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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   24-JUN-2015, entry version 61.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   Name=pca {ECO:0000313|EMBL:ABQ74776.1};
GN   OrderedLocusNames=MRA_2995 {ECO:0000313|EMBL:ABQ74776.1};
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ74776.1, ECO:0000313|Proteomes:UP000001988};
RN   [1] {ECO:0000313|EMBL:ABQ74776.1, ECO:0000313|Proteomes:UP000001988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative
RT   genomic analysis of Mycobacterium tuberculosis strain H37Ra versus
RT   H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate. {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
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DR   EMBL; CP000611; ABQ74776.1; -; Genomic_DNA.
DR   RefSeq; WP_003415003.1; NC_009525.1.
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   KEGG; mra:MRA_2995; -.
DR   PATRIC; 18146329; VBIMycTub106795_3354.
DR   eggNOG; COG1038; -.
DR   HOGENOM; HOG000282801; -.
DR   KO; K01958; -.
DR   OMA; PIEAYLD; -.
DR   OrthoDB; EOG6CVV6Z; -.
DR   BioCyc; MTUB419947:GJ8N-3096-MONOMER; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; 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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2};
KW   Biotin {ECO:0000256|RuleBase:RU000428};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001988};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2};
KW   Pyruvate {ECO:0000313|EMBL:ABQ74776.1}.
FT   ACT_SITE    292    292       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       533    533       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       703    703       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       732    732       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       734    734       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     117    117       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     200    200       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     235    235       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     605    605       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     867    867       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
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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