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Database: UniProt
Entry: P9WPQ2
LinkDB: P9WPQ2
Original site: P9WPQ2 
ID   BCCA_MYCTO              Reviewed;         654 AA.
AC   P9WPQ2; L0T9T8; P0A508; P46401;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   13-FEB-2019, entry version 34.
DE   RecName: Full=Acetyl-/propionyl-coenzyme A carboxylase alpha chain;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
DE   Includes:
DE     RecName: Full=Biotin carboxyl carrier protein;
DE              Short=BCCP;
GN   Name=accA1; Synonyms=bccA; OrderedLocusNames=MT2576;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: This protein carries two functions: biotin carboxyl
CC       carrier protein and biotin carboxyltransferase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Multimer comprised of 2 different subunits, the larger
CC       one (63/64 kDa) has biotin carboxylase and biotin carrier
CC       functions, while the smaller subunit possesses carboxyltransferase
CC       and substrate binding activity. {ECO:0000250}.
DR   EMBL; AE000516; AAK46880.1; -; Genomic_DNA.
DR   PIR; B55579; B55579.
DR   RefSeq; WP_003899356.1; NZ_KK341227.1.
DR   ProteinModelPortal; P9WPQ2; -.
DR   EnsemblBacteria; AAK46880; AAK46880; MT2576.
DR   KEGG; mtc:MT2576; -.
DR   PATRIC; fig|83331.31.peg.2778; -.
DR   KO; K11263; -.
DR   BioCyc; MTBCDC1551:GT3Z-7021-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001020; 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:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Multifunctional enzyme; Nucleotide-binding.
FT   CHAIN         1    654       Acetyl-/propionyl-coenzyme A carboxylase
FT                                alpha chain.
FT                                /FTId=PRO_0000426912.
FT   DOMAIN        1    448       Biotin carboxylation.
FT   DOMAIN      120    319       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      578    653       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    294    294       {ECO:0000250}.
FT   BINDING     116    116       ATP. {ECO:0000250}.
FT   BINDING     200    200       ATP. {ECO:0000250}.
FT   BINDING     235    235       ATP. {ECO:0000250}.
FT   MOD_RES     620    620       N6-biotinyllysine. {ECO:0000250,
FT                                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
//
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