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Database: UniProt/TrEMBL
Entry: W6QT92_PSEP5
LinkDB: W6QT92_PSEP5
Original site: W6QT92_PSEP5 
ID   W6QT92_PSEP5            Unreviewed;       878 AA.
AC   W6QT92;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-SEP-2017, entry version 26.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CDM39702.1};
GN   ORFNames=BN5_1100 {ECO:0000313|EMBL:CDM39702.1};
OS   Pseudomonas pseudoalcaligenes (strain CECT 5344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=1182590 {ECO:0000313|EMBL:CDM39702.1, ECO:0000313|Proteomes:UP000032841};
RN   [1] {ECO:0000313|EMBL:CDM39702.1, ECO:0000313|Proteomes:UP000032841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5344 {ECO:0000313|Proteomes:UP000032841};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Complete genome sequence of the cyanide-degrading bacterium
RT   Pseudomonas pseudoalcaligenes CECT 5344.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; HG916826; CDM39702.1; -; Genomic_DNA.
DR   RefSeq; WP_003462639.1; NZ_HG916826.1.
DR   EnsemblBacteria; CDM39702; CDM39702; BN5_1100.
DR   KEGG; ppse:BN5_1100; -.
DR   KO; K01595; -.
DR   Proteomes; UP000032841; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032841};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CDM39702.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CDM39702.1}.
FT   ACT_SITE    140    140       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    545    545       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   878 AA;  97343 MW;  66398DBD76BDADE6 CRC64;
     MAEIDARLRE EVHLLGELLG HTISTQLGDE FLDKIERIRK SAKAGRRGSA AGAEQLTSTL
     GDLGDDELLP VARAFNQFLN LANIAEQQHR VRRRRAGEPE PFELRVLDEL LERLLAAGQG
     SDDLARQLGR LDIELVLTAH PTEVARRTLI QKYDAIAAQL TALDHSDLSP SERERIVERL
     QRLIAEAWHT EEIRRSRPSP VDEAKWGFAV IEHSLWQAVP QFLRRADQSL QAATGLRLPL
     EAAPIRFASW MGGDRDGNPN VTARVTREVL LLARWMAADL YLRDVDNLAA ELSMQQASDE
     LRAQVGDSAE PYRALLKQLR ERLRETRSWA QQALTADVAP STAVLCDNHE LLAPLQLCYQ
     SLHACGMGVI ADGPLLDCLR RAATFGLFLV RLDVRQDSSR HAAAMSEITD YLGLGRYVEW
     DEEARLSFLQ RELDNRRPLL PNDYRPSADT AEVLATCREV AAAPAASLGS YVISMAGAAS
     DVLAVQLLLK EAGLRRPMRV VPLFETLADL DHAGPVIDRL LGLPGYRARL HGPQEVMIGY
     SDSAKDAGTT AAAWAQYRAQ EELVRLCREH QVELLLFHGR GGTVGRGGGP AHAAILSQPP
     GSVAGRFRTT EQGEMIRFKF GLPDIAVQNL NLYLAAVLEA TLLPPPVPEP SWRAMMDRLA
     DVGVKAYRGV VREHPQFVEY FRQATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
     QTRLMLPAWL GWEQALGQAL QGGDADLLKS MREQWPFFRT RIDMLEMVLT KADANIAALY
     DQRLVEPALQ PLGAQLRDLL SQACAAVLEL TGQSRLLAHN PETLESISVR NTYLDPLHLL
     QVELLARCRQ RQQAPESPLE QALLVSVAGI AAGLRNTG
//
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