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Database: UniProt/TrEMBL
Entry: A0A1L3JLG5_9FLAO
LinkDB: A0A1L3JLG5_9FLAO
Original site: A0A1L3JLG5_9FLAO 
ID   A0A1L3JLG5_9FLAO        Unreviewed;       859 AA.
AC   A0A1L3JLG5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=LPB136_11415 {ECO:0000313|EMBL:APG65933.1};
OS   Tenacibaculum sp. LPB0136.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG65933.1, ECO:0000313|Proteomes:UP000181898};
RN   [1] {ECO:0000313|EMBL:APG65933.1, ECO:0000313|Proteomes:UP000181898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0136 {ECO:0000313|EMBL:APG65933.1,
RC   ECO:0000313|Proteomes:UP000181898};
RA   Kim E., Yi H.;
RT   "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL   Submitted (NOV-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: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; CP018155; APG65933.1; -; Genomic_DNA.
DR   RefSeq; WP_072556456.1; NZ_CP018155.1.
DR   KEGG; ten:LPB136_11415; -.
DR   KO; K01595; -.
DR   Proteomes; UP000181898; 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:UP000181898};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:APG65933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000181898}.
SQ   SEQUENCE   859 AA;  98293 MW;  1B961943E638C9FA CRC64;
     MATQPKLIRF NQNVLSKYQI YNSIFMTLPF DTITKTGALL PLFHETCQKG FSQKDNPTTI
     VETFFKKYQS SRSKESQTNL LFRFIQYIER QVVLFDAIED AAFPFVNNMD GIGTLRSLKE
     NATAENKLEA LKAYLEEFKV RIVLTAHPTQ FYPGSVLGII TDLTEAIREN DLLKINDLLA
     QLGKTPFFKH EKPTPYDEAV SLIWYLENVF YKSFGSIYDY IQQNIFDGEH INNDIINIGF
     WPGGDRDGNP FVTPEITLKV ANRLRETVIK NYYRDIRRLR RKLTFEDVEN RITILERELY
     KMITNQESDL TLTSFNSELK EIKQVIIDKH QSLYVTEVNS LLNKIHLFGF HFANLDIRQD
     SRKHEQFFND MVNALIESGS AIFPKNYHDL PESEQVKLLS KVEGAVDLSL IKDEETLKAL
     NTMKAIKTIQ TTNGEVAANR YIISNNQTTL HVMQLFAMLK LVAFQDKLTV DVGPLFETIT
     DLENAPQVME DLYTNPEYAA HLKSRGNKQT IMLGFSDGTK DGGYLMANWA IYKAKENLTT
     ISRKYGVTVI FFDGRGGPPA RGGGKTHNFY ASLGPTIEDK EVQLTIQGQT ISSNFGTLDS
     SQYNLEQLIS SGIYNSLSDK DLSMLPENRE VMTDLSERSY KAYSDFKAHP KFISYLEYMS
     TLKYYAKTNI GSRPSKRGKA EGLVFEDLRA IPFVGSWSQL KQNVPGFFGV GTALKHYEDT
     NTFEKVQTLF KTSDFFKTLI ENSMMSLSKS FFDLTKYMSE DEEYGGFWNV IYEEYKTSKR
     LLLKLTGYTE LMQEEPAGSA SIAVRESIVL PLLTIQQYAL KKIQELEKAE TKDEEQIKVY
     EKLVTRSLFG NINASRNSA
//
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