ID   ACCA1_MYCBO             Reviewed;         654 AA.
AC   P0A509; A0A1R3Y3I1; P46401; X2BLJ9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit {ECO:0000250|UniProtKB:P9WPQ3};
DE   Includes:
DE     RecName: Full=Biotin carboxylase {ECO:0000250|UniProtKB:P9WPQ3};
DE              Short=BC {ECO:0000250|UniProtKB:P9WPQ3};
DE              EC=6.3.4.14 {ECO:0000250|UniProtKB:P9WPQ3};
DE   Includes:
DE     RecName: Full=Biotin carboxyl carrier protein {ECO:0000250|UniProtKB:P9WPQ3};
DE              Short=BCCP {ECO:0000250|UniProtKB:P9WPQ3};
GN   Name=accA1; Synonyms=bccA; OrderedLocusNames=BQ2027_MB2529C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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:0000250|UniProtKB:P9WPQ3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
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:0000250|UniProtKB:P9WPQ3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC         Evidence={ECO:0000250|UniProtKB:P9WPQ3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00409};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01066};
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation.
CC       {ECO:0000250|UniProtKB:P9WPQ3}.
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:0000250|UniProtKB:P9WPQ3}.
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DR   EMBL; LT708304; SIU01145.1; -; Genomic_DNA.
DR   RefSeq; NP_856174.1; NC_002945.3.
DR   RefSeq; WP_003899356.1; NC_002945.4.
DR   AlphaFoldDB; P0A509; -.
DR   SMR; P0A509; -.
DR   GeneID; 45426495; -.
DR   PATRIC; fig|233413.5.peg.2784; -.
DR   UniPathway; UPA00363; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 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; 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; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..654
FT                   /note="Biotin-dependent 3-methylcrotonyl-coenzyme A
FT                   carboxylase alpha1 subunit"
FT                   /id="PRO_0000146796"
FT   DOMAIN          1..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   DOMAIN          120..319
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          578..653
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   BINDING         148..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         275
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   MOD_RES         620
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   654 AA;  70592 MW;  FAA0A1A46432CABF CRC64;
     MFDTVLVANR GEIAVRVIRT LRRLGIRSVA VYSDPDVDAR HVLEADAAVR LGPAPARESY
     LDIGKVLDAA ARTGAQAIHP GYGFLAENAD FAAACERARV VFLGPPARAI EVMGDKIAAK
     NAVAAFDVPV VPGVARAGLT DDALVTAAAE VGYPVLIKPS AGGGGKGMRL VQDPARLPEA
     LVSARREAMS SFGDDTLFLE RFVLRPRHIE VQVLADAHGN VVHLGERECS LQRRHQKVIE
     EAPSPLLDPQ TRERIGVAAC NTARCVDYVG AGTVEFIVSA QRPDEFFFME MNTRLQVEHP
     VTEAITGLDL VEWQLRVGAG EKLGFAQNDI ELRGHAIEAR VYAEDPAREF LPTGGRVLAV
     FEPAGPGVRV DSSLLGGTVV GSDYDPLLTK VIAHGADREE ALDRLDQALA RTAVLGVQTN
     VEFLRFLLAD ERVRVGDLDT AVLDERSADF TARPAPDDVL AAGGLYRQWA LARRAQGDLW
     AAPSGWRGGG HMAPVRTAMR TPLRSETVSV WGPPESAQVQ VGDGEIDCAS VQVTREQMSV
     TISGLRRDYR WAEADRHLWI ADERGTWHLR EAEEHKIHRA VGARPAEVVS PMPGSVIAVQ
     VESGSQISAG DVVVVVEAMK MEHSLEAPVS GRVQVLVSVG DQVKVEQVLA RIKD
//