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Database: UniProt
Entry: A0A0N1CK37_9ENTE
LinkDB: A0A0N1CK37_9ENTE
Original site: A0A0N1CK37_9ENTE 
ID   A0A0N1CK37_9ENTE        Unreviewed;      1142 AA.
AC   A0A0N1CK37;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   10-APR-2019, entry version 19.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=AEQ18_10300 {ECO:0000313|EMBL:KPG69805.1};
OS   Enterococcus sp. RIT-PI-f.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1690244 {ECO:0000313|EMBL:KPG69805.1, ECO:0000313|Proteomes:UP000037898};
RN   [1] {ECO:0000313|EMBL:KPG69805.1, ECO:0000313|Proteomes:UP000037898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-f {ECO:0000313|EMBL:KPG69805.1,
RC   ECO:0000313|Proteomes:UP000037898};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         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|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:KPG69805.1}.
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DR   EMBL; LHOX01000017; KPG69805.1; -; Genomic_DNA.
DR   RefSeq; WP_054116252.1; NZ_LHOX01000017.1.
DR   EnsemblBacteria; KPG69805; KPG69805; AEQ18_10300.
DR   PATRIC; fig|1690244.3.peg.1947; -.
DR   Proteomes; UP000037898; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; 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   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; PS00866; CPSASE_1; 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:UP000037898};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:KPG69805.1};
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:KPG69805.1}.
FT   DOMAIN        1    451       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      528    796       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1071   1140       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    291    291       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       537    537       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       706    706       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       735    735       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       737    737       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     116    116       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     200    200       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     235    235       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     609    609       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     870    870       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1142 AA;  127776 MW;  B7E9D5CC6A2E3F4A CRC64;
     MKKILVANRG EIAIRVFRAC AELGIKTVGI YAAEDEYSVH RFKADEAYLV GKGKRPIDAY
     LDIEDIIRTA KKAGAQGIHP GYGFLSENLG FAQRCEEEGL IFIGPSTHHL DIFGDKIKAK
     AAAVEAGIQS IPGSDGPVDT VEEVLDFAKT HEYPIMIKAA LGGGGRGMRV AHDEKEARDG
     YERAKSEAKA AFGSDEVYVE KYISNPKHIE VQILGDKHGN VVHLFERDCS VQRRHQKVVE
     VAPCVSMDEA QREKICQAAV QLMKHVGYIN AGTVEFLVEG DKFYFIEVNP RVQVEHTITE
     MITNLDIVTT QILIAQGKDL HKEIGIPKQE DIRFEGVAIQ CRVTTEDPAN QFMPDTGKID
     TYRSPGGFGV RLDVGNAYAG AVVTPYFDSL LVKVCTHAAT FDQAIQKMMR CLKEFRIRGV
     KTNILFMRNV VSHPAFRSGE AKTTFIDNTP ELFDFPRIRD RGNKTMKYIG EITINGFPGI
     EKQPKPFYNE PRLPQKIETL ADYTSAKQVL DQNGADAVVS WIGNQKNVLL TDTTFRDAHQ
     SLLATRVRTQ DFKKIAAMTE EAIPQLFSSE MWGGATFDVA YRFLTEDPWE RLRMFRKRMP
     NTLLQMLFRG SNAVGYSNYP DNVLVEFIKE AADQGIDVFR IFDSLNWIPQ MEKSIQAVRD
     TGKIAEATIC YTGDINDPTR QKYSVQYYKD MAKELQNLGA HIIAIKDMAG LLKPQAAYRL
     ISELKDSIDV PIHLHTHDTS GNGIITYSAA TKAGVDIVDV AMSAVSGATS QPSMSSLYYA
     LVNGARCPEI NVDNIQQLNH YWEDVRMYYH SFENGLNAPQ TEVYKHEMPG GQYSNLQQQA
     KAVGLGEKWD EIKEVYHDVN MMFGDIVKVT PSSKVVGDMA LFMVQNGLSE QDIYEQGDNL
     SFPESVVTFF QGELGQPVGG FPEKLQKIIL KGRPAYTERP GAFAKPVDFE TVKQELAEKI
     GYQPKHEEVL SYLMYPQVFL DYRKAYEQFA DVKVLDTPTF FNGMRLGETI NVELEKGKIL
     IIRLDEIGEA DIEGNRTLFF NLNGQRREIV VKDNSIISSV QTKRKAEPTN KEQIGASMSG
     SVLEILVHKG DRVAKGQTLM VTEAMKMETS VEARFAGVVE HVYVAAGEPI QSGDLLIEIK
     EK
//
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