Comparing 201058 FitnessBrowser__MR1:201058 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)
70% identity, 100% coverage: 1:535/535 of query aligns to 3:537/537 of 3u9sF
8f3dA 3-methylcrotonyl-coa carboxylase in filament, beta-subunit centered (see paper)
65% identity, 89% coverage: 48:524/535 of query aligns to 82:566/566 of 8f3dA
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
37% identity, 93% coverage: 22:517/535 of query aligns to 9:500/520 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)
37% identity, 93% coverage: 22:517/535 of query aligns to 5:490/510 of 1on3C
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
35% identity, 92% coverage: 26:517/535 of query aligns to 7:495/515 of 1vrgA
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)
34% identity, 94% coverage: 22:526/535 of query aligns to 1:499/510 of Q168G2
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
34% identity, 93% coverage: 29:526/535 of query aligns to 4:495/506 of 3n6rB
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
32% identity, 91% coverage: 23:510/535 of query aligns to 6:494/521 of 3ib9A
1xnyA Biotin and propionyl-coa bound to acyl-coa carboxylase beta subunit from s. Coelicolor (pccb) (see paper)
32% identity, 91% coverage: 23:510/535 of query aligns to 6:494/521 of 1xnyA
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
34% identity, 94% coverage: 29:529/535 of query aligns to 4:498/506 of 8pn7A
7ybuP Human propionyl-coenzyme a carboxylase
33% identity, 88% coverage: 38:510/535 of query aligns to 16:480/507 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, 93% coverage: 26:522/535 of query aligns to 6:496/511 of 5iniF
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
32% identity, 88% coverage: 42:510/535 of query aligns to 1:462/489 of 8sgxE
3gf3A Glutaconyl-coa decarboxylase a subunit from clostridium symbiosum co- crystallized with glutaconyl-coa (see paper)
25% identity, 94% coverage: 21:524/535 of query aligns to 28:541/563 of 3gf3A
3gmaB Glutaconyl-coa decarboxylase a subunit from clostridium symbiosum co- crystallized with glutaryl-coa (see paper)
25% identity, 94% coverage: 21:524/535 of query aligns to 28:545/566 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: 65:520/535 of query aligns to 1:436/441 of 4g2rB
6tzvA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
28% identity, 85% coverage: 64:520/535 of query aligns to 1:421/426 of 6tzvA
6prwA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
28% identity, 85% coverage: 64:520/535 of query aligns to 1:421/426 of 6prwA
6pk2A Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
28% identity, 85% coverage: 64:520/535 of query aligns to 1:421/426 of 6pk2A
6p7uA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p from mycobacterium tuberculosis
28% identity, 85% coverage: 64:520/535 of query aligns to 1:421/426 of 6p7uA
>201058 FitnessBrowser__MR1:201058
MTQLSSRINARSDEFKAKSDDMAALVADLKTKLAKIELGGGPVALERHLSRGKRLPRQRV
EKLLDAGSPFLELSQFAAFEVYDEEVPAAGIIAGIGRVSGVECMIIANDATVKGGTYYPI
TVKKHIRAQEIASRCHLPCIYLVDSGGANLPRQDEVFPDRDHFGRIFYNQAQMSAKGIPQ
IAVVMGLCTAGGAYVPAMADESIIVKDQGTIFLAGPPLVKAATGEEVSAEELGGADVHTK
ISGVADHLAQNDEHALELARRAVSRLNHQKEITLRLSPVKPPKFDISELYGIVGTDLKKP
FDVKEVIARIVDDSDFDEFKANYGATLVCGFARIHGYPVGIVANNGILFSESAQKGAHFI
ELCCQRKIPLLFLQNITGFMVGKKYEHEGIAKHGAKMVTAVSCANVPKFTVIIGGSYGAG
NYGMCGRAFEPTMMWMWPNARISVMGGEQAAGVLATVRRDGLARKGEEWSAEDEKAFKAP
IIAQYDKEGHPYHASARLWDDGIIDPAQTRDVVGLALSAALNAPIEDTRFGVFRM
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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