ID CAPP2_SOYBN Reviewed; 967 AA.
AC P51061;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=PPC1;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Enrei;
RX PubMed=8022928; DOI=10.1104/pp.103.3.1025;
RA Vazquez-Tello A.V., Whittier R.F., Kawasaki T., Sugimoto T., Kawamura Y.,
RA Shibata D.;
RT "Sequence of a soybean (Glycine max L.) phosphoenolpyruvate carboxylase
RT cDNA.";
RL Plant Physiol. 103:1025-1026(1993).
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; D13998; BAA03100.1; -; mRNA.
DR RefSeq; NP_001241357.1; NM_001254428.1.
DR RefSeq; XP_006591889.1; XM_006591826.2.
DR RefSeq; XP_006591890.1; XM_006591827.2.
DR AlphaFoldDB; P51061; -.
DR SMR; P51061; -.
DR STRING; 3847.P51061; -.
DR PaxDb; 3847-GLYMA12G35840-1; -.
DR ProMEX; P51061; -.
DR EnsemblPlants; KRH27344; KRH27344; GLYMA_12G229400.
DR EnsemblPlants; KRH27345; KRH27345; GLYMA_12G229400.
DR EnsemblPlants; KRH27346; KRH27346; GLYMA_12G229400.
DR GeneID; 100805069; -.
DR Gramene; KRH27344; KRH27344; GLYMA_12G229400.
DR Gramene; KRH27345; KRH27345; GLYMA_12G229400.
DR Gramene; KRH27346; KRH27346; GLYMA_12G229400.
DR KEGG; gmx:100805069; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; P51061; -.
DR OMA; KDLWPFG; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000008827; Chromosome 12.
DR Genevisible; P51061; GM.
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:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 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"
FT /id="PRO_0000166681"
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 967 AA; 110761 MW; 2460434DFAD522A7 CRC64;
MATRNLEKMA SIDAQLRQLA PAKVSEDDKL IEYDALLLDR FLDILQDLHG EDLKETVQEV
YELSAEYEGK HDPKKLEELG NLITSLDAGD SILVAKSFSH MLNLANLAEE VQISRRRRNK
LKKGDFADEN NATTESDIEE TLKKLVFDLK KSPQEVFDAL KNQTVDLVLT AHPTQSIRRS
LLQKHGRIRN CLSQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWNG VPRFLRRVDT ALNNIGIKER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANLYYSQIED LMFELSMWRC NDELRVRAEE LHRSSKKDEV AKHYIEFWKK
VPPNEPYRVV LGEVRDRLYQ TRERSRHLLS NGYSDIPEEA TFTNVEEFLE SLELCYRSLC
ACGDRAIADG SLLDFMRQVS TFGLSLVRLD IRQESDRHTD VLDAITKHLE IGSYQEWSEE
KRQEWLLSEL SGKRPLFGPD LPQTEEIRDV LDTFHVIAEL PPDNFGAYII SMATAPSDVL
AVELLQRECH IKHPLRVVPL FEKLADLEAA PAALARLFSI DWYRNRINGK QEVMIGYSDS
GKDAGRFSAA WQLYKAQEEL INVAKKFGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
HGSLRVTVQG EVIEQSFGEQ HLCFRTLQRF TAATLEHGMH PPISPKPEWR ALMDQMAVIA
TEEYRSIVFK EPRFVEYFRL ATPELEYGRM NIGSRPAKRR PSGGIETLRA IPWIFAWTQT
RFHLPVWLGF GAAFKKVIEE NVKNLNMLQE MYNQWPFFRV TLDLVEMVFA KGDPKIAALN
DRLLVSKDLW PFGDQLRNKY EETRKLLLQV AGHKEILEGD PYLKQRLRLR HAPITTLNIV
QAYTLKRIRD PNYNVKVRPR ISKESAEASK SADELVKLNP TSEYAPGLED TLILTMKGIA
AGMQNTG
//
