ID A0A1G3HU14_9RHOO Unreviewed; 669 AA.
AC A0A1G3HU14;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000313|EMBL:OHC72130.1};
GN ORFNames=A3H93_01960 {ECO:0000313|EMBL:OHC72130.1};
OS Rhodocyclales bacterium RIFCSPLOWO2_02_FULL_63_24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales.
OX NCBI_TaxID=1802018 {ECO:0000313|EMBL:OHC72130.1, ECO:0000313|Proteomes:UP000178519};
RN [1] {ECO:0000313|EMBL:OHC72130.1, ECO:0000313|Proteomes:UP000178519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHC72130.1}.
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DR EMBL; MHZX01000031; OHC72130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3HU14; -.
DR Proteomes; UP000178519; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR048429; MCC_alpha_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF21139; MCC_alpha_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 592..663
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 669 AA; 72110 MW; A444443AF13E944D CRC64;
MFTKILIANR GEIACRVIKT ARRMGIRSVA VYSEADAGAR HVRLADEAVC IGAPPPRESY
LVVDKIIGAA LATCAQAIHP GYGFLSENEE FAEACSANSI VFIGPPVSAI RAMGSKSEAK
KLMEKAGVPL TPGYHGDKQE PDFLRQQADG IGYPVLIKAA AGGGGKGMRA VHKSEEFLDA
LASCKREATS SFGDDHVLIE KYLQRPRHIE IQVFGDSHGN CVYLFERDCS VQRRHQKVLE
EAPAPNMPPE RRAAMGKAAV DAAQAVGYVG AGTVEFIANQ DGTFYFMEMN TRLQVEHPVT
EMITGLDLVE WQLKVGAGEA LPLRQEQLAI RGHALEARIY AEDPDKGFLP SVGRLIHLAP
PAETLNVRVD TGVEQDDEIS PHYDPMIAKL IVWDESRERA LARMLQALAD YRVVGVANNI
GFLSRLVACP AFAQADLDTG LIERERAFLF PESVAPPAEA WLVVALGELI RDQQYAAADA
SASSDPHSPW HARDGWRLNG AARREIKLRA GETEKVVSAR YAGDSFALEF EGQSTTAAGR
FTASGELRVD LGGRRINVTV VSANEKRHVF IDGVCFVFAA IDPLFHAGSG GGAEGGLTAP
MPGKVIALIV EVGAKVEKGA PLLILEAMKM EHTIAAPTAG TIKAFLYNVG EQVSDGAELV
EFEPGNKQS
//
