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Database: UniProt/TrEMBL
Entry: A0A172TQA0_9BACT
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ID   A0A172TQA0_9BACT        Unreviewed;       856 AA.
AC   A0A172TQA0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   31-JAN-2018, entry version 11.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=SY85_00700 {ECO:0000313|EMBL:ANE49241.1};
OS   Flavisolibacter tropicus.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Flavisolibacter.
OX   NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49241.1, ECO:0000313|Proteomes:UP000077177};
RN   [1] {ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL   Submitted (JAN-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; CP011390; ANE49241.1; -; Genomic_DNA.
DR   RefSeq; WP_066401314.1; NZ_CP011390.1.
DR   EnsemblBacteria; ANE49241; ANE49241; SY85_00700.
DR   KEGG; fla:SY85_00700; -.
DR   PATRIC; fig|1492898.3.peg.154; -.
DR   KO; K01595; -.
DR   Proteomes; UP000077177; 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:UP000077177};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ANE49241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077177}.
SQ   SEQUENCE   856 AA;  97435 MW;  9F8EFA426098AE6A CRC64;
     MDYPSSRALE NFKRQVGLKF QLYNSLFTAL PFHRIEKTGV LLALFLNNCE EGYENKQSPT
     EIVTDFFNRF TSYAGGKEQI DLLFRFVQYV ERQVVLFDAL EDAAFNEVND LVGAGTLKQL
     ISKVVQVNNR QTLIARLKNF SVSLVLTAHP TQFYPGSVLG IINDLAKALK DNKTDQVNLY
     LQQLGKTPLF KHEKPTPYDE AVSLIWYLEN VFYKAIGRIL AELKMEIAGL NLLESQVVKL
     GFWPGGDRDG NPNVTVDTSL KVADALRTSI IKCYYQDVRR LRHRLTFKGV ESILADLESK
     LYHHLFIPGS DITLSQQEIL QSLQQIRNIL VKEHNSLFLF LLDDLINKVE VFGLHFASLD
     IRQESSVHNT VLEEIAAKEN LLPRDYATLN EKEKIELLTS IEGRADISLY EGLTKDTLQS
     FEVIKAIQAT NGPLGCYRYI ISQCTSALNV LEVYGLFLCN GWKKEELSAD IIPLFETIDD
     LKRAPQVMRD LYENQAYRQH LQRRKNIQTI MVGFSDGTKD GGYLMANWSI YKAKNELSLV
     SKEYGIEVIF FDGRGGPPAR GGGKTHKYYA AMGQQISSKE IQLTIQGQTI SSNFGNVDAA
     QYNIEQLLDA GVTNVLFADS KMQMLPEQEE VIIELADISY QAYNQLKQHP QFFDYLAEIS
     PLNYFSDTNI SSRPSKRGKT SGLTLKDLRA IPFVGAWSQI KQNVPGYFGV GTALQTLDDK
     GKLEDIKHLY KQSLYFKTLL DNCEMVMKKS YFSLTAYLAG NPVYSNIYDI IWREYELTKK
     YILLVTERPE LMSDYPVEQL SIQMREKIVL PLTTIQQFAL TKLREDKEMP AEERSVLERL
     VVRTSFGIIN AGRNSV
//
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