Comparing WP_051185093.1 NCBI__GCF_000422285.1:WP_051185093.1 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
48% identity, 98% coverage: 14:528/528 of query aligns to 6:515/515 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)
46% identity, 99% coverage: 3:525/528 of query aligns to 1:517/520 of 1on3E
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
45% identity, 97% coverage: 15:528/528 of query aligns to 1:506/506 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)
45% identity, 97% coverage: 15:528/528 of query aligns to 5:510/510 of Q168G2
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
46% identity, 97% coverage: 15:528/528 of query aligns to 1:506/506 of 8pn7A
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
45% identity, 98% coverage: 14:528/528 of query aligns to 8:521/521 of 3ib9A
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
45% identity, 98% coverage: 14:528/528 of query aligns to 8:521/521 of 1xnyA
1on3C Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
45% identity, 98% coverage: 9:525/528 of query aligns to 3:507/510 of 1on3C
8xl5B Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
44% identity, 97% coverage: 16:528/528 of query aligns to 5:507/507 of 8xl5B
8xl4B Structure of human propionyl-coa carboxylase in complex with acetyl- coa (pcc-aco)
44% identity, 97% coverage: 16:528/528 of query aligns to 5:507/507 of 8xl4B
8xl3B Structure of human propionyl-coa carboxylase at apo-state (pcc-apo)
44% identity, 97% coverage: 16:528/528 of query aligns to 5:507/507 of 8xl3B
7ybuC Human propionyl-coenzyme a carboxylase (see paper)
44% identity, 97% coverage: 16:528/528 of query aligns to 5:507/507 of 7ybuC
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
40% identity, 98% coverage: 14:528/528 of query aligns to 5:511/511 of 5iniF
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
41% identity, 94% coverage: 31:528/528 of query aligns to 1:489/489 of 8sgxE
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
36% identity, 80% coverage: 83:504/528 of query aligns to 28:433/441 of 4g2rB
6tzvA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
35% identity, 80% coverage: 83:504/528 of query aligns to 29:418/426 of 6tzvA
6prwA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
35% identity, 80% coverage: 83:504/528 of query aligns to 29:418/426 of 6prwA
6pk2A Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
35% identity, 80% coverage: 83:504/528 of query aligns to 29:418/426 of 6pk2A
6p7uA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p from mycobacterium tuberculosis
35% identity, 80% coverage: 83:504/528 of query aligns to 29:418/426 of 6p7uA
6tzvC Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
34% identity, 80% coverage: 83:504/528 of query aligns to 29:402/410 of 6tzvC
>WP_051185093.1 NCBI__GCF_000422285.1:WP_051185093.1
MSNNDKTVSKNQKRMEDWWQRREKIMQMGGPKAVEQHRKKGLMTARERVDYFFDAGTFTE
IGTFVTHRATAFGMDNKEVPADGVVTGFGTVNGRYVVTASEDYTCMGGSFGEAHGRKFAY
AIDFAKDKGWPFVSMNDSGGLRMQEGMDALEAYGWLFRAQDQASGIIPQISLILGPCLGG
QAYHPVMQDFVIQVRGSGFLGIAGPAFVKAQTAEEISLEDLCGVKAHAVKSGQTHIVAEN
DKDCLDKCKQLLSFFPSNNKEAPPTVVSKDNPEREIEGLLDIIPDEPFRVFDMYKIIKKV
VDEDSFFETLSQYATNMITGFARFNGRTVGIVANQPCRLAGAIDINASDKAARFIRFCDL
FNIPLITFVDCPAYMIGSQQDWGGILRHGAKLLFAWSNATVPLISIIIRKSYAGAHYGML
DKSIGADFVYAWPTAIVTALDGKTVASVIFDKEIKAADDSEKIRAQKIAEYNEIYANPYH
AAARGFIDDVIDPKDTRKIINNSLNVLQNKWKTSYYSQPWRKYSNINM
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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