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CAPP2_SOYBN
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   03-AUG-2022, entry version 122.
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.GLYMA12G35840.1; -.
DR   PRIDE; P51061; -.
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; GPTHRFI; -.
DR   OrthoDB; 775417at2759; -.
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   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..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
 
 
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