ID   CAPP_PHAVU              Reviewed;         968 AA.
AC   Q9AU12;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Blanco L.L., Lara F.M.;
RT   "Sequence of a nodule enhanced French bean (Phaseolus vulgaris) cDNA.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AF288382; AAK28444.1; -; mRNA.
DR   AlphaFoldDB; Q9AU12; -.
DR   SMR; Q9AU12; -.
DR   STRING; 3885.XP_007149391.1; -.
DR   PRIDE; Q9AU12; -.
DR   ProMEX; Q9AU12; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   PhylomeDB; Q9AU12; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; 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   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   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Phosphoprotein; Photosynthesis.
FT   CHAIN           1..968
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166672"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   968 AA;  110709 MW;  EA4FD233852BF9FB CRC64;
     MANRNLEKMA SIDAQLRQLA PSKVSEDDKL IEYDALLLDR FLDILQNLHG EDLKETVQEV
     YELSAEYEGK HDPKKLEELG NVITSLDAGD SIVVAKSFSH MLNLANLAEE VQISRRRRNK
     LKKGDFADEN NATTESDIEE TLKKLVFELK KSPQEVFDAL KNQTVDLVLT AHPTQSVRRS
     LLQKHARIRN CLSKLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
     SYFHETIWNG VPSFLRRVDT ALNNIGIKER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANMYYSQIED LMFELSMWRC NDELRVHADE VHRSSNKDEV AKHYIEFWKK
     VPTNEPYRVV LGEVRDRLYQ TRERSRHLLS NGYSDIPEEN TFTSVEEFLQ PLELCYRSLC
     ACGDRAIADG SLLDFLRQVS TFGLSIVRLD IRQESDRHTD VLDAITKHLE IGSYQEWSEE
     KRQEWLLSEL SGKRPLFGPD LPQTEEIRDV LDTFHVIAEL PPDNFGAYII SMATAPSDVL
     AVELLQRECH VKHPLRVVPL FEKLADLEAA PAALARLFSV DWYKNRIDGK QEVMIGYSDS
     GKDAGRFSAA WQLYKAQEEL VKVAKKFGIK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
     HGSLRVTVQG EVIEQCFGEQ HLCFRTLQRF TAATLEHGMN PPISPKPEWR AMMDQMAVIA
     TEEYRSIVFK EPRFVEYFRL ATPELEYGRM NIGSRPAKRR PSGGIETLRA IPWIFAWTQT
     RFHLPVWLGF GAAFKQVLDK NAKKNLSMLQ EMYNQWPFFR VTLDLVEMVF AKGDPKIGAL
     NDRLLVSKDL WPFGDQLRNK YEETKKLLLQ VAGHKEILEG DPYLKQRLRL RHSPITTLNV
     FQAYTLKRIR DPNYKVKARP RISKESAEAS KSADELIKLN PTSEYAPGLE DTLILTMKGI
     AAGMQNTG