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Database: UniProt/TrEMBL
Entry: A0A077EGU4_9FLAO
LinkDB: A0A077EGU4_9FLAO
Original site: A0A077EGU4_9FLAO 
ID   A0A077EGU4_9FLAO        Unreviewed;       845 AA.
AC   A0A077EGU4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=BD94_2008 {ECO:0000313|EMBL:AIL45783.1};
OS   Elizabethkingia anophelis NUHP1.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Elizabethkingia.
OX   NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL45783.1, ECO:0000313|Proteomes:UP000028933};
RN   [1] {ECO:0000313|EMBL:AIL45783.1, ECO:0000313|Proteomes:UP000028933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL45783.1};
RX   PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA   Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M.,
RA   Lin R.T., Yang L.;
RT   "First case of E anophelis outbreak in an intensive-care unit.";
RL   Lancet 382:855-856(2013).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00635164};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP007547; AIL45783.1; -; Genomic_DNA.
DR   RefSeq; WP_024564362.1; NZ_CP007547.1.
DR   EnsemblBacteria; AIL45783; AIL45783; BD94_2008.
DR   GeneID; 23373245; -.
DR   KEGG; eao:BD94_2008; -.
DR   KO; K01595; -.
DR   Proteomes; UP000028933; 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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028933};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AIL45783.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028933}.
SQ   SEQUENCE   845 AA;  98507 MW;  BE033B027DD771DA CRC64;
     MKTNEQVEKF RQIVKNKFQI YNSLFMSLPY DKMTNIGMLL PFLHEESKEG YENGKSPMEV
     MKHFFDSHTD LKTEEERIDL LFRIIQYVER QVVLFDSIED SAFSTLNANT DPGTVRNLYE
     VASQQGKLHI IKEKMEHFGV KVVFTAHPTQ FYSNSVQSIL HDLNQAIKSD SVTNIDMLLQ
     QLGMTSFINQ EKPTPYDEAQ SIIYYLRYVY YDTLGELYRD TKRVFDDAHI NPHLFQLGFW
     PGGDRDGNPF VTSEITQRVS SELRLAILKC YYEHLKKLRK RITFPRVTEM LRLISERVYQ
     NIFENKYDLT AGEFKKALQD IRHEVKENNN GLFIDKIDDL LGRIDLFGIY FASLDIRQNS
     KIHYKALEQI FEKEFCKDYH ALGDDEKLNL LLNTSLHVNP EDYSDDIVQD TLKNIYQVKE
     IQKINGEKSI HRYIISDSSS IYDVLNVYAL FKYCGYQGED IKIDIVPLFE TIEGFENAEA
     TMKKLYNLSQ YKEHLTRRSD RQFIMLGFSD GTKDAGYIKA NWDIYTTKEV LTKVSDENDI
     KVIFFDGRGG PPARGGGKTH QFYASQGKSI ANHQIELTIQ GQTITSVFGT KDQATFNFEQ
     LLTAGIENEI FPQDKINLKD WERDLLNELA GISYQKYKAL KDHPLFVPYL EEVSTLKYYG
     RTNIGSRPSK RNDGQLVFED LRAIPFVGSW SLLKQNVPGY FGVGTALQRL KEEGRLEDLK
     KLYRESMFFK TLIQNSMMSM SKTYFPLTYY LRNDKIFGEF WQILHNEYLL THEMLLEIAN
     YKSLMEEEPL SKSSIKMREN IVLPLLTIQQ YALQKIKEEN PHKETYEKIV TRALFGNINA
     SRNSA
//
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