Comparing WP_038216155.1 NCBI__GCF_000745855.1:WP_038216155.1 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)
72% identity, 100% coverage: 1:536/536 of query aligns to 3:537/537 of 3u9sF
8k2vG 3-methylcrotonyl-coa carboxylase in mccd state with acetyl coa
66% identity, 97% coverage: 15:536/536 of query aligns to 20:541/541 of 8k2vG
8j4zJ Human 3-methylcrotonyl-coa carboxylase in bccp-cts state with substrate
66% identity, 97% coverage: 15:536/536 of query aligns to 20:541/541 of 8j4zJ
8jxmC Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state with mcoa
62% identity, 98% coverage: 12:536/536 of query aligns to 17:520/520 of 8jxmC
8rthF Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
63% identity, 96% coverage: 14:525/536 of query aligns to 32:542/542 of 8rthF
8f3dA 3-methylcrotonyl-coa carboxylase in filament, beta-subunit centered (see paper)
61% identity, 96% coverage: 9:525/536 of query aligns to 24:566/566 of 8f3dA
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
35% identity, 95% coverage: 21:530/536 of query aligns to 2:507/515 of 1vrgA
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
35% identity, 96% coverage: 19:534/536 of query aligns to 6:518/520 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)
35% identity, 96% coverage: 19:534/536 of query aligns to 2:508/510 of 1on3C
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
34% identity, 94% coverage: 26:530/536 of query aligns to 1:498/506 of 8pn7A
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)
33% identity, 95% coverage: 22:529/536 of query aligns to 1:501/510 of Q168G2
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
33% identity, 94% coverage: 26:529/536 of query aligns to 1:497/506 of 3n6rB
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
33% identity, 94% coverage: 28:532/536 of query aligns to 11:517/521 of 3ib9A
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
33% identity, 94% coverage: 28:532/536 of query aligns to 11:517/521 of 1xnyA
7ybuP Human propionyl-coenzyme a carboxylase
34% identity, 92% coverage: 39:529/536 of query aligns to 17:498/507 of 7ybuP
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
31% identity, 90% coverage: 42:523/536 of query aligns to 23:496/511 of 5iniF
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
32% identity, 88% coverage: 43:511/536 of query aligns to 3:462/489 of 8sgxE
3gf3A Glutaconyl-coa decarboxylase a subunit from clostridium symbiosum co- crystallized with glutaconyl-coa (see paper)
26% identity, 97% coverage: 8:525/536 of query aligns to 19:541/563 of 3gf3A
3gmaB Glutaconyl-coa decarboxylase a subunit from clostridium symbiosum co- crystallized with glutaryl-coa (see paper)
26% identity, 97% coverage: 8:525/536 of query aligns to 19:545/566 of 3gmaB
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
30% identity, 85% coverage: 65:521/536 of query aligns to 1:436/441 of 4g2rB
>WP_038216155.1 NCBI__GCF_000745855.1:WP_038216155.1
MSKLVSKLNPRSEEFQANAQAMRALVDDLRTQFAQVEQGGGEAARAKHTARGKLLPRERV
SRLLDPGTPFLELSPLAAHGMYKGDAPGAGLIAGIGRVNGVDCMVVCNDATVKGGTYYPM
TVKKHLRAQEIAQQNRLPCIYLVDSGGANLPNQDEVFPDREHFGRIFYNQANMSAEGIAQ
IAVVMGSCTAGGAYVPAMSDESIIVKNQGTIFLGGPPLVKAATGEVVTAEDLGGGDVHTR
LSGVADHLAENDLHALALARSAVANLNATPAVRAEPVEAGHAPAFAPEELYGVIPTDTRK
PFDVREIIARIVDGSEFHEFKARFGATLVCGFAQIEGMPVGIVANNGILFSESAQKGAHF
IELCGQRKIPLVFLQNITGFMVGRKYENEGIARHGAKMVTAVATVNVPKFTVIIGGSFGA
GNYGMCGRAYSPRFLWMWPNARISVMGGEQAASVLATVKRDGIEAKGGAWSAEEEEAFKS
PIRQQYEHQGHPYYATARLWDDGVIDPADTRRVLALGLAAARNAPIPEPKFGVFRM
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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