:512/519 of query aligns to 8:513/521 of 1xnyA
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
33% identity, 98% coverage: 6:512/519 of query aligns to 8:513/521 of 3ib9A
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
32% identity, 95% coverage: 2:493/519 of query aligns to 8:493/520 of 1on3E
7ybuP Human propionyl-coenzyme a carboxylase
32% identity, 92% coverage: 21:497/519 of query aligns to 18:484/507 of 7ybuP
1on3C Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
31% identity, 95% coverage: 2:493/519 of query aligns to 4:483/510 of 1on3C
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
32% identity, 92% coverage: 29:503/519 of query aligns to 8:473/489 of 8sgxE
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
30% identity, 98% coverage: 2:508/519 of query aligns to 1:496/511 of 5iniF
3u9sF Crystal structure of p. Aeruginosa 3-methylcrotonyl-coa carboxylase (mcc) 750 kd holoenzyme, coa complex (see paper)
32% identity, 92% coverage: 18:493/519 of query aligns to 39:512/537 of 3u9sF
8k2vG 3-methylcrotonyl-coa carboxylase in mccd state with acetyl coa
28% identity, 92% coverage: 19:496/519 of query aligns to 42:519/541 of 8k2vG
8j4zJ Human 3-methylcrotonyl-coa carboxylase in bccp-cts state with substrate
28% identity, 92% coverage: 19:496/519 of query aligns to 42:519/541 of 8j4zJ
8f3dA 3-methylcrotonyl-coa carboxylase in filament, beta-subunit centered (see paper)
27% identity, 96% coverage: 5:501/519 of query aligns to 58:560/566 of 8f3dA
8rthF Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
28% identity, 91% coverage: 28:498/519 of query aligns to 68:533/542 of 8rthF
8jxmC Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state with mcoa
26% identity, 92% coverage: 19:496/519 of query aligns to 42:498/520 of 8jxmC
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
25% identity, 88% coverage: 42:498/519 of query aligns to 4:431/441 of 4g2rB
6tzvA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
28% identity, 43% coverage: 274:498/519 of query aligns to 187:416/426 of 6tzvA
Sites not aligning to the query:
6prwA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
28% identity, 43% coverage: 274:498/519 of query aligns to 187:416/426 of 6prwA
Sites not aligning to the query:
>WP_012043673.1 NCBI__GCF_000015165.1:WP_012043673.1
MSWQPELEELARREAFAREMGGPDKVKRQHDQGRLTVRERIDGVVDAGSFHEIGAVAGLG
EYDEQGELKHVTPANCVFGRARIDGRTVVVVGDDFTVRGGSADASIAAKPLMAEEMAHDF
RLPIIRIIEGSGGGGSVKTIETKGAANLPGGIGGNRWYRYTTENMSLVPVVALGLGSVAG
LGAARLAASHYSVMTKQSAMFVAGPPVVKRLGQDLGKMELGGADIQTRAGGVDHAVDTEA
EAFACARRFLSYLPSSVYELPPTLPCTDDPQRTDEQLISAVPRDRRRVYKMRPIIESVVD
SGSFFEVAQNYGRPIIIGLARLEGRAVMVLASDPYHYGGSWTADACQKVIRWVDFAETFH
LPIVYLMDCPGFMVGLEAEKAATIRHGVRAMAAVNQSTVPWCTVIVRNSFGVAGVVHQPA
DRFSIRYAWPSAYWGSLPLEGGIEAAYRAEIDAAPDPKAKLKEIEERLNKLRSPFRSAEK
FWVEEIIDPRKTRALLCEFARLAEPLRTVGPPTAMTTRP
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