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Database: UniProt/TrEMBL
Entry: A0A0C5VUY8_9FLAO
LinkDB: A0A0C5VUY8_9FLAO
Original site: A0A0C5VUY8_9FLAO 
ID   A0A0C5VUY8_9FLAO        Unreviewed;       862 AA.
AC   A0A0C5VUY8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 16.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=AW14_04225 {ECO:0000313|EMBL:AJR02961.1};
OS   Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Siansivirga.
OX   NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR02961.1, ECO:0000313|Proteomes:UP000032229};
RN   [1] {ECO:0000313|EMBL:AJR02961.1, ECO:0000313|Proteomes:UP000032229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR02961.1,
RC   ECO:0000313|Proteomes:UP000032229};
RA   Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL   Submitted (FEB-2014) 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; CP007202; AJR02961.1; -; Genomic_DNA.
DR   RefSeq; WP_044637664.1; NZ_CP007202.1.
DR   EnsemblBacteria; AJR02961; AJR02961; AW14_04225.
DR   KEGG; sze:AW14_04225; -.
DR   PATRIC; fig|1454006.5.peg.821; -.
DR   KO; K01595; -.
DR   Proteomes; UP000032229; 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:UP000032229};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AJR02961.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032229}.
SQ   SEQUENCE   862 AA;  99132 MW;  F1A38E7AD0753C79 CRC64;
     MSVEPKLSRF KQQVLSKYQI YNSIFMTLPF DTITKTGVLL PLFHETCKKG FANGDDPTKI
     VDTFFEKYQG RRSKESQINL LFRFIQYIER QVVLFDAVED AAFPIVNNME GIGTLRNLKE
     SASSNNKLEE LKKYLEEFKV RIVLTAHPTQ FYPGTVLGII TDLTAAIKSN NLSEINNLFA
     QLGKTPFFKH EKPTPYDEAK SLIWYLENVF YHSFGEIYNY IQQNIYDDGK KHNEIINIGF
     WPGGDRDGNP FVKPDTTLKV ARKLKQAALK KYYADLKNLR RKLTFRGVEE RIIRLETIMY
     NYSININTPE KITAKELLKE LLSIRNLIEE KHQSLYVNEI NNLINRIHLF GFHFATLDIR
     QDSRIHHSVF TNVVDHLIAT GSKSFPKNYH DLTEAQQIEI LSKVSDEKID FDAFEDEMVY
     NTLKTIEVIK DIQKTNGERG ANRYIISNNQ TALNVMQLFA MLKMVAFKDE LTVDVVPLFE
     TIDDLENAPK VMEQLYTNPV YMEHLKSRGN RQTIMLGFSD GTKDGGYLMA NWGIYKAKEL
     LTAMSRKYDI TAIFFDGRGG PPARGGGKTH QFYSSLGPTI EDKEVQLTIQ GQTISSNFGT
     LDSSQYNLEQ LISSGMFNRL GKENHKMSDE DKIVMADLAE TSYAAYKEFK GHEMFIPYLE
     RMSTLKYYAK TNIGSRPSKR GTSDKLVFSD LRAIPFVGSW SQLKQNVPGF FGVGTALKKY
     EDKGEFYKVE QLYKNSKFFK TLLENSMMSL TKSFFDLTKY MSKDEEFGAF WNIIYTEYTT
     TKALLLKLTG YKELMENEPS GKASIEVRES IVLPLLTIQQ YALKKIQELN RSGVQDEEQL
     KIYEKIVTRS LFGNINASRN SA
//
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