Comparing WP_017597037.1 NCBI__GCF_000341125.1:WP_017597037.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
79% identity, 97% coverage: 15:536/536 of query aligns to 1:521/521 of 1xnyA
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
78% identity, 97% coverage: 15:536/536 of query aligns to 1:521/521 of 3ib9A
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
61% identity, 97% coverage: 18:536/536 of query aligns to 1:511/511 of 5iniF
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
59% identity, 96% coverage: 23:536/536 of query aligns to 1:506/506 of 8pn7A
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
57% identity, 96% coverage: 23:536/536 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)
57% identity, 96% coverage: 23:536/536 of query aligns to 5:510/510 of Q168G2
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
58% identity, 96% coverage: 22:536/536 of query aligns to 6:515/515 of 1vrgA
7ybuP Human propionyl-coenzyme a carboxylase
55% identity, 95% coverage: 26:536/536 of query aligns to 7:507/507 of 7ybuP
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
51% identity, 97% coverage: 18:536/536 of query aligns to 8:520/520 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)
50% identity, 97% coverage: 18:536/536 of query aligns to 4:510/510 of 1on3C
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
53% identity, 92% coverage: 45:536/536 of query aligns to 8:489/489 of 8sgxE
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
44% identity, 81% coverage: 91:523/536 of query aligns to 28:440/441 of 4g2rB
6tzvA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
42% identity, 81% coverage: 91:523/536 of query aligns to 29:425/426 of 6tzvA
6prwA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
42% identity, 81% coverage: 91:523/536 of query aligns to 29:425/426 of 6prwA
6pk2A Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
42% identity, 81% coverage: 91:523/536 of query aligns to 29:425/426 of 6pk2A
6p7uA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p from mycobacterium tuberculosis
42% identity, 81% coverage: 91:523/536 of query aligns to 29:425/426 of 6p7uA
6tzvC Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
41% identity, 81% coverage: 91:523/536 of query aligns to 29:409/410 of 6tzvC
6prwC Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
41% identity, 81% coverage: 91:523/536 of query aligns to 29:409/410 of 6prwC
6pk2C Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
41% identity, 81% coverage: 91:523/536 of query aligns to 29:409/410 of 6pk2C
6p7uC Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p from mycobacterium tuberculosis
41% identity, 81% coverage: 91:523/536 of query aligns to 29:409/410 of 6p7uC
>WP_017597037.1 NCBI__GCF_000341125.1:WP_017597037.1
MATEAPEPLSAAEIDIHTTAGKLADLQRRRYEAVHAGSERAVEKQHAKGKMTARERIDAL
LDPGSFVEFDALARHRSTSFGLDRNRPYGDGVVTGHGTVDGRPVAVFSQDVTVFGGSLGE
VYGEKITKVLDHALTNGCPVVGINEGGGARIQEGVVSLGLYAEIFKRNTHASGVIPQISL
VMGAAAGGHVYSPALTDFVVMVDETSQMFITGPDVIKTVTGEDVSMEELGGARTHNTKSG
VAHYMGADERDAIEYVRTLLSHLPDNNLEEAPVLPPEEEPGDEPTDTDLALDAFIPDSAN
QPYDMKRVIEAVLDDGDFLEVHAQFATNIVVGFGRVDGRSVGVVANQPMSFAGCLDIDAS
EKAARFVRTCDAFNVPVLTFVDVPGFLPGTDQEWDGIIRRGAKLLYAYAEATVPLITVIT
RKAFGGAYDVMGSKHLGADVNLAWPTAQIAVMGAQGAVNILHRRTLAEADDVEAERTRLV
TEYEDTLLNPYSAAERGYVDGVIMPSETRDQVSKALKALRNKRKQLPPKKHGNIPL
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