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Database: UniProt/TrEMBL
Entry: A0A1U9LAD5_9FLAO
LinkDB: A0A1U9LAD5_9FLAO
Original site: A0A1U9LAD5_9FLAO 
ID   A0A1U9LAD5_9FLAO        Unreviewed;       859 AA.
AC   A0A1U9LAD5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=BXQ17_13140 {ECO:0000313|EMBL:AQS94969.1};
OS   Polaribacter sp. BM10.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Polaribacter.
OX   NCBI_TaxID=1529069 {ECO:0000313|EMBL:AQS94969.1, ECO:0000313|Proteomes:UP000189235};
RN   [1] {ECO:0000313|EMBL:AQS94969.1, ECO:0000313|Proteomes:UP000189235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM10 {ECO:0000313|EMBL:AQS94969.1,
RC   ECO:0000313|Proteomes:UP000189235};
RA   Lee J.-Y., Bae J.-W.;
RT   "Polaribacter aureus sp. nov., isolated from the gut of a blood
RT   cockle, tegillarca granosa.";
RL   Submitted (FEB-2017) 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; CP019704; AQS94969.1; -; Genomic_DNA.
DR   KEGG; pola:BXQ17_13140; -.
DR   KO; K01595; -.
DR   Proteomes; UP000189235; 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:UP000189235};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AQS94969.1}.
SQ   SEQUENCE   859 AA;  98714 MW;  A6D550B0D92BC713 CRC64;
     MSGLPKLARF NENVLSKYQI YNSIFMTLPF DTINNTGVLL PLFNELCKKG FQEGKNPTEI
     VDAFFSKYQE NPSEKEKTDL LFRFIQYIER QVVLFDAIED AAFPVVNNMD GVGTLRNSKE
     TAILGEKKEA LKAYLEEFKV RVVLTAHPTQ FYPGSVLGII TDLDKAIQND DLLLIKKLLA
     QLGKTPFYKK SKPTPFDEAV SLIWYLENVF YHSVSKIYNY IQNNIYDGNP MDNEIIDLGF
     WPGGDRDGNP FVTTQITLDV AERLRQSVLR SYYRDVRKLK RRFTFDGVQE ILTKIEKRLY
     KHVVRSYSKV NFSQGILLQE LAEARKIVET KHQSLFIEEL DDFINKVRIF GFHFATLDIR
     QDSRVHHKAF TQIVKDLQET GDTTFPKNYE HLPEDEQIEI LSVVKGSIDP KSLSDETSVS
     TIESIYALKE IQKRNGERGA NRYIISNNQT ALNVMETFAM LNLCGFENEL PVDVIPLFET
     VEDLQNAEEV MRKLYSNRTY RYHLEKRKNK QTIMLGFSDG TKDGGYLMAN WGIFKAKEAL
     TKVSREFDIE VIFFDGRGGP PARGGGKTHQ FYASLGPTIE DKEIQLTIQG QTISSNFGTE
     NSAQYNLEQL LSSGIKNDIF TKDQLNEKNR ELIEDMAATS YQTYVDFKNH AQFLPYLEKM
     STLKYYAKTN IGSRPSKRGG SDKLDFSALR AIPFVGSWSQ LKQNVPGFFG VGTALKKYED
     ADRFDEVIAF YNESDFFKTL LENSMMSLTK SFFELTAYMA NDKEFGDFWK LIYEEYKTTK
     RLLLKLTGHK DLMENFPVGK ASIEIREQIV LPLLTIQQFA LKQIQELQNS DGNSEKLKIY
     EKMVMRSLFG NINASRNSA
//
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