Comparing WP_011952998.1 NCBI__GCF_000016765.1:WP_011952998.1 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)
3u9sF Crystal structure of p. Aeruginosa 3-methylcrotonyl-coa carboxylase (mcc) 750 kd holoenzyme, coa complex (see paper)
67% identity, 100% coverage: 1:533/533 of query aligns to 3:537/537 of 3u9sF
8xl8B Structure of human 3-methylcrotonyl-coa carboxylase in complex with propionyl-coa (mcc-pco)
64% identity, 99% coverage: 4:533/533 of query aligns to 9:541/541 of 8xl8B
8xl6B Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
64% identity, 99% coverage: 4:533/533 of query aligns to 9:541/541 of 8xl6B
8k2vG 3-methylcrotonyl-coa carboxylase in mccd state with acetyl coa (see paper)
64% identity, 99% coverage: 4:533/533 of query aligns to 9:541/541 of 8k2vG
8j4zJ Human 3-methylcrotonyl-coa carboxylase in bccp-cts state with substrate (see paper)
64% identity, 99% coverage: 4:533/533 of query aligns to 9:541/541 of 8j4zJ
8jxmC Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state with mcoa (see paper)
61% identity, 99% coverage: 4:533/533 of query aligns to 9:520/520 of 8jxmC
8rthF Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
62% identity, 96% coverage: 8:521/533 of query aligns to 26:542/542 of 8rthF
8f3dA 3-methylcrotonyl-coa carboxylase in filament, beta-subunit centered (see paper)
57% identity, 96% coverage: 8:521/533 of query aligns to 23:566/566 of 8f3dA
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
35% identity, 89% coverage: 39:514/533 of query aligns to 21:495/515 of 1vrgA
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
35% identity, 91% coverage: 25:507/533 of query aligns to 9:494/521 of 3ib9A
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)
32% identity, 94% coverage: 23:522/533 of query aligns to 2:498/510 of Q168G2
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
33% identity, 93% coverage: 27:522/533 of query aligns to 2:494/506 of 3n6rB
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
35% identity, 91% coverage: 25:507/533 of query aligns to 9:494/521 of 1xnyA
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
34% identity, 93% coverage: 21:514/533 of query aligns to 1:500/520 of 1on3E
1on3C Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
34% identity, 89% coverage: 39:514/533 of query aligns to 22:490/510 of 1on3C
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
34% identity, 92% coverage: 27:514/533 of query aligns to 2:486/506 of 8pn7A
8xl5B Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
33% identity, 91% coverage: 24:507/533 of query aligns to 2:480/507 of 8xl5B
8xl4B Structure of human propionyl-coa carboxylase in complex with acetyl- coa (pcc-aco)
33% identity, 91% coverage: 24:507/533 of query aligns to 2:480/507 of 8xl4B
8xl3B Structure of human propionyl-coa carboxylase at apo-state (pcc-apo)
33% identity, 91% coverage: 24:507/533 of query aligns to 2:480/507 of 8xl3B
7ybuC Human propionyl-coenzyme a carboxylase (see paper)
33% identity, 91% coverage: 24:507/533 of query aligns to 2:480/507 of 7ybuC
>WP_011952998.1 NCBI__GCF_000016765.1:WP_011952998.1
MTRLSTLADPASPDFAANAAHNRALADELRARVATAALGGSEAHRERHVARGKLLPRDRV
HRLLDPGSPFLEIGQLAANGMYDKEGGPPGAGVIAGIGSVRGRHCMIVANDPTVKGGAYF
PMTVKKHLRAQEIARENRLPCIYLVDSGGANLPHQAEVFPDRDHFGRIFFNQAQMSAEGI
PQIACVMGSCTAGGAYVPAMSDETVIVRQQGTIFLAGPPLVKAATGEVITAEDLGGGDLH
ARKSGVVDHLAENDEHALLIVRDIVATLQPPSPAPVNRADPKAPLFDPAELYGIVPQDVR
APYDVHEVIARIVDGSELHEFKPLYGTTLVCGFAHIWGQPVAILANNGVLFSESALKGAH
FIELACQRRVPLLFLQNISGFMVGGKYEAEGIAKNGAKLVTAVATASVPKITVLIGGSFG
AGNYGMCGRAYQPRFLFTWPNARISVMGGEQAASVLATVHRDADTWTPEQAEAFKAPIRQ
KYEDEGNPYYATARMWDDGIIDPAQTRDVLGLALAATLNAPIPDRAQFGVFRM
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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