ID H1SHH0_9BURK Unreviewed; 333 AA.
AC H1SHH0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:EHP38014.1};
DE Flags: Fragment;
GN ORFNames=OR16_39494 {ECO:0000313|EMBL:EHP38014.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP38014.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP38014.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP38014.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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:EHP38014.1}.
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DR EMBL; AHJE01000153; EHP38014.1; -; Genomic_DNA.
DR AlphaFoldDB; H1SHH0; -.
DR PATRIC; fig|1127483.3.peg.7859; -.
DR Proteomes; UP000005808; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
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; PF00364; Biotin_lipoyl; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 1..113
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 256..329
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHP38014.1"
SQ SEQUENCE 333 AA; 35120 MW; CD93E01A28321381 CRC64;
KQFLPSTGTL RYLRTPAAVT FTLGQDGSGP AGVRIDSGVR EGDTISPYYD PMIAKLIVWG
RDRDEALARM AQALAEYHVV GLSTNVAFLR RLVTSQAFRI ADLDTGLIER NQAALFPPPA
PVGMEVIALA VAALLDAQAR ARRVDPADAH SPWQHAGAWR LNGGERRALR FSVGSPAGGL
VGSHIAEVTL ATAARGSTLF FADQAAPFRA QCAGDDIRVD LGTRRARGQV HAEGDTFHVF
SGHRHLALTW IDPLAHAAEG GKLTAPMPGK VIAVMVQAGS RVARGAPLLV MEAMKTEHTI
SAPADGVVGE VLYGVGEQVG EGAQLLSFEA GNG
//