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Database: UniProt/TrEMBL
Entry: A0A1B8U3Q3_9FLAO
LinkDB: A0A1B8U3Q3_9FLAO
Original site: A0A1B8U3Q3_9FLAO 
ID   A0A1B8U3Q3_9FLAO        Unreviewed;       859 AA.
AC   A0A1B8U3Q3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   22-NOV-2017, entry version 8.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=LPB3_00460 {ECO:0000313|EMBL:OBY66505.1};
OS   Polaribacter vadi.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Polaribacter.
OX   NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY66505.1, ECO:0000313|Proteomes:UP000092584};
RN   [1] {ECO:0000313|EMBL:OBY66505.1, ECO:0000313|Proteomes:UP000092584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0003 {ECO:0000313|EMBL:OBY66505.1,
RC   ECO:0000313|Proteomes:UP000092584};
RA   Wen L., He K., Yang H.;
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}.
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:OBY66505.1}.
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DR   EMBL; LSFM01000001; OBY66505.1; -; Genomic_DNA.
DR   RefSeq; WP_065317627.1; NZ_LSFM01000001.1.
DR   EnsemblBacteria; OBY66505; OBY66505; LPB3_00460.
DR   KEGG; pob:LPB03_09075; -.
DR   KO; K01595; -.
DR   Proteomes; UP000092584; Unassembled WGS sequence.
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:UP000092584};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:OBY66505.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092584}.
SQ   SEQUENCE   859 AA;  98648 MW;  44A64C62F23CB4D4 CRC64;
     MSALPELTRF NDNVLSKYQI YNSIFITLPF DTIDNTGVLL PLFHKICEKG FEQGKNPTEI
     VEEFFSKYQD SSEGKNKTDL LFQFIQYIER QVVLFDAIED AAFPIVNNMD GIGTLRNSKE
     IAILNDKKEE LKKHLEDFKV RVVLTAHPTQ FYPGSVLGII TDLDQAIQND DLLLIKKLLA
     QLGKTPFYKK TKPTPYDEAI SLIWYLENVF YHSVPKIYNY IQHNVYDGHP IDNEIIDLGF
     WPGGDRDGNP FVTTQITLDV AERLRQSILR NYYRDVRRLK RRFTFDGVHE ILSKIEKRLY
     KHVIRSYSKV NFSQKILLEE LYAARDIITE NHNSLFIEEL NDFINKVRIF GFHFATLDIR
     QDSRVHHKAF TQIVEDLLAS GDATFPKNYH QLSEDDQIKV LAEIKGTIDP AILSDEMSVK
     TIESIYALKT IQQRNGERGA NRYIISNNQT TLNVMQTFAM LNLCGFENEL PVDVIPLFET
     VDDLENASDV MRTLYTNNTY RYHLSKRKNK QTIMLGFSDG TKDGGYLMAN WGIFKAKEAL
     TKISREFDIE VIFFDGRGGP PARGGGKTHQ FYASLGPTIE DKEIQLTIQG QTISSNFGTL
     NSSQYNLEQL ISSGIKNEVF TKDQLNDAHR TIIDDLAKTS YKTYVDFKNH PQFLPYLEQM
     STLKYYAKTN IGSRPSKRSN SDTLDFSALR AIPFVGSWSQ LKQNVPGFYG VGTALKKYED
     ANRFDEIVEF YNASDFLKTL LENSMMSLTK SFFGLTAYMA DDEVFGEFWT LIYEEYKTTK
     RLLLKLAGHT VLMENHPVGK ASIEIRESIV LPLLTIQQYA LKKIQELQKS EGNEAEIEIF
     EKMVMRSLFG NINASRNSA
//
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