ID   CAPP_PEA                Reviewed;         967 AA.
AC   P51062;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
OS   Pisum sativum (Garden pea).
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; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sparkle; TISSUE=Root nodule;
RA   Suganuma N., Okada Y., Kanayama Y.;
RL   Submitted (SEP-1995) 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; D64037; BAA10902.1; -; mRNA.
DR   AlphaFoldDB; P51062; -.
DR   SMR; P51062; -.
DR   PRIDE; P51062; -.
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..967
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166673"
FT   REGION          915..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   967 AA;  111008 MW;  CA7E810C6A0D8567 CRC64;
     MANKMEKMAS IDAQLRQLAP AKVSEDDKLI EYDALLLDRF LDILQDLHGE DLKDSVQEVY
     ELSAEYERKH DPKKLEELGK LITGLDAGDS IVVAKSFSHM LNLANLAEEV QIAHRRRNKL
     KKGDFRDESN ATTESDIEET LKKLVFNMKK SPQEVFDALK NQTVDLVLTA HPTQSVRRSL
     LQKHARVRNC LSQLYAKDIT PDDKQELDES LQREIQAAFR TDEIKRTPPT PQDEMRAGMS
     YFHETIWKGV PKFLRRVDTA LKNIGINERV PYNAPLIQFS SWMGGDRDGN PRVTPEVTRD
     VCLLARMMAA NLYYSQIEDL MFELSMWRCN DELRDRAEEL HRNSKKDEVA KHYIEFWKKV
     PLNEPYRVIL GHVRDKLYRT RERSRYLLAH GYSDIPEEDT FTNFDEFLEP LELCYRSLCF
     CGDRAIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV MDAITKHLEI GSYQEWSEEK
     RQEWLLSELV GKRPLFGPDL PTTDEIRDVL DTFHVIAELP SDNFGAYIIS MATAPSDVLA
     VELLQRECKI KNPLRVVPLF EKLADLEAAP AALARLFSID WYRNRIDGKQ EVMIGYSDSG
     KDAGRFSAAW QLYKAQEELI NVAQKFSVKL TMFHGRGGTV GRGGGPTHLA ILSQPPDTIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMRP PSSPKPEWRA LMDQMAIIAT
     EEYRSIVFKE PRFVEYFRLA TPEMEYGRMN IGSRPAKRRP SGGIETLRAI PWIFPWTQTR
     FHLPVWLGFG SAFKQVIEKD VKNLHMLQDM YNQWPFFRVT IDLVEMVFAK GDPGIAALND
     RLLVSQNLWP FGEQLRNKYE ETKKLLLQVA THKEVLEGDP YLKQRLRLRD SYITTLNVFQ
     AYTLKRIRDP KSSVNASRLP LSRESPEATK PADELVTLNP TSEYAPGLED TLILTMKGIA
     AGMQNTG