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Database: UniProt
Entry: P46392
LinkDB: P46392
Original site: P46392 
ID   BCCA_MYCLE              Reviewed;         598 AA.
AC   P46392;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   16-JAN-2019, entry version 135.
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=bccA; OrderedLocusNames=ML0726; ORFNames=B1308_C1_129;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; 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
RT   carboxyl carrier protein genes from Mycobacterium leprae and M.
RT   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: 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; 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   ProteinModelPortal; P46392; -.
DR   SMR; P46392; -.
DR   STRING; 272631.ML0726; -.
DR   EnsemblBacteria; CAC30235; CAC30235; CAC30235.
DR   GeneID; 909662; -.
DR   KEGG; mle:ML0726; -.
DR   PATRIC; fig|272631.5.peg.1321; -.
DR   Leproma; ML0726; -.
DR   eggNOG; ENOG4108JIK; Bacteria.
DR   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   KO; K11263; -.
DR   OMA; FVEICSH; -.
DR   BioCyc; MLEP272631:G1GT5-794-MONOMER; -.
DR   UniPathway; UPA00094; -.
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: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; Reference proteome.
FT   CHAIN         1    598       Acetyl-/propionyl-coenzyme A carboxylase
FT                                alpha chain.
FT                                /FTId=PRO_0000146797.
FT   DOMAIN        8    452       Biotin carboxylation.
FT   DOMAIN      127    324       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      522    598       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    299    299       {ECO:0000250}.
FT   BINDING     123    123       ATP. {ECO:0000250}.
FT   BINDING     207    207       ATP. {ECO:0000250}.
FT   BINDING     242    242       ATP. {ECO:0000250}.
FT   MOD_RES     564    564       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT     30     30       D -> H (in Ref. 1; CAA45070).
FT                                {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
//
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