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}.
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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
//