ID   S7J231_9FIRM            Unreviewed;      1144 AA.
AC   S7J231;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   01-OCT-2014, entry version 5.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=NM10_06128 {ECO:0000313|EMBL:EPP18001.1};
OS   Megasphaera sp. NM10.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1273103 {ECO:0000313|EMBL:EPP18001.1};
RN   [1] {ECO:0000313|EMBL:EPP18001.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NM10 {ECO:0000313|EMBL:EPP18001.1};
RX   PubMed=24260205;
RA   Shetty S.A., Marathe N.P., Lanjekar V., Ranade D., Shouche Y.S.;
RT   "Comparative Genome Analysis of Megasphaera sp. Reveals Niche
RT   Specialization and Its Potential Role in the Human Gut.";
RL   PLoS ONE 8:E79353-E79353(2013).
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: Biotin. {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EPP18001.1}.
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DR   EMBL; APHY01000027; EPP18001.1; -; Genomic_DNA.
DR   EnsemblBacteria; EPP18001; EPP18001; NM10_06128.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; 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; 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; 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   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; 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   Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:EPP18001.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594};
KW   Pyruvate {ECO:0000313|EMBL:EPP18001.1}.
SQ   SEQUENCE   1144 AA;  127790 MW;  C88FC30FC52EFB8D CRC64;
     MKKIRSVLVA NRGEIAIRVF RACNELGIRT VAIYSKEDSL SLHRFRADES YLVGEGKKPV
     DAYLDIEDII RIAHEHDVDA IHPGYGFLSE NADLAKRCEE EGIIFIGPKV EHLIMFGDKI
     NARIQAKKAG IQYIPGSDGP VMNYAEVEKF AKQVGFPIML KAVNGGGGRG MRMVDRMADL
     RDAYDRAKSE AKLAFGNDEI YLEKCIVNPK HVEVQIMGDE HGNVIHLFER DCSIQRRHQK
     VVETAPASAL PVELRQKICN AALKLMKNVH YVNAGTVEFL VTPDGEFYFI EVNPRVQVEH
     TVTEMITGID IVQTQIKVAE GYALDSDEIG IKSQDDVRCL GDAIQCRITT EDPMNNFMPD
     SGKIMVYRSG GGFGVRLDSG NAYTGAIITP YYDSLLVKTT TYGRTHKEAA EKMLRVLKEF
     RIRGVKTNIG FLINVLKSPE FIAGTYNVNF IDDHPELFNL PVVQDRGTKL LKYIGNTTIN
     GYADAGHQDK PEFEALELPT PVAGPYPDGT KQKFDAMGPE KFSQWIKDQK KVFFTDTTMR
     DAHQSLFATR VRSIDMLRVL EAASKKLPNL FSYECWGGAT FDVAYRFLYE DPWVRLHQMR
     KKAPNILLQM LVRGANAVGY TSYPDNVVKN FIDLSAKNGI DVFRVFDSLN SLDNMYGTIQ
     AVRENNKLAE VALCYTGDIL DPARDKYDLK YYVNMAKELQ NAGANIIAIK DMAGLLKPEA
     AYRLVSALKD AVDLPIHLHT HDGSGNAICT YDRAIDAGVD IVDVAYSAFA GGTSQPSMST
     LYYALSGKDR QPDLDVDAME EMSRYWATVR PYYKGVDKAD AYPNTEVYQH EMPGGQFSNL
     RQQAKAVGLG DRWNEIKKMY HTVSMMFGDI IKVTPSSKVV GDMTLFMVQN NLTEQDVYDK
     GDVLDFPQSV VEFFEGRIGI PYQGFPEKLQ KIVLKGKKPL TERPGKSLAP VDFEAIRKKL
     TDAGYKHEDE DINAYCQYPK VFKDFNETVK KYGDVSVLDT PTFFFGMKKN EEVHVEIEEG
     KDLIITLINI SDPDDSGVRT ITFMFNGAER EIQVQDKSVD MKTVTRRKAD PDKAGDIGAT
     LSGSVVKVLV TKGQKVKKGE PLVVTEAMKM ETTITSPIDG TVGEIYATKG QAIISGDCLL
     EVLA
//