ID   R4K7G3_CLOPA            Unreviewed;      1142 AA.
AC   R4K7G3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   07-SEP-2016, entry version 18.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=Clopa_4405 {ECO:0000313|EMBL:AGK99117.1};
OS   Clostridium pasteurianum BC1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK99117.1, ECO:0000313|Proteomes:UP000013523};
RN   [1] {ECO:0000313|EMBL:AGK99117.1, ECO:0000313|Proteomes:UP000013523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC1 {ECO:0000313|EMBL:AGK99117.1,
RC   ECO:0000313|Proteomes:UP000013523};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA   Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT   "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL   Submitted (JAN-2012) 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       {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; CP003261; AGK99117.1; -; Genomic_DNA.
DR   RefSeq; WP_015617389.1; NC_021182.1.
DR   EnsemblBacteria; AGK99117; AGK99117; Clopa_4405.
DR   KEGG; cpas:Clopa_4405; -.
DR   KO; K01958; -.
DR   OrthoDB; POG091H02XZ; -.
DR   Proteomes; UP000013523; 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:0003677; F:DNA binding; 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; 1.10.10.60; -; 1.
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; 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; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR009057; Homeodomain-like.
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; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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; PS00866; CPSASE_1; 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|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013523};
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:AGK99117.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013523}.
FT   DOMAIN        3    456       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      123    320       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      528    796       PYR_CT. {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1067   1142       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    295    295       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       537    537       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       706    706       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       735    735       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       737    737       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     119    119       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     203    203       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     238    238       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     609    609       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     870    870       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1142 AA;  127343 MW;  C16AD5572E784BD0 CRC64;
     MKEFKRVLVA NRGEIAIRIF RACKELGIRT VAIYSNEDKY SLFRTKADEA YLIGENKSPV
     EAYLNIEEII SLALKKGVDA IHPGYGFLSE NAEFAKKCAE AGIEFIGPTS EMMDKLGDKI
     KSKIAAKAVG VSTIPGYERD IKTVEEAKKL AKECGYPIML KAAAGGGGRG MRIVRNEEEL
     PDAFMSAKSE AKKAFGIDVM FMEKYLEKPK HIEVQVLGDK YGNIVHLHER DCSIQRRHQK
     VIEFTPAFSL SDEKRNKICE DALKIARSVN YRSAGTLEFL VDANGNHYFI EMNPRVQVEH
     TITEMITGID IVQSQILIAE GYELGSEEIG IYSQDDIKIN GYSIQCRITT EDPFHNFAPD
     TGKIEVYRTS SGFGIRLDGG NGFSGAVISP YYDSLLVKNI SWSRTFKDCV RKTIRAIKET
     NITGVKTNIG FLINVLNHPT FLKGECDTGF IDENPELINI LPHEDEEGRL LKFIGEKVVN
     ETKGIKKEYD VPVVPKVEIQ DTLIGTKQLL DTKGTEGLVS WIKDQSKLLL TDTTMRDANQ
     SLMATRVRTR DMIKIAEATS AYGKDLFSLE MWGGATFDVA YRFLGESPWE RLAQLRKKIP
     NVLFQMLIRG ANAVGYKNYP DNVIREFIRE SANNGIDVFR IFDSLNWLKG MEVSIDEVLK
     SGKVAEACIC YTGDILNDKK TKYNLDYYIK LAKEIEKTGA HILGIKDMSA LLKPHAAYKL
     VGALKQEIGM PIHLHTHDTT GNGVATVLMA AEAGVDIVDT AFNSMSGLTS QPALNSVAAA
     LKNTRRDTGI DLRGIQRVSD YWAAVRPVYY KFESELKSGS AEIYEYEIPG GQYSNLKPQV
     ESFGLGHKFN EIKAMYKKVN DMLGDIVKVT PSSKMVGDFA IFMVQNDITP ENIYDKAVNM
     AFPDSVVAYF KGMMGQPMEG FPKKLQDLVL KGEEPITCRP GELLPEEDFN KIEEYLKDKY
     DIAPNKKDAL SYALYPDVFE DYLNYIKEFG DLSRLGSDVY FHGLSEGETC EAEVANGKTY
     MIKLSGMGKV DQEGNKTLYF EVDGNRREIK IKDRDSKNAQ ETFSTKMADS SNPLEVGAPI
     PGTILKVLVS EGEKVSENQP LMIVEAMKME TRVSASASGT VELINASEGQ QVKAGELLIS
     LK
//