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Database: UniProt/TrEMBL
Entry: C3KEC5_PSEFS
LinkDB: C3KEC5_PSEFS
Original site: C3KEC5_PSEFS 
ID   C3KEC5_PSEFS            Unreviewed;       875 AA.
AC   C3KEC5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   25-APR-2018, entry version 73.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CAY47497.1};
GN   OrderedLocusNames=PFLU_1239 {ECO:0000313|EMBL:CAY47497.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47497.1, ECO:0000313|Proteomes:UP000002332};
RN   [1] {ECO:0000313|EMBL:CAY47497.1, ECO:0000313|Proteomes:UP000002332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY47497.1,
RC   ECO:0000313|Proteomes:UP000002332};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; AM181176; CAY47497.1; -; Genomic_DNA.
DR   RefSeq; WP_012722566.1; NC_012660.1.
DR   STRING; 216595.PFLU1239; -.
DR   EnsemblBacteria; CAY47497; CAY47497; PFLU_1239.
DR   KEGG; pfs:PFLU_1239; -.
DR   PATRIC; fig|216595.4.peg.1471; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; PFLU216595:G1G1K-1809-MONOMER; -.
DR   Proteomes; UP000002332; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002332};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:CAY47497.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:CAY47497.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002332}.
FT   COILED      163    183       {ECO:0000256|SAM:Coils}.
FT   COILED      759    779       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    137    137       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    542    542       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   875 AA;  97458 MW;  3822BFA055651D8A CRC64;
     MSDIDARLRE DVHLLGELLG NTIREQYGDA FLDKIEQIRK GAKADRRGAG DELSASLNQL
     QENELLPVAR AFNQFLNLAN IAEQYQLIHR RDESQPAPFE SRVLPELLAR LQSEGHSNES
     LARQLGRLEI ELVLTAHPTE VARRTLIQKY DAIAAQLALQ DHRDLTTAER EQIRQRLQRL
     IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWHAIPNYL RKADQALHAA TGLRLPLEAA
     PIRFASWMGG DRDGNPNVTA PVTREVLLLA RWMAADLYLR DIDHLASELS MQQASPALQA
     KVGDSVEPYR ALLKQLRERL RATRQWAHTA LSSSTPAPAE VLQNNRDLLE PLELCYQSLH
     ECGMGVIADG PLLDCLRRAV TFGLFLVRLD VRQDSSRHSA AMTEITDYLG LGRYEDWDEE
     ARISFLMKEL ANRRPLLPGY FKPSADTAEV LNTCKEVAAA PAASLGSYVI SMAGAASDVL
     AVQLLLKESG VQRPMRVVPL FETLADLDNA GPVIEQLLLL PGYRTRLQGP QEVMIGYSDS
     AKDAGTTAAA WAQYRAQERL VDICREQQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
     AGRFRTTEQG EMIRFKFGLP DIAEQNLNLY LAAVLEATLL PPPPPEPAWR HLMDELAADG
     VSAYRAVVRE NPQFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
     LMLPAWLGWE AALSKALERG EGELLGQMRE QWPFFRTRID MLEMVLAKAD ADIARLYDER
     LVQPDLLPLG THLRDLLSQA CSVVLGLTGQ SQLLAHSPDT LEFIRLRNTY LDPLHLLQAE
     LLARSRQQEA AQDSPLEQAL LVSVAGIAAG LRNTG
//
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