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Database: UniProt
Entry: P9WPQ3
LinkDB: P9WPQ3
Original site: P9WPQ3 
ID   BCCA_MYCTU              Reviewed;         654 AA.
AC   P9WPQ3; 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 35.
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=Rv2501c;
GN   ORFNames=MTCY07A7.07c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 50410;
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
RT   carboxyl carrier protein genes from Mycobacterium leprae and M.
RT   tuberculosis.";
RL   J. Bacteriol. 176:2525-2531(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   PUPYLATION AT LYS-322, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA   Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA   Gygi S.P., Darwin K.H.;
RT   "Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT   tuberculosis.";
RL   PLoS ONE 5:E8589-E8589(2010).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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;
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; Z19549; CAA79609.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45295.1; -; Genomic_DNA.
DR   PIR; B55579; B55579.
DR   RefSeq; NP_217017.1; NC_000962.3.
DR   RefSeq; WP_003899356.1; NZ_NVQJ01000063.1.
DR   ProteinModelPortal; P9WPQ3; -.
DR   STRING; 83332.Rv2501c; -.
DR   PaxDb; P9WPQ3; -.
DR   PRIDE; P9WPQ3; -.
DR   EnsemblBacteria; CCP45295; CCP45295; Rv2501c.
DR   GeneID; 887309; -.
DR   KEGG; mtu:Rv2501c; -.
DR   TubercuList; Rv2501c; -.
DR   eggNOG; ENOG4108JIK; Bacteria.
DR   eggNOG; COG4770; LUCA.
DR   KO; K11263; -.
DR   OMA; DYDPMLA; -.
DR   PhylomeDB; P9WPQ3; -.
DR   BioCyc; MTBH37RV:G185E-6737-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   ATP-binding; Biotin; Complete proteome; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Isopeptide bond; Ligase; Lipid biosynthesis;
KW   Lipid metabolism; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN         1    654       Acetyl-/propionyl-coenzyme A carboxylase
FT                                alpha chain.
FT                                /FTId=PRO_0000146798.
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}.
FT   CROSSLNK    322    322       Isoglutamyl lysine isopeptide (Lys-Gln)
FT                                (interchain with Q-Cter in protein Pup).
FT                                {ECO:0000269|PubMed:20066036}.
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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