ID   CAPP_SOLTU              Reviewed;         965 AA.
AC   P29196; Q43841;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=PPC1; Synonyms=PPC;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8251640; DOI=10.1007/bf00021542;
RA   Merkelbach S., Gehlen J., Denecke M., Hirsch H.-J., Kreuzaler F.;
RT   "Cloning, sequence analysis and expression of a cDNA encoding active
RT   phosphoenolpyruvate carboxylase of the C3 plant Solanum tuberosum.";
RL   Plant Mol. Biol. 23:881-888(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Merkelbach S.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RA   Panstruga R., Seiler A., Hirsch H.-J., Kreuzaler F.;
RT   "Genomic structure of a phosphoenolpyruvate carboxylase gene from potato
RT   (Solanum tuberosum).";
RL   (er) Plant Gene Register PGR95-086(1995).
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   -!- PATHWAY: Photosynthesis; C3 acid pathway.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; X67053; CAA47437.1; -; mRNA.
DR   EMBL; X90982; CAA62469.1; -; Genomic_DNA.
DR   PIR; S40304; S40304.
DR   RefSeq; NP_001274942.1; NM_001288013.1.
DR   AlphaFoldDB; P29196; -.
DR   SMR; P29196; -.
DR   STRING; 4113.PGSC0003DMT400039809; -.
DR   PRIDE; P29196; -.
DR   GeneID; 102603323; -.
DR   KEGG; sot:102603323; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   InParanoid; P29196; -.
DR   OrthoDB; 775417at2759; -.
DR   UniPathway; UPA00321; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P29196; baseline and differential.
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:0048366; P:leaf development; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..965
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166679"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        7
FT                   /note="D -> E (in Ref. 3; CAA62469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   965 AA;  110313 MW;  4DD364013EA5374B CRC64;
     MTTRNLDKLA SIDAQLRQLV PAKVSEDDKL VEYDALLLDR FLDILQDLHG EDLKETVQEC
     YELSAEYEAK HDPKKLEELG NVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRQK
     LKKKGDFGDE SNATTESDIE ETFKKLVGDL KKSPQEVFDA IKNQTVDLVL TAHPTQSVRR
     SLLQKHGRIR DCLAQLYAKD ITPDDKQELD EALQREIQAA FRTDEIRRTP PTPQDEMRAG
     MSYFHETIWK GVPKFLRRVD TALKNIGINE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT
     RDVCLLARMM AANLYYSQIE DLMFELSMWR CNEELRVRAD DLQRSSRRDE KHYIEFWKQV
     PPNEPYRVIL GDVRDKLYQT RERARQLLGH GYSEIPEEAT YTNIEQFLEP LELCYRSLCA
     CGDLSIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV LDAITQHLEI GSYRDWSEER
     RQEWLLSELS GKRPLFGPDL PKTEEIADVL DTFHVIAELP ADCFGAYIIS MATAPSDVLA
     VELLQRECRV RQPLRVVPLF EKLADLDAAP AAVARLFSIE WYRNRINGKQ EVMIGYSDSG
     KDAGRLSAAW QLYKAQEELI QVAKEFDVKL TMFHGRGGTV GRGGGPAHLA ILSQPPETIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMHP PVSPKPEWRA LMDEIAVVAT
     EKYRSIVFKE PRFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR
     FHLPVWLGFG AAFKYAIEKD IKNLRMLQEM YNAWPFFRVT IDLVEMVFAK GDPGIAALFD
     KLLVSEDLWS FGELLRSKYE ETKSLLLQIA GHKDLLEGDP YLKQRLRLRD SYITTLNVCQ
     AYTLKRIRDP DYSVTPRPHI SKEYMEAKPA TELVNLNPTS EYAPGLEDTL ILTMKGIAAG
     MQNTG