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}.
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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
//