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Database: UniProt/TrEMBL
Entry: A4CP85_ROBBH
LinkDB: A4CP85_ROBBH
Original site: A4CP85_ROBBH 
ID   A4CP85_ROBBH            Unreviewed;       848 AA.
AC   A4CP85;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   OrderedLocusNames=RB2501_02240 {ECO:0000313|EMBL:EAR14206.1};
OS   Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Robiginitalea.
OX   NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14206.1, ECO:0000313|Proteomes:UP000009049};
RN   [1] {ECO:0000313|EMBL:EAR14206.1, ECO:0000313|Proteomes:UP000009049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC   {ECO:0000313|Proteomes:UP000009049};
RX   PubMed=19767438; DOI=10.1128/JB.01191-09;
RA   Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL   J. Bacteriol. 191:7144-7145(2009).
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; CP001712; EAR14206.1; -; Genomic_DNA.
DR   RefSeq; WP_015755642.1; NC_013222.1.
DR   ProteinModelPortal; A4CP85; -.
DR   STRING; 313596.RB2501_02240; -.
DR   EnsemblBacteria; EAR14206; EAR14206; RB2501_02240.
DR   KEGG; rbi:RB2501_02240; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000028632; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; RBIF313596:GH7G-3040-MONOMER; -.
DR   Proteomes; UP000009049; 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; 1.
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:UP000009049};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:EAR14206.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009049}.
SQ   SEQUENCE   848 AA;  98416 MW;  1E6CC8C583CD5FCB CRC64;
     MSQVERLKEF KKSVRNKFNI YNSLFLNLPY TEGENVGIYI PLLFQQCDRG LKSGKNPTEI
     LDDFFENFTQ ATDEKERIDL MFRIIQYVER QVVLYDSVED AAFPRLHVHT DSLSIRDYFQ
     LAKKNKRWDK VSKKLESFSA RIVLTAHPTQ FYTPAVLDII AELRTLILEN KIDEIDVTLQ
     QLGLTSLINS KKPTPLDEAK NIIYTLRHVY YQAVGDLYAY IKGSIENDAY DNPDIIKLGF
     WPGGDRDGNP YVTADITMDV ADELRTTLMK CYYNDLKTLQ KRISFRGVQE QMQQLRGKAY
     VAMFDTSKTL SYEEMIETLR EIREILVRDY YGLYLKELDH FIDKVRLFKT HFATLDIRQD
     HSKHYQVVET VLRHHGLIKE SLDELPEERL VELLTRESLE LDPSAYDDPI VKDTLVNMAQ
     LEEIQRKNGE DGCNRYIISN SEDIFSVLFV FGLLRWSGWK NRDLTFDIIP LFETMKGMAE
     AESVMQTLFD LPEYRAHVAQ RRDLQTIMLG FSDGTKDGGY LKANWSIFKT KETLSRVCRR
     NKIKAIFFDG RGGPPARGGG KTHRFYAAQT KAIANHEIQL TVQGQTITST FGTKELFMHN
     SEQLLTAGLS NTIFGKENVI DKSQRDLLET LSELSFEKYN ALKQHELFLP YLENRSTLKY
     YSNANIGSRP GKRGNKAKLE FSDLRAISFV GSWSQLKQNV PGYYGIGTAL KQLKDEGRMP
     ELKKMYKEVA FFRALMLNSM MSLTKCYFEL TSYMKEDEVY KGFWEMLYRE YKLSKQMLLQ
     LSGYKVLMEN ESVSRESVKI RENIVLPLLV IQQYALHRIA EGTDRKELYE KIVTRSLYGN
     INASRNSA
//
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