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Database: UniProt/TrEMBL
Entry: A0A142ER67_9BACT
LinkDB: A0A142ER67_9BACT
Original site: A0A142ER67_9BACT 
ID   A0A142ER67_9BACT        Unreviewed;       843 AA.
AC   A0A142ER67;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=AO498_14315 {ECO:0000313|EMBL:AMQ57622.1};
OS   Algoriphagus sp. M8-2.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ57622.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-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: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; CP012836; AMQ57622.1; -; Genomic_DNA.
DR   RefSeq; WP_067549124.1; NZ_CP012836.1.
DR   EnsemblBacteria; AMQ57622; AMQ57622; AO498_14315.
DR   KEGG; alm:AO498_14315; -.
DR   PATRIC; fig|1727163.4.peg.3007; -.
DR   KO; K01595; -.
DR   Proteomes; UP000073816; 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:UP000073816};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AMQ57622.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073816}.
SQ   SEQUENCE   843 AA;  96770 MW;  0C9320601D3723E1 CRC64;
     MFQVYDTQVA KRFTIYNSLF LDLPFDDIYR TGTLLPTLAT ACQKGFQSGK TPREIITGFF
     EEMMPNHSEK ERHDLLFQMI QYVERQVVLF DSIEDAAYEK INDLKGKGSI KALIDRADND
     HKREELIEKL KTFSVRLTLT AHPTQFYPGN VLGIITDLEK AIRNDDLGDI NLLLMQLGKT
     GFINREKPTP LDEAVSLIWF LENVFYQSIS DIMIRLLKSL NQPLHTWENP GLLKVGFWPG
     GDRDGNPFVT HETTLNVAER LKKWILRCYY RDIRNLRKRL TFKHVEPIIL KAEQGIFSTL
     FDNKIVYHSK EELLQDLLEA RNGLVTYHNG LFLDLLDEFI LKVRIFGFHF AHMDLRQDSR
     KHDSLWGEIF QLQGRDFDGN EDQLIQALLK TLSLPAIDKF QDSFHREMLE SFGTIRAVQQ
     SNGEEGLHRY IISNCQSALH VMEVFQLSRL TMDQSKNLPL DIVPLFETID DLQAAPEIMA
     KLYSNPDYRA HLKERGNKQT VMLGFSDGTK DGGYLKANWS ILRAKEELTR ASREYDVQVV
     FFDGRGGPPA RGGGNMHNFY ASLGQKVENA EIQVTIQGQT ISANYGKQAS CTYNFEQLLS
     AGLENHLYSD AERNLSDAQR ALIDELADMG YDAYKKLKSH PKFVPYLEHV TPLKYFGMTN
     VGSRPLKRGK GSGLKFEDLR AIPFVGSWAQ MKQNIPGFYG VGAAIEQMKE QGRLDELKKL
     YRESLFFRTL LGNSMQSLTK SFYPATEYLK DNVEYGEFWN ILFAEYTRSI DMLKQISEMK
     ELMGDNPVSK TSIEIREKIV LPLITIQQFA IQTLLDSKIE DQSLQRLILR SMFGIINAAR
     NAA
//
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