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Database: UniProt/SWISS-PROT
Entry: CAPP_PSEAE
LinkDB: CAPP_PSEAE
Original site: CAPP_PSEAE 
ID   CAPP_PSEAE              Reviewed;         878 AA.
AC   Q9HXV3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-JUL-2017, entry version 95.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=PA3687;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00595}.
DR   EMBL; AE004091; AAG07075.1; -; Genomic_DNA.
DR   PIR; H83184; H83184.
DR   RefSeq; NP_252377.1; NC_002516.2.
DR   RefSeq; WP_003113850.1; NC_002516.2.
DR   ProteinModelPortal; Q9HXV3; -.
DR   SMR; Q9HXV3; -.
DR   STRING; 208964.PA3687; -.
DR   PaxDb; Q9HXV3; -.
DR   PRIDE; Q9HXV3; -.
DR   EnsemblBacteria; AAG07075; AAG07075; PA3687.
DR   GeneID; 879083; -.
DR   KEGG; pae:PA3687; -.
DR   PATRIC; fig|208964.12.peg.3856; -.
DR   PseudoCAP; PA3687; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   InParanoid; Q9HXV3; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   PhylomeDB; Q9HXV3; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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; Complete proteome; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN         1    878       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166613.
FT   ACT_SITE    140    140       {ECO:0000255|HAMAP-Rule:MF_00595}.
FT   ACT_SITE    545    545       {ECO:0000255|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   878 AA;  97840 MW;  51D1309A70425BDA CRC64;
     MPEIDARLRE DVHQLGELLG DTIREQYGPR FLDKIELIRK GAKAARRGSA EGAQQLTATL
     DGLEEDELLP VARAFNQFLN LANIAEQYHR IRRRRPNEPE PFENLVLEEL LGRLKDAGHA
     PGQLARQLAG LEIELVLTAH PTEVARRTLI QKYDAITAQL AAKDHADLLP EERSRIQQRL
     QRLVAEAWHT DEIRKVRPTP VDEAKWGFAV IEHSLWQALP NVLRHVDEVL LRSTGERLPL
     TAAPLRFASW MGGDRDGNPN VTASVTREVL LLARWMAADL YLRDIDRLAA ELSMQQASPQ
     LLARVGDSAE PYRALLKQLR ERLRVTRNWT HQALAGEVPA AEGVLEHNRD LVEPLQLCHE
     SLHACGMGVI ADGALLDCLR RAATFGLFLV RLDVRQDSAR HAAALSEITE YLELGSYDEW
     DEKTRLEFLL EELNSRRPLL PAHYQPSADT AEVLATCRAI AAAPPASLGS YVISMAGQPS
     DVLAVQLLLK ESGVDWPMRV VPLFETLDDL DNAGPCMERL LTLPGYRSRL SGVQEVMIGY
     SDSAKDAGTL TAAWAQYRAQ EKLVEICRQH EVELLLFHGR GGTVGRGGGP AHAAILSQPP
     GSVAGRFRVT EQGEMIRFKF GLPDIAEQNL NLYLAAVLEA TLMPPPAPEP AWRAQMDRLA
     KDALLAYRRV VRDDPQFVEY FRLATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
     QTRLMLPAWL GWETALLNAI ERGEGALLGQ MREQWPFFTT RIDMLEMVLA KADADIARLY
     DERLVPLELR PLGRRLRDLL SQAVRVVLGL TGQSLLLAHA SETRESISVR NSYLDPLHLL
     QAELLARSRR CRGDACGGLE QALLVTVAGV AAGLRNTG
//
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