CAPP_PSEA7
ID CAPP_PSEA7 Reviewed; 878 AA.
AC A6V1A0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=PSPA7_1451;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000255|HAMAP-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. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
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DR EMBL; CP000744; ABR84834.1; -; Genomic_DNA.
DR RefSeq; WP_012074668.1; NC_009656.1.
DR AlphaFoldDB; A6V1A0; -.
DR SMR; A6V1A0; -.
DR EnsemblBacteria; ABR84834; ABR84834; PSPA7_1451.
DR KEGG; pap:PSPA7_1451; -.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000001582; 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; Lyase; Magnesium.
FT CHAIN 1..878
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025575"
FT ACT_SITE 140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 545
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 878 AA; 97731 MW; C41DD18AC146E0F3 CRC64;
MPEIDARLRE DVHQLGELLG DTIREQYGPA FLDKIERIRK GAKAARRGSA EGAQQLTATL
DGLEESELLP VARAFNQFLN LANIAEQYHR IRRRRPNEPE PFENLALEEL LGRLKDAGHA
PGQLARQLAG LEIELVLTAH PTEVARRTLI QKYDAITAQL ATKDHADLLP EERSRIQRRL
QRLVAEVWHT DEIRKVRPTP VDEAKWGFAV IEHSLWEALP NVLRHVDEVL LRSTGERLPL
SAAPLRFASW MGGDRDGNPN VTAGVTREVL LLARWMAADL YLRDIDRLAA ELSMQEASPA
LLARVGDSAE PYRALLKQLR ERLRLTRSWT HQALAGEVPA AEGVLEHNRD LVEPLQLCHE
SLHACGMGVI ADGALLDCLR RAATFGLFLV RLDVRQDAGR HAAALSEITE YLELGSYAEW
DEKTRLEFLL EELNSRRPLL PAHYQPSAET AEVLATCRAI AAAPPASLGS YVISMAGQPS
DVLAVQLLLK ESGVDWPMRV VPLFETLDDL DNAGPCMERL LTLPGYRSRL SGVQEVMIGY
SDSAKDAGTL TAAWAQYRAQ EKLVEICRHH EVELLLFHGR GGTVGRGGGP AHAAILSQPP
GSVAGRFRVT EQGEMIRFKF GLPDIAEQNL NLYLAAVLEA TLMPPPAPEP AWRAQMDRLA
KDALHAYRRV VRDDPQFVEY FRLATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
QTRLMLPAWL GWETALLNAI ERGEGALLGQ MRERWPFFTT RIDMLEMVLA KADADIARLY
DERLVPLELR PLGRRLRDLL SQAVRVVLGL TGQSLLLAHA SETRESISVR NSYLDPLHLL
QAELLARSRR CRGDACGGLE QALLVTVAGI AAGLRNTG