ID   CAPP_MEDSA              Reviewed;         966 AA.
AC   Q02735;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=PEPC;
OS   Medicago sativa (Alfalfa).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1421147; DOI=10.1007/bf00040603;
RA   Pathirana S.M., Vance C.P., Miller S.S., Gantt J.S.;
RT   "Alfalfa root nodule phosphoenolpyruvate carboxylase: characterization of
RT   the cDNA and expression in effective and plant-controlled ineffective
RT   nodules.";
RL   Plant Mol. Biol. 20:437-450(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Saranac;
RA   Pathirana S.M., Gantt J.S.;
RL   Submitted (JAN-1996) 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   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; M83086; AAB46618.1; -; mRNA.
DR   EMBL; L39371; AAB41903.1; -; Genomic_DNA.
DR   PIR; S26235; S26235.
DR   AlphaFoldDB; Q02735; -.
DR   SMR; Q02735; -.
DR   PRIDE; Q02735; -.
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..966
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166669"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   966 AA;  110890 MW;  5828EA10C2C41DD7 CRC64;
     MANKMEKMAS IDAQLRQLVP AKVSEDDKLI EYDALLLDRF LDILQDLHGE DLKDSVQEVY
     ELSAEYERKH DPKKLEELGN LITSFDAGDS IVVAKSFSHM LNLANLAEEV QIAHRRRNKL
     KKGDFRDESN ATTESDIEET LKKLVFDMKK SPQEVFDALK NQTVDLVLTA HPTQSVRRSL
     LQKHGRVRNC LSQLYAKDIT PDDKQELDEA LQREIQAAFR TDEIKRTPPT PQDEMRAGMS
     YFHETIWKGV PKFLRRVDTA LKNIGINERV PYNAPLIQFS SWMGGDRDGN PRVTPEVTRD
     VCLLARMMAA NLYYSQIEDL MFELSMWRCN DELRVRAEEL HRNSKKDEVA KHYIEFWKKI
     PLNEPYRVVL GEVRDKLYRT RERSRYLLAH GYCEIPEEAT FTNVDEFLEP LELCYRSLCA
     CGDRAIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV MDAITKHLEI GSYQEWSEEK
     RQEWLLSELI GKRPLFGPDL PQTDEIRDVL DTFRVIAELP SDNFGAYIIS MATAPSDVLA
     VELLQRECKV RNPLRVVPLF EKLDDLESAP AALARLFSID WYINRIDGKQ EVMIGYSDSG
     KDAGRFSAAW QLYKAQEDLI KVAQKFGVKL TMFHGRGGTV GRGGGPTHLA ILSQPPETIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMRP PSSPKPEWRA LMDQMAVIAT
     EEYRSIVFKE PRFVEYFRLA TPEMEYGRMN IGSRPAKRRP SGGIETLRAI PWIFAWTQTR
     FHLPVWLGFG AAFRQVVQKD VKNLHMLQEM YNQWPFFRVT IDLVEMVFAK GDPGIAALND
     RLLVSKDLWP FGEQLRSKYE ETKKLLLQVA AHKEVLEGDP YLKQRLRLRD SYITTLNVFQ
     AYTLKRIRDP NYKVEVRPPI SKESAETSKP ADELVTLNPT SEYAPGLEDT LILTMKGIAA
     GMQNTG