ID A0A1I1VF18_9RHOB Unreviewed; 644 AA.
AC A0A1I1VF18;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:SFD81536.1};
GN ORFNames=SAMN04515678_103163 {ECO:0000313|EMBL:SFD81536.1};
OS Roseivivax sediminis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=936889 {ECO:0000313|EMBL:SFD81536.1, ECO:0000313|Proteomes:UP000325289};
RN [1] {ECO:0000313|EMBL:SFD81536.1, ECO:0000313|Proteomes:UP000325289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM D21,KCTC 23444,ACCC 10710
RC {ECO:0000313|Proteomes:UP000325289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOMS01000003; SFD81536.1; -; Genomic_DNA.
DR RefSeq; WP_149755072.1; NZ_FOMS01000003.1.
DR AlphaFoldDB; A0A1I1VF18; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000325289; 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 FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 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; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
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 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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000325289};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 556..641
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 644 AA; 67629 MW; B403552720AF01E4 CRC64;
MFAKILIANR GEIAVRVIRT ARAMGVGTVA VHSDVDDHAL HVAEADEAVA IGGAAPAESY
LRGERIIEAA LATGAQAIHP GYGFLSENAD FVEAVEAAGL VFIGPSAEAI RKMGLKDAAK
RLMAEAGVPV VPGYMGEDQA PGRLAREAAA IGYPVLIKAV AGGGGKGMRL VERAADFDDA
LAAARGEARG AFGNDAVLIE KLVATPRHIE VQVFGDGTRA VHLFERDCSL QRRHQKVIEE
TPAPGMTEEM RAAMGDSAVR AAEAIGYAGA GTVEFIVDGS DGLRPDRFWF MEMNTRLQVE
HPVTEMVTGV DLVDWQLRVA AGEPLPAAQE DLTLSGHAFE ARLYAEDVPA GFLPATGRLT
ELRFPEGARA DTGVRAGDAI SPHYDPMIAK LIVQGSTRAV ALRKLSRALS ETRVAGTVTN
LAFLGALAAH EGFARGAVDT GLIGRDLAAL TAMPEVPATV VAEAALAMAG FDRAEEPLAG
FTLWAPLERS LRLVRSGREV RCRLRMTGPG SAVIDVDGTE VAAARKAGVW RFEGRSAHGT
AISGGRVTVF AGHGSVFDIV DPLEQAEAAT GETTIEAPMP GRVVRVAVAP GQRVVAGDRL
VVLEAMKMEH ALTAWRDGEI AEVLVAEGDQ VAAGTALVRL EAET
//
