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Database: UniProt/TrEMBL
Entry: A0A0P0CTW9_9BACT
LinkDB: A0A0P0CTW9_9BACT
Original site: A0A0P0CTW9_9BACT 
ID   A0A0P0CTW9_9BACT        Unreviewed;       858 AA.
AC   A0A0P0CTW9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=DC20_15225 {ECO:0000313|EMBL:ALJ00077.1};
OS   Rufibacter tibetensis.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ00077.1, ECO:0000313|Proteomes:UP000061382};
RN   [1] {ECO:0000313|EMBL:ALJ00077.1, ECO:0000313|Proteomes:UP000061382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1351 {ECO:0000313|EMBL:ALJ00077.1,
RC   ECO:0000313|Proteomes:UP000061382};
RA   Dai J.;
RT   "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT   radiation-resistant bacterium from tibet plateau.";
RL   Submitted (AUG-2015) 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; CP012643; ALJ00077.1; -; Genomic_DNA.
DR   RefSeq; WP_062544618.1; NZ_CP012643.1.
DR   EnsemblBacteria; ALJ00077; ALJ00077; DC20_15225.
DR   KEGG; rti:DC20_15225; -.
DR   PATRIC; fig|512763.3.peg.3348; -.
DR   KO; K01595; -.
DR   Proteomes; UP000061382; 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   Complete proteome {ECO:0000313|Proteomes:UP000061382};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ALJ00077.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061382}.
SQ   SEQUENCE   858 AA;  97838 MW;  61E20F455623FC25 CRC64;
     MDGSSTSALQ NYDKHVGLKF QLYNSLFTSL PFHRVEKTGV LLSIFLLHCE EGFAKEQSPD
     EIISTFFNQY TPYRTEQEQL DLLFRFVQYA ERQVVLFDAL EDASFRETHD MAGAGTLKHL
     QAEVEQTQTQ AQLQEKLKDF SVRLVLTAHP TQFYPSEVLG IINDLSKALL NDNTAQVNSY
     LRQLGKTPFF KNEKPSPYDE AVSLIWYLEN VFYQAAGQIM SHLKSQFPEA VSEENPLIRL
     GFWPGGDRDG NPFVTASITL RVAEALRGAI IKSYYQDVRR LKRRLTFKGI LNELISLEEK
     LYNNLFLPGY KADITKEAIL APLLRIKDIL IREHNSLFLP LAENLIRKVE LFGLFFASLD
     VRQDSSAHTE ALEAIAATSG ALPENYSQLS AKEKISALLN ANTTVAAESL ENELHRDTLE
     SMQAMKTIQE INGSEGCHRY IISHSTSALD VMEVYGLFML SGWKPEELSV DIVPLFETID
     DLKNAHDVME ALYNSEVYRQ HLHRRGNIQS IMLGFSDGTK DGGYLMSNWS IYKAKEELSR
     LAQQYDLQVV FFDGRGGPPA RGGGRTHQFY ASMGPTIASK EIQLTIQGQT ISSNFGTIDA
     AQYNMEQLMH AGIRNTLFSS KETTFTDQEE DLMQRLAEES YVAYNTLKNN PYFLEYLNYA
     SPLRYYAEAN IGSRPSKRKP GKLNLNDLRA VPYVGSWSQL KQNLPGYYGV GAAMERMEAE
     GQWEAIEHLY SRSLFFRTLL GNCEMAMTKC FFPLTAFLSK HPHYGELWNN IHEEFERTKK
     YVLRLTKNAH LMEDKPVNLL SIQMRQRIEM PLLTIQQFAL TKIREMEEQE NNTPGKSKFE
     KLVMRCSFGI INAERNSA
//
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