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Database: UniProt/TrEMBL
Entry: W0F2M1_9BACT
LinkDB: W0F2M1_9BACT
Original site: W0F2M1_9BACT 
ID   W0F2M1_9BACT            Unreviewed;       860 AA.
AC   W0F2M1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   20-DEC-2017, entry version 25.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=NIASO_12320 {ECO:0000313|EMBL:AHF15724.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15724.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF15724.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007035; AHF15724.1; -; Genomic_DNA.
DR   RefSeq; WP_008585919.1; NZ_CP007035.1.
DR   EnsemblBacteria; AHF15724; AHF15724; NIASO_12320.
DR   KEGG; nso:NIASO_12320; -.
DR   KO; K01595; -.
DR   Proteomes; UP000003586; 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; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|SAAS:SAAS00946757};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003586};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AHF15724.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003586}.
FT   COILED      823    843       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   860 AA;  97317 MW;  CBF3BFF626AF6167 CRC64;
     MDVVASQSVQ RFKNDVGVRF QLYNSLFTSL PFHKIEKTGI LLSLLSSMCE EGYEKGSSPV
     TIIEDFFSRH TSLTVPREQL DLLFRFVQYV ERQVVLFDAL EDASYKKIND VNGPGTLKQL
     MAAVVQNNRE QQFDKVLEDF CVRLVLTAHP TQFYPGSVLG IIRDLSNALV KNDASEINTL
     LQQLGKTPFF KKIKPTPFDE AVSLIWYLEN VFYPAAGRIL NELKNQFPAI AADKHALIKM
     GFWPGGDRDG NPFVTTDTTL QVAAALRGAI LKCYYFDVRR LRRRLTFHDV EDIMSDLERR
     LYEEVFIPGK DAKITDKEII SILKGVKQIV IERANGLFVS RIQDLISKIE IFGLHFASLD
     IRQDSSIHEK VFSQIAASPA GLLPKDYDSL EENEKVKLLL NLKQIDTASI FGDSVVRDTV
     EVVNAICAIQ NSNGEQGCNR YIISHATSVL SIIEVIGLFK LNGIDNDEIN VDIVPLFETI
     EDLQNAGEVM KTLYSLPEYK ALLERRGKTQ TIMLGFSDGT KDGGYLMANW SIYRAKEELT
     RITRQYGFDV IFFDGRGGPP SRGGGKTHKF YASMGRNISN KEIQLTIQGQ TVSANFGIID
     SAQFNIEQLI NAGVSSSLFA DRYPPLNGKQ EQLLQELSSY GFDAYVQLKN HPQLANYLYE
     MSPLRFYSET NIGSRPAKRG QQQTTISLGD LRAIPFSGAW SQLKQNVPGF FGVGTALKRM
     EYIGRFDELK QLYNESLYFK TLLDNCEMAM SKSYFPITAY IANDEQFGDI WQMIYDEFAL
     TKQYIYKLTG HDTLMASYPV DKLSIRMRER IVMPLVTIQQ YALVKLRDGN SELEDSLREA
     YEKLVMRCSF GIINAGRNSA
//
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