ID   H6RIM2_BLASD            Unreviewed;       666 AA.
AC   H6RIM2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   02-SEP-2026, entry version 60.
DE   RecName: Full=Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit {ECO:0000256|ARBA:ARBA00074050};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   OrderedLocusNames=BLASA_1277 {ECO:0000313|EMBL:CCG02216.1};
OS   Blastococcus saxobsidens (strain DD2).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG02216.1, ECO:0000313|Proteomes:UP000007517};
RN   [1] {ECO:0000313|EMBL:CCG02216.1, ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|EMBL:CCG02216.1,
RC   ECO:0000313|Proteomes:UP000007517};
RX   PubMed=22535935; DOI=10.1128/JB.00320-12;
RA   Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA   Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA   Gury J., Pujic P., Normand P.;
RT   "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT   Bacterium.";
RL   J. Bacteriol. 194:2752-2753(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA   Genoscope.;
RT   "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of a biotin-dependent acyl-CoA carboxylase complex.
CC       This subunit catalyzes the ATP-dependent carboxylation of the biotin
CC       carried by the biotin carboxyl carrier (BCC) domain, resulting in the
CC       formation of carboxyl biotin. When associated with the beta1 subunit
CC       AccD1, is involved in branched amino-acid catabolism with
CC       methylcrotonyl coenzyme A as the substrate.
CC       {ECO:0000256|ARBA:ARBA00053351}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP =
CC         N(6)-carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H(+);
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00048501};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC         Evidence={ECO:0000256|ARBA:ARBA00048501};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation.
CC       {ECO:0000256|ARBA:ARBA00046317}.
CC   -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC       of AccA1, which contains the biotin carboxylase (BC) and biotin
CC       carboxyl carrier protein (BCCP) domains, and AccD1, which contains the
CC       carboxyl transferase (CT) domain. The AccA1/AccD1 complex forms a
CC       dodecamer. {ECO:0000256|ARBA:ARBA00065901}.
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DR   EMBL; FO117623; CCG02216.1; -; Genomic_DNA.
DR   RefSeq; WP_014375113.1; NC_016943.1.
DR   AlphaFoldDB; H6RIM2; -.
DR   STRING; 1146883.BLASA_1277; -.
DR   KEGG; bsd:BLASA_1277; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_11; -.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000007517; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.30.700.40; -; 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; 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; 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; PF21139; BT_MCC_alpha; 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; 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};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PROSITE-
KW   ProRule:PRU00969};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PROSITE-
KW   ProRule:PRU00969};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          579..657
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   666 AA;  69745 MW;  36A62CC73C3595A8 CRC64;
     MFDTVLVANR GEIAVRVIRT LREMGIRSVA VYSDADAGAL HTRLADVAVR LGPAPAAQSY
     LLVERVLAAA AETGAQAVHP GYGFLSENVE FARACESAGI VFIGPPVAAI EAMGDKIRAK
     QTVMAAGVPV VPGRSEPGMS DEEVAEAAVA AGFPVLLKPS AGGGGKGMRV VRSKDELPDA
     IAGARREARS SFGDDTLLVE RYVGNSRHIE VQVLGDTHGT VIHLGERECS LQRRHQKVIE
     EAPSPLLDTS MRASMGRAAV EAAKAVGYTG AGTVEFIVDA DRPRDFFFLE MNTRLQVEHP
     VTEAITGLDL VEQQIRVAAG ERLPIDQSDV SLDGHAIEAR LYAEDPARGF LPQAGTVLAL
     IEPAGPGIRV DSSLAVGSVV GTDYDPMLAK VIAWGPDRET ARARLVGALG RTAVLGVSTN
     AAFLRALLTD EDVVAGRLDT GLIERRGNDL TAADPVPESV YASAALALQL EAEPTGPVVD
     RFDVPDGWRL GEPAWTVRRL QAPGGEPVVI RLRGRAADAE LCIGDGAPVP ARAARYGDDL
     VVTVGDWTAR YAVVHVGGSV WLAADGRVTE LREQERLASS AAGAAAGDGV VTSPMPGTVT
     VVQASVGDEV EAGTPLLVVE AMKMEHVLTA PVAGTVAELG VTAGQTVALD ERLALVMPKA
     PDQQEL
//