ID S7J231_9FIRM Unreviewed; 1144 AA. AC S7J231; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 12-OCT-2022, entry version 33. DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594}; DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, 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; unclassified 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 and CC the transfer of the carboxyl group to pyruvate in the second. CC {ECO:0000256|PIRNR:PIRNR001594}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1; CC Evidence={ECO:0000256|PIRNR:PIRNR001594}; CC -!- COFACTOR: CC Name=biotin; Xref=ChEBI:CHEBI:57586; CC Evidence={ECO:0000256|ARBA:ARBA00001953, CC ECO:0000256|PIRNR:PIRNR001594}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 STRING; 1273103.NM10_06128; -. DR EnsemblBacteria; EPP18001; EPP18001; NM10_06128. DR PATRIC; fig|1273103.4.peg.1166; -. DR eggNOG; COG1038; Bacteria. DR Proteomes; UP000014835; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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 InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011761; ATP-grasp. 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_sf. 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594}; KW Biotin {ECO:0000256|PIRNR:PIRNR001594}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:EPP18001.1}. FT DOMAIN 3..456 FT /note="Biotin carboxylation" FT /evidence="ECO:0000259|PROSITE:PS50979" FT DOMAIN 123..320 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 532..800 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" FT DOMAIN 1074..1144 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT ACT_SITE 295 FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1" FT BINDING 119 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 238 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 541 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 613 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 710 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /note="via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 739 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 741 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 874 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR: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 //