ID   CAPP2_MAIZE             Reviewed;         967 AA.
AC   P51059;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 125.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 2;
DE            Short=PEPC 2;
DE            Short=PEPCase 2;
DE            EC=4.1.1.31;
GN   Name=PEP4; Synonyms=PEP;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. H84; TISSUE=Root;
RX   PubMed=1429504; DOI=10.1093/oxfordjournals.jbchem.a123855;
RA   Kawamura T., Shigesada K., Toh H., Okumura S., Yanagisawa S., Izui K.;
RT   "Molecular evolution of phosphoenolpyruvate carboxylase for C4
RT   photosynthesis in maize: comparison of its cDNA sequence with a newly
RT   isolated cDNA encoding an isozyme involved in the anaplerotic function.";
RL   J. Biochem. 112:147-154(1992).
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. {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; X61489; CAA43709.1; -; mRNA.
DR   PIR; JH0667; JH0667.
DR   RefSeq; NP_001105438.1; NM_001111968.1.
DR   AlphaFoldDB; P51059; -.
DR   SMR; P51059; -.
DR   STRING; 4577.P51059; -.
DR   PaxDb; 4577-GRMZM2G473001_P01; -.
DR   GeneID; 542393; -.
DR   KEGG; zma:542393; -.
DR   MaizeGDB; 30066; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   InParanoid; P51059; -.
DR   OrthoDB; 355614at2759; -.
DR   SABIO-RK; P51059; -.
DR   UniPathway; UPA00321; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P51059; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF22; PHOSPHOENOLPYRUVATE CARBOXYLASE 2; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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..967
FT                   /note="Phosphoenolpyruvate carboxylase 2"
FT                   /id="PRO_0000166668"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000250"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   967 AA;  109999 MW;  7034A2AD5521645B CRC64;
     MAALGPKMER LSSIDAQLRM LVPGKVSEDD KLIEYDALLL DRFLDILQDL HGDDLKEMVQ
     ECYEVAAEYE TKHDLQKLDE LGKMITSLDP GDSIVIAKSL SHMLNLANLA EEVQIAYRRR
     IKLKKGDFAD ENSAITESDI EETLKRLVVD LKKSPAEVFD ALKSQTVDLV LTAHPTQSVR
     RSLLQKHSRI RNCLVQLYSK DITPDDKQEL DEALQREIQA AFRTDEIRRT QPTPQDEMRA
     GMSYFHETIW KGVPKFLRRV DTALKNIGIN ERVPYNAPLI QFSSWMGGDR DGNPRVTPEV
     TRDVCLLARM MASNLYCSQI EDLMFELSMW RCSDELRMRA DVLHLSTKKD AKHYIEFWKK
     VPPNEPYRVI LSDVRDKLYN TRERSRELLS SGHSDIPEEA TLTNVEQLLE PLELCYRSLC
     ACGDSVIADG TLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTYLG IGSYREWTEE
     RRQEWLLSEL NGKRPLFGSD LPKTEEISDV LDTFHVIAEL PSDNFGAYII SMATAPSDVL
     AVELLQRECH VKTPLRVVPL FEKLADLEAA PAALARLFSI DWYRQRINGK QEVMIGYSDS
     GKDAGRLSAA WQLYKAQEEL IKVAKDFGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
     HGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMH PPNAPKPEWR ALLDEMAVVA
     TEEYRSIVFK EPRFVEYFRL ATPETEYGRM NIGSRPSKRK PSGGIDSLRA IPWIFAWTQT
     RFHLPVWLGF GAAFKNVLQK DIRNLHMLQE MYNEWPFFRV TIDLVEMVFA KGNPGIAALY
     DKLLVSEELH PLGEKLRANY EETQKLLLQV AGHRDLLEGD LYLKQRLRLR DAYITTLNVC
     QAYTLKRIRD PDYHVALRPH LSKEIMDSTK AAADVVKLNP GSEYAPGLED TLILTMKGIA
     AGLQNTG
//