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Database: UniProt/TrEMBL
Entry: A0A0H4PD88_9BACT
LinkDB: A0A0H4PD88_9BACT
Original site: A0A0H4PD88_9BACT 
ID   A0A0H4PD88_9BACT        Unreviewed;       850 AA.
AC   A0A0H4PD88;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=CA2015_2804 {ECO:0000313|EMBL:AKP52214.1};
OS   Cyclobacterium amurskyense.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=320787 {ECO:0000313|EMBL:AKP52214.1, ECO:0000313|Proteomes:UP000036520};
RN   [1] {ECO:0000313|EMBL:AKP52214.1, ECO:0000313|Proteomes:UP000036520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12363 {ECO:0000313|EMBL:AKP52214.1,
RC   ECO:0000313|Proteomes:UP000036520};
RA   Kim K.M.;
RL   Submitted (JUL-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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP012040; AKP52214.1; -; Genomic_DNA.
DR   RefSeq; WP_048644529.1; NZ_CP012040.1.
DR   EnsemblBacteria; AKP52214; AKP52214; CA2015_2804.
DR   KEGG; camu:CA2015_2804; -.
DR   PATRIC; fig|320787.5.peg.3065; -.
DR   KO; K01595; -.
DR   Proteomes; UP000036520; 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   PANTHER; PTHR30523; PTHR30523; 2.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036520};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AKP52214.1}.
SQ   SEQUENCE   850 AA;  96910 MW;  7EAB31B7FE2FE030 CRC64;
     MANIYETEVA KRFTIYNSLF LDLPFDQIYR TGTLLPILSE ACQSGFQENK TPKEIIRQFF
     EELMADKPEE ERHDLLFKMV QYIERQVVLF DSIEDASFEK FNDIKGKGTM TALIARAEND
     HKKEELIEKL KNFSVRLTLT AHPTQFYPGN VLAIITDLEQ AIRKNDLGDV DLLLRQLGKT
     AFINKEKPSP YEEAVSLTWF LEYVFYPSIS DIMIRILNQL NIPLHDWENP NLLKVGFWPG
     GDRDGNPFVT HEITKKVSDK LQNSILKCYY RDIRKVRRRL TFHNVESHLI KAEKGIYNTL
     FSGEGEVFHS KDELLAVLYE ARKGIIEEHG GLSLELLDEF ILKVRVFGFH FASMDVRQDS
     RKHDALWDEI LEKSEGEAAL EVYHQGDEEA KIQKILSVDK LPEINSLEDP FHREMLESIS
     SIAYIQKNNG PMGCHRYIIS NNQSVLHVLE VYQLNKLLLA NGGDLFLDIV PLFETIDDLA
     AAHSVMSSLY NNKTYRDHLR KRGNKQSIML GFSDGTKDGG YIRANWSILR AKEELTKVAR
     EEGIDVVFFD GRGGPPARGG GNTHNFYASL GPNVENREIQ ITIQGQTISA NYGKPVSCSY
     NLEQLLSAGM ESHLYPSSEN SLTDKQKSLI DEMADISYNA YKELKNHEQF VPYLEKVTPL
     KFFGMTNIGS RPVKRSKGGS MKFEDLRAIP FVGAWAQMKQ NIPGFFGVGK AIEELEKQGR
     LGEVQQLYKD SLFFRSLLGN SMQSLAKSFY PATAYLKDDP QFGGFWELMY GEYQRSYDKI
     LSVAGMSTLL EDSPLSKESI AIRERIVLPL ITIQQYAIQT ILEKGKEDTA LQKLILRTMF
     GIINAARNAA
//
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