ID   ACCA3_MYCLE             Reviewed;         598 AA.
AC   P46392;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit {ECO:0000250|UniProtKB:P96890};
DE   Includes:
DE     RecName: Full=Biotin carboxylase {ECO:0000250|UniProtKB:P96890};
DE              Short=BC {ECO:0000250|UniProtKB:P96890};
DE              EC=6.3.4.14 {ECO:0000250|UniProtKB:P96890};
DE   Includes:
DE     RecName: Full=Biotin carboxyl carrier protein {ECO:0000250|UniProtKB:P96890};
DE              Short=BCCP {ECO:0000250|UniProtKB:P96890};
GN   Name=bccA; OrderedLocusNames=ML0726; ORFNames=B1308_C1_129;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7909542; DOI=10.1128/jb.176.9.2525-2531.1994;
RA   Norman E., de Smet K.A.L., Stoker N.G., Ratledge C., Wheeler P.R.,
RA   Dale J.W.;
RT   "Lipid synthesis in mycobacteria: characterization of the biotin carboxyl
RT   carrier protein genes from Mycobacterium leprae and M. tuberculosis.";
RL   J. Bacteriol. 176:2525-2531(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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. {ECO:0000250|UniProtKB:P96890}.
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:P96890};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC         Evidence={ECO:0000250|UniProtKB:P96890};
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: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P96890}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P96890}.
CC   -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC       of AccA3, which contains the biotin carboxylase (BC) and biotin
CC       carboxyl carrier protein (BCCP) domains, and an AccD protein, which
CC       contains the carboxyl transferase (CT) domain.
CC       {ECO:0000250|UniProtKB:P96890}.
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DR   EMBL; X63470; CAA45070.1; -; Genomic_DNA.
DR   EMBL; U00012; AAA85920.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30235.1; -; Genomic_DNA.
DR   PIR; A55579; A55579.
DR   PIR; G86999; G86999.
DR   RefSeq; NP_301567.1; NC_002677.1.
DR   RefSeq; WP_010907891.1; NC_002677.1.
DR   AlphaFoldDB; P46392; -.
DR   SMR; P46392; -.
DR   STRING; 272631.gene:17574550; -.
DR   KEGG; mle:ML0726; -.
DR   PATRIC; fig|272631.5.peg.1321; -.
DR   Leproma; ML0726; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_6_11; -.
DR   OrthoDB; 9760256at2; -.
DR   UniPathway; UPA00094; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000000806; 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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Ligase; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..598
FT                   /note="Biotin-dependent acyl-coenzyme A carboxylase alpha3
FT                   subunit"
FT                   /id="PRO_0000146797"
FT   DOMAIN          8..452
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT   DOMAIN          127..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          522..598
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          506..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         155..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         297
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   MOD_RES         564
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   CONFLICT        30
FT                   /note="D -> H (in Ref. 1; CAA45070)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   598 AA;  63863 MW;  5F2E291D7C54515D CRC64;
     MASHASSRIA KVLVANRGEI AVRVIRAARD ARLPSVAVYA EPDAEAPHVR LADEAFALGG
     HTSAESYLDF GKILDAAAKS GANAIHPGYG FLAENADFAQ AVIDAGLIWI GPSPQSIRDL
     GDKVTARHIA ARAQAPLVPG TPDPVKNADE VVAFAKEHGV PIAIKAAFGG GGKGMKVART
     LEEISELYES AVREATVAFG RGECFVERYL DKPRHVEAQV IADQHGNIVV AGTRDCSLQR
     RFQKLVEEAP APFLTDAQRK EIHESAKRIC KEAHYYGAGT VEYLVGQDGL ISFLEVNTRL
     QVEHPVTEET TGIDLVLQQF KIANGEKLEL IKDPIPCGHA IEFRINGEDA GRNFLPSPGP
     VSKFHPPTGP GVRLDSGVET GSVIGGQFDS MLAKLIVHGA TRQEALARAR RALDEFEVEG
     LATVIPFHRA VVSDPALIGD NNSFSVHTRW IETEWNNTIE PFIDNQPLDE EDTRPQQTVI
     VEVDGRRLEV SLPADLALAN PAGCNPAGVI RKKPKPRKRG GHTGAATSGD AVTAPMQGTV
     VKVAVAEGQT VMTGDLVVVL EAMKMENPVT AHKDGIITGL AVEAGTAITQ GTVLAEIK
//