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Database: UniProt/TrEMBL
Entry: A5U6X6_MYCTA
LinkDB: A5U6X6_MYCTA
Original site: A5U6X6_MYCTA 
ID   A5U6X6_MYCTA            Unreviewed;      1127 AA.
AC   A5U6X6;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   11-JUN-2014, entry version 54.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
GN   Name=pca; OrderedLocusNames=MRA_2995;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RA   Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y.,
RA   Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.;
RT   "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra,
RT   a non-pathogenic variant closely related to the well-characterized
RT   pathogenic strain H37Rv.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step
CC       and the transfer of the carboxyl group to pyruvate in the second
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate.
CC   -!- COFACTOR: Biotin (By similarity).
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DR   EMBL; CP000611; ABQ74776.1; -; Genomic_DNA.
DR   RefSeq; YP_001284338.1; NC_009525.1.
DR   ProteinModelPortal; A5U6X6; -.
DR   SMR; A5U6X6; 4-1126.
DR   STRING; 419947.MRA_2995; -.
DR   EnsemblBacteria; ABQ74776; ABQ74776; MRA_2995.
DR   GeneID; 5211878; -.
DR   KEGG; mra:MRA_2995; -.
DR   PATRIC; 18146329; VBIMycTub106795_3354.
DR   eggNOG; COG1038; -.
DR   HOGENOM; HOG000282801; -.
DR   KO; K01958; -.
DR   OMA; YAIQSRV; -.
DR   OrthoDB; EOG6CVV6Z; -.
DR   BioCyc; MTUB419947:GJ8N-3096-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866:SF10; PTHR18866:SF10; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 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; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Complete proteome; Ligase; Nucleotide-binding;
KW   Pyruvate.
SQ   SEQUENCE   1127 AA;  120424 MW;  84B0A4CC1A23CD90 CRC64;
     MFSKVLVANR GEIAIRAFRA AYELGVGTVA VYPYEDRNSQ HRLKADESYQ IGDIGHPVHA
     YLSVDEIVAT ARRAGADAIY PGYGFLSENP DLAAACAAAG ISFVGPSAEV LELAGNKSRA
     IAAAREAGLP VLMSSAPSAS VDELLSVAAG MPFPLFVKAV AGGGGRGMRR VGDIAALPEA
     IEAASREAES AFGDPTVYLE QAVINPRHIE VQILADNLGD VIHLYERDCS VQRRHQKVIE
     LAPAPHLDAE LRYKMCVDAV AFARHIGYSC AGTVEFLLDE RGEYVFIEMN PRVQVEHTVT
     EEITDVDLVA SQLRIAAGET LEQLGLRQED IAPHGAALQC RITTEDPANG FRPDTGRISA
     LRTAGGAGVR LDGSTNLGAE ISPYFDSMLV KLTCRGRDLP TAVSRARRAI AEFRIRGVST
     NIPFLQAVLD DPDFRAGRVT TSFIDERPQL LTARASADRG TKILNFLADV TVNNPYGSRP
     STIYPDDKLP DLDLRAAPPA GSKQRLVKLG PEGFARWLRE SAAVGVTDTT FRDAHQSLLA
     TRVRTSGLSR VAPYLARTMP QLLSVECWGG ATYDVALRFL KEDPWERLAT LRAAMPNICL
     QMLLRGRNTV GYTPYPEIVT SAFVQEATAT GIDIFRIFDA LNNIESMRPA IDAVRETGSA
     IAEVAMCYTG DLTDPGEQLY TLDYYLKLAE QIVDAGAHVL AIKDMAGLLR PPAAQRLVSA
     LRSRFDLPVH LHTHDTPGGQ LASYVAAWHA GADAVDGAAA PLAGTTSQPA LSSIVAAAAH
     TEYDTGLSLS AVCALEPYWE ALRKVYAPFE SGLPGPTGRV YHHEIPGGQL SNLRQQAIAL
     GLGDRFEEIE EAYAGADRVL GRLVKVTPTS KVVGDLALAL VGAGVSADEF ASDPARFGIP
     ESVLGFLRGE LGDPPGGWPE PLRTAALAGR GAARPTAQLA ADDEIALSSV GAKRQATLNR
     LLFPSPTKEF NEHREAYGDT SQLSANQFFY GLRQGEEHRV KLERGVELLI GLEAISEPDE
     RGMRTVMCIL NGQLRPVLVR DRSIASAVPA AEKADRGNPG HIAAPFAGVV TVGVCVGERV
     GAGQTIATIE AMKMEAPITA PVAGTVERVA VSDTAQVEGG DLLVVVS
//
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