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Database: UniProt
Entry: A0A150YEI6_9BACI
LinkDB: A0A150YEI6_9BACI
Original site: A0A150YEI6_9BACI 
ID   A0A150YEI6_9BACI        Unreviewed;      1144 AA.
AC   A0A150YEI6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 15.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=A0U40_11330 {ECO:0000313|EMBL:KYG89380.1};
OS   [Bacillus] sp. KCTC 13219.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1811976 {ECO:0000313|EMBL:KYG89380.1, ECO:0000313|Proteomes:UP000075350};
RN   [1] {ECO:0000313|EMBL:KYG89380.1, ECO:0000313|Proteomes:UP000075350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13219 {ECO:0000313|EMBL:KYG89380.1,
RC   ECO:0000313|Proteomes:UP000075350};
RA   Jeong H., Park S.-H., Choi S.-K.;
RT   "Genome sequence of Bacillus sp. KCTC 13219.";
RL   Submitted (MAR-2016) 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:KYG89380.1}.
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DR   EMBL; LUFJ01000034; KYG89380.1; -; Genomic_DNA.
DR   RefSeq; WP_066169654.1; NZ_LUFJ01000034.1.
DR   EnsemblBacteria; KYG89380; KYG89380; A0U40_11330.
DR   Proteomes; UP000075350; 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:UP000075350};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
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:KYG89380.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075350}.
FT   DOMAIN        3    455       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      123    319       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      532    800       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1069   1144       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    294    294       {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;  127129 MW;  431870787747375D CRC64;
     MKKISKILVA NRGEIAIRIF RACNELGIKT VAIYSREDSG AYHRYKADEA YLVGAGKKPI
     DAYLDIESIL SIAKDAQVDA IHPGYGFLSE NVDFARRCEE EGIQFIGPTS AHLDMFGDKV
     KAREQAIQAD IPVIPGTDGP VADLGEVEAF AEKYGYPIMI KAALGGGGRG MRMVQTKDEL
     ASAYERAKSE AKAAFGSDEV YVEKCIVKPK HIEVQILGDM TGEIVHLYER DCSIQRRHQK
     VVEIAPSNSI SADLRQRICD AAVKLMRNVN YINAGTVEFL VAGDDFYFIE VNPRIQVEHT
     ITEMITGIDI VHAQIKVAEG HALHSELIGI PAQDKIPLFG YAIQSRVTTE DPTNDFMPDT
     GKLMVYRSSG GFGVRLDAGN GFQGAVVTPY YDSLLVKIST WGMTFAQAAA KMDRNLREFR
     IRGVKTNIPF LENVVVHEKF LNGQFDTSFI DTTPELFEFP ERKDRGTKLL NYIGNVTLNG
     FPGVEKRTKP IFVQPNKPKI DLLTPPPTGT KQILDERGAD GLVEWIKAQN DVLLTDTTFR
     DAHQSLLATR MRSQDMFQIA DHTARMMHNF FSLEMWGGAT FDVAYRFLKE DPWARLEKLR
     QQMPNVLFQM LLRGANAVGY TNYPDNLIRE FIQESAASGI DVFRIFDSLN WIKGMEVAID
     EVRNSGKIAE AAICYTGDIL DDTRAKYTVQ YYKDMARELE AAGAHILAIK DMAGLLKPEA
     AYRLIAELKD ATSLPIHLHS HDTSGNGIYL YAKAIEAGVD IVDTALGSMA GLTSQPSANS
     LYYATKGASR EIRADIESLE QLNYYWEDVR KYYKDFESGM NSPHSEIYVH EMPGGQYSNL
     QQQAKAVGLG DRWDEVKKMY SQVNFMFGDI VKVTPSSKVV GDMALFMVQN DLTEDNILER
     GQGIDFPDSV IEFFQGYLGQ PHGGFPQDLQ RVVLKEREAI TVRPGELLAP VDFEQLTAEL
     TEKIGRAVTK KDVLAYALYP KVFEEYANIY AQFGDTSVLD TPTFLYGLKL GEEIEVEIEK
     GKTLIVKLVS IGEPQHDGTR IIYFELNGQS RELVIQDLTV EVDGSVALKA DPSNPNQIAA
     TMPGTVLKVV VSKGSAVKRG DHLLITEAMK METTVQAPKD GVVKEIYAAS GDAISTGDLL
     IELE
//
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