Comparing RR42_RS29410 FitnessBrowser__Cup4G11:RR42_RS29410 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)
45% identity, 95% coverage: 1:514/540 of query aligns to 3:514/537 of 3u9sF
8f3dA 3-methylcrotonyl-coa carboxylase in filament, beta-subunit centered (see paper)
41% identity, 96% coverage: 7:523/540 of query aligns to 20:563/566 of 8f3dA
1vrgA Crystal structure of propionyl-coa carboxylase, beta subunit (tm0716) from thermotoga maritima at 2.30 a resolution
30% identity, 89% coverage: 45:523/540 of query aligns to 27:499/515 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)
28% identity, 94% coverage: 22:530/540 of query aligns to 1:501/510 of Q168G2
3n6rB Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
28% identity, 92% coverage: 33:530/540 of query aligns to 6:497/506 of 3n6rB
8pn7A Engineered glycolyl-coa carboxylase (g20r variant) with bound coa (see paper)
30% identity, 94% coverage: 26:531/540 of query aligns to 1:498/506 of 8pn7A
1on3E Transcarboxylase 12s crystal structure: hexamer assembly and substrate binding to a multienzyme core (with methylmalonyl-coenzyme a and methylmalonic acid bound) (see paper)
30% identity, 91% coverage: 33:521/540 of query aligns to 18:502/520 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)
30% identity, 91% coverage: 33:521/540 of query aligns to 14:492/510 of 1on3C
3ib9A Propionyl-coa carboxylase beta subunit, d422l (see paper)
30% identity, 91% coverage: 20:512/540 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)
30% identity, 91% coverage: 20:512/540 of query aligns to 6:494/521 of 1xnyA
7ybuP Human propionyl-coenzyme a carboxylase
27% identity, 94% coverage: 27:534/540 of query aligns to 5:496/507 of 7ybuP
5iniF Structural basis for acyl-coa carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics (see paper)
27% identity, 90% coverage: 37:523/540 of query aligns to 20:495/511 of 5iniF
8sgxE Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
27% identity, 87% coverage: 42:512/540 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)
28% identity, 81% coverage: 18:456/540 of query aligns to 25:480/563 of 3gf3A
3gmaB Glutaconyl-coa decarboxylase a subunit from clostridium symbiosum co- crystallized with glutaryl-coa (see paper)
28% identity, 81% coverage: 18:456/540 of query aligns to 25:484/566 of 3gmaB
4g2rB Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor haloxyfop from mycobacterium tuberculosis (see paper)
27% identity, 85% coverage: 64:520/540 of query aligns to 1:434/441 of 4g2rB
6tzvA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor phenyl-cyclodiaone from mycobacterium tuberculosis
26% identity, 85% coverage: 63:520/540 of query aligns to 1:419/426 of 6tzvA
6prwA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
26% identity, 85% coverage: 63:520/540 of query aligns to 1:419/426 of 6prwA
6pk2A Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p derivative from mycobacterium tuberculosis
26% identity, 85% coverage: 63:520/540 of query aligns to 1:419/426 of 6pk2A
6p7uA Crystal structure of the carboxyltransferase subunit of acc (accd6) in complex with inhibitor quizalofop-p from mycobacterium tuberculosis
26% identity, 85% coverage: 63:520/540 of query aligns to 1:419/426 of 6p7uA
>RR42_RS29410 FitnessBrowser__Cup4G11:RR42_RS29410
MANIESRLSAGSEAFQANRAGMLALLERIRAFEQRAASLSAASRERFEKRGQLLPRDRLA
LLLDPGAPFIELSSLAGLGLDNPDLDKSVPGGGLIAGIGFVSGLRCMISASDSGINAGAL
QPKGLDKQLRVQEIALENKLPYVQLVESAGANLMTYKVEDFVRGGNLFRNLALLSAAGLP
VVTVTHGSSTAGGAYQTGLSDYIIMVRGRSRAFLAGPPLLMAATGEVATEEELGGAVMHT
SVSGLGDYLAEDDRDALRIAREILGKIDWHRDQPAAAPRSYKPPRFDAEELLGVMPMDHK
RPVDMKEVIARIADDSDFLEFGENYGGATVCGHVKIEGWPLGIITNNGPIDPAGATKATH
FIQACCQSRTPILYLNNTTGFMVGRSHEEAGIIKHGSKMIQAVSNATVPQITIYCGASFG
AGNYGMCGRGFHPRFCFSWPNAKTAVMGGEQAARTMAIVTEAAMKRKGGQADADQLEALQ
KGIVERFDRQMSVFVTSAHVLDDGVIDPRNTRAVLANVLAICREGDARTPQAMQFGVARP
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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