ID S7J231_9FIRM Unreviewed; 1144 AA. AC S7J231; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 10-MAY-2017, entry version 19. 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; Veillonellales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=1273103 {ECO:0000313|EMBL:EPP18001.1, ECO:0000313|Proteomes:UP000014835}; RN [1] {ECO:0000313|EMBL:EPP18001.1, ECO:0000313|Proteomes:UP000014835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: CC Name=biotin; Xref=ChEBI:CHEBI:57586; CC Evidence={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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; APHY01000027; EPP18001.1; -; Genomic_DNA. DR RefSeq; WP_020310685.1; NZ_APHY01000027.1. DR RefSeq; WP_020310685.1; NZ_APHY01000027.1. DR RefSeq; WP_020310685.1; NZ_APHY01000027.1. DR EnsemblBacteria; EPP18001; EPP18001; NM10_06128. DR Proteomes; UP000014835; Unassembled WGS sequence. 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 InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR005481; BC-like_N. 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; 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; 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, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594}; KW Complete proteome {ECO:0000313|Proteomes:UP000014835}; KW Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:EPP18001.1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594, KW ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:EPP18001.1}. FT DOMAIN 3 456 Biotin carboxylation. FT {ECO:0000259|PROSITE:PS50979}. FT DOMAIN 123 320 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 532 800 Pyruvate carboxyltransferase. FT {ECO:0000259|PROSITE:PS50991}. FT DOMAIN 1074 1144 Lipoyl-binding. {ECO:0000259|PROSITE: FT PS50968}. FT ACT_SITE 295 295 {ECO:0000256|PIRSR:PIRSR001594-1}. FT METAL 541 541 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001594-3}. FT METAL 710 710 Divalent metal cation; via carbamate FT group. {ECO:0000256|PIRSR:PIRSR001594-3}. FT METAL 739 739 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001594-3}. FT METAL 741 741 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 613 613 Substrate. {ECO:0000256|PIRSR: FT PIRSR001594-2}. FT BINDING 874 874 Substrate. {ECO:0000256|PIRSR: FT PIRSR001594-2}. 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 //