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Database: UniProt/TrEMBL
Entry: A0A126NTX2_9BRAD
LinkDB: A0A126NTX2_9BRAD
Original site: A0A126NTX2_9BRAD 
ID   A0A126NTX2_9BRAD        Unreviewed;       941 AA.
AC   A0A126NTX2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-NOV-2017, entry version 9.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=AXW83_09230 {ECO:0000313|EMBL:AMJ60450.1};
OS   Bosea sp. PAMC 26642.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bosea.
OX   NCBI_TaxID=1792307 {ECO:0000313|EMBL:AMJ60450.1, ECO:0000313|Proteomes:UP000061184};
RN   [1] {ECO:0000313|Proteomes:UP000061184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 26642 {ECO:0000313|Proteomes:UP000061184};
RA   Park H.;
RT   "Complete genome of Burkholderia sp.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP014301; AMJ60450.1; -; Genomic_DNA.
DR   RefSeq; WP_066612555.1; NZ_CP014301.1.
DR   EnsemblBacteria; AMJ60450; AMJ60450; AXW83_09230.
DR   KEGG; bop:AXW83_09230; -.
DR   KO; K01595; -.
DR   Proteomes; UP000061184; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 3.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000061184};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AMJ60450.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061184}.
SQ   SEQUENCE   941 AA;  102835 MW;  91965BE7D64D16CF CRC64;
     MTDGSNHIIT PAALAQELLG TIAQARIDAQ EDPFGSPVLR VTLWLTRRMD RGELTLDAAL
     DLVRHLGRQS LRERAARTAD YVGLTEDGDA ALVAVAERLA EASEREASPF EHFRAVVARA
     RFAAVYTAHP TFGMTRTLAH ALAGLASGDA AAAAVMDEPD LTFRPDGKIT LQDEFEQARF
     AVRHARDAID RLNSALLSAA RLRWPDRWRE LAPKPLILAS WVGCDTDGRT DIGWWDTLRY
     RLESKRGQFV RMLEKLPEVA ATAEVREMVA AAIAAVERQL ALAPPISSQP ALTALQAFAL
     SLVGEREAAL PEASRLLAAL DTAIEAAGSD EATATALCLA RAGCVAHGVS IALPHFRLNA
     SQLHNAMRGV IPLDEEPSQP AQRRAFLSAA NAALAKVEPT PVDFGALAAE RASATRMMMT
     IAQIVKHIDG TRPVRFLIAE TETGYTLLSA LWLARRFGIA DKIEISPLFE TSDALEQGPR
     IIDEALRSPH FRDYLKTHGR LCIQFGYSDS GRYIGQIAAS FWVERLRIRI AELLTRYGLT
     AIELVIFDTH GESAGRGAHP GSLEDRLAYL EPAWPRQAFA KAGIATVRET SFQGSDGYLL
     FGTPQLAAAT IGRIAEAVFD SPGEAPADPI YDEPDFATEF FQTVREEMTT LVDDPGYAAL
     IGTFGPSLLD KTGSRPAARQ SDAGGPTRIR HPRELRAIPN NAILQQLGWL ANSVHGIGQA
     ASRSPDLFNQ LRERSERFER AYRLAEHAMA NSDLDVLRAY LDTLDPGNWF DRARRTEREG
     RRDELLAVAE ALAGLELAPA LRRLFWRLSS DWLKLKAVAV ETPQMSARLV ALHALRLSVM
     HRIWLSATHI PDFRPSAGLT REALMERILR LDIPGSLAAL AEIFPLDPDP TIGLDFGEPP
     GPREGGAYAA LHRDVLAPMA TCFALLREIS GAIQHEIGAF G
//
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