Comparing WP_012471292.1 NCBI__GCF_000020385.1:WP_012471292.1 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)
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
38% identity, 72% coverage: 57:470/574 of query aligns to 25:445/515 of 1vrgA
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
35% identity, 88% coverage: 46:548/574 of query aligns to 16:495/521 of 3ib9A
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
35% identity, 88% coverage: 46:548/574 of query aligns to 16:495/521 of 1xnyA
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
37% identity, 72% coverage: 57:470/574 of query aligns to 19:440/506 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)
37% identity, 72% coverage: 57:470/574 of query aligns to 23:444/510 of Q168G2
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
33% identity, 87% coverage: 57:557/574 of query aligns to 19:489/506 of 8pn7A
8xl5B Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
37% identity, 72% coverage: 57:467/574 of query aligns to 22:442/507 of 8xl5B
8xl4B Structure of human propionyl-coa carboxylase in complex with acetyl- coa (pcc-aco)
37% identity, 72% coverage: 57:467/574 of query aligns to 22:442/507 of 8xl4B
8xl3B Structure of human propionyl-coa carboxylase at apo-state (pcc-apo)
37% identity, 72% coverage: 57:467/574 of query aligns to 22:442/507 of 8xl3B
7ybuC Human propionyl-coenzyme a carboxylase (see paper)
37% identity, 72% coverage: 57:467/574 of query aligns to 22:442/507 of 7ybuC
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
35% identity, 78% coverage: 44:488/574 of query aligns to 8:461/511 of 5iniF
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
32% identity, 88% coverage: 61:567/574 of query aligns to 8:482/489 of 8sgxE
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, 82% coverage: 57:528/574 of query aligns to 27:501/510 of 1on3C
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
36% identity, 72% coverage: 57:471/574 of query aligns to 31:451/520 of 1on3E
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
30% identity, 68% coverage: 103:495/574 of query aligns to 35:409/441 of 4g2rB
8rthF Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
30% identity, 64% coverage: 89:458/574 of query aligns to 105:472/542 of 8rthF
Sites not aligning to the query:
8xl8B Structure of human 3-methylcrotonyl-coa carboxylase in complex with propionyl-coa (mcc-pco)
28% identity, 62% coverage: 104:458/574 of query aligns to 104:452/541 of 8xl8B
Sites not aligning to the query:
8xl6B Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
28% identity, 62% coverage: 104:458/574 of query aligns to 104:452/541 of 8xl6B
Sites not aligning to the query:
8k2vG 3-methylcrotonyl-coa carboxylase in mccd state with acetyl coa (see paper)
28% identity, 62% coverage: 104:458/574 of query aligns to 104:452/541 of 8k2vG
8j4zJ Human 3-methylcrotonyl-coa carboxylase in bccp-cts state with substrate (see paper)
28% identity, 62% coverage: 104:458/574 of query aligns to 104:452/541 of 8j4zJ
Sites not aligning to the query:
>WP_012471292.1 NCBI__GCF_000020385.1:WP_012471292.1
MSKKAIKPSLKNPFAPPETVEFTIPGEIPGKKGGYEEAMKEGHDLIQRPIKSVSIAQIEK
QHFKKRMTVWERIKVLTEKEPNVLFQNWGKNLDGASLVTGILNVNGRDVALYGHDFTVRA
GSIDATNGRKLALLFQMAGEKGIPVIGMNDSAGAFVPAGVGGLDGYAEAFTALRKISGVV
PSIMCMFGFNAGGGSYLPRQGSFVIQPNDTFFGLTGPGVVKSVLGEDVTPEDLGGPKVHG
ASGVADLTVEDEVGALRASLQLLSYVPDNNSVAPRFRQTSDPLDRKTWEINTLLKKAFNS
PTGFNTPFDVSIMIQQICDHGDYFEMQPDRAREAVTAFGRLGGNVVGFVANNSAVASGQI
SVDSAYKIARFNRFCNIYNIPLIFMEDTTGFLPGREQESRGIVQAGRAMLDSIVDIRTPR
ILLIIRNAYGGAYASYNNYPTGADLVLALPTTRLAVMGPAGKEFVYKDELRKLRGAVKDK
VKSGVQERVAAGMDAGQATKDAEKDVADWLRIEEAALNLRYEKELMNPKEGLALGSISSL
VMPTDLRKVLGENMNFLLRHYKPGPMQAIQREFH
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