ID   CAPP1_SOYBN             Reviewed;         967 AA.
AC   Q02909;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Phosphoenolpyruvate carboxylase, housekeeping isozyme;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
DE   AltName: Full=PEPC 1;
GN   Name=PPC16;
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].
RX   PubMed=1450389; DOI=10.1007/bf00046459;
RA   Sugimoto T., Kawasaki T., Kato T., Whittier R.F., Shibata D., Kawamura Y.;
RT   "cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene
RT   from soybean.";
RL   Plant Mol. Biol. 20:743-747(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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; D10717; BAA01560.1; -; mRNA.
DR   PIR; JW0072; JW0072.
DR   PIR; S28428; S28428.
DR   RefSeq; NP_001237602.1; NM_001250673.1.
DR   AlphaFoldDB; Q02909; -.
DR   SMR; Q02909; -.
DR   STRING; 3847.GLYMA20G09810.1; -.
DR   PRIDE; Q02909; -.
DR   ProMEX; Q02909; -.
DR   EnsemblPlants; KRH26228; KRH26228; GLYMA_12G161300.
DR   GeneID; 547769; -.
DR   Gramene; KRH26228; KRH26228; GLYMA_12G161300.
DR   KEGG; gmx:547769; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   InParanoid; Q02909; -.
DR   OMA; YMEAKPA; -.
DR   OrthoDB; 775417at2759; -.
DR   Proteomes; UP000008827; Chromosome 12.
DR   Genevisible; Q02909; 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, housekeeping
FT                   isozyme"
FT                   /id="PRO_0000166680"
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;  110686 MW;  CBD9247121A44A22 CRC64;
     MANRNLEKMA SIDAQLRLLV PAKVSEDDKL VEYDALLLDR FLDILQDLHG EDLKETVQEV
     YELSAEYEGK HDPKKLEELG NLITSLDAGD SIVVAKSFSH MLNLANLAEE VQIAHSRRNK
     LKKGDFADEN NATTESDIEE TLKKLVVDMK KSPQEVFDAL KNQTVDLVLT AHPTQSVRRS
     LLQKHGRIRN NLTQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
     SYFHETIWKG VPTFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
     DVCLLARMMA ANLYYSQIED LMFELSMWRC NDELRVRADE LNRSSKKNSV AKHYIEFWKA
     IPPNEPYRVL LGEVRNRLYQ TRERSRHLLA HGYSDIPEEE TFTNVEEFLE PLELCYRSLC
     ACGDRAIADG SLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITKHLE IGSYQEWSEE
     KRQQWLLSEL SGKRPLFGPD LPQTEEIRDV LETFHVIAEL PLDNFGAYII SMATAPSDVL
     AVELLQRECH VKHPLRVVPL FEKLADLEAA PAALARLFSV DWYRNRINGK QEVMIGYSDS
     GKDAGRFSAA WQLYKAQEEL IMVAKQYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPETI
     HGSLRVTVQG EVIEQSFGEQ HLCFRTLQRF TAATLEHGMH PPISPKPEWR ALMDEMAVIA
     TEEYRSIVFK EPRFVEYFRL ATPELEYGRM NIGSRPAKRR PSGGIETLRA IPWIFAWTQT
     RFHLPVWLGF GAAFKHVIEK DVRNIHVLQE MYNQWPFFRV TIDLVEMVFA KGDPGIAALY
     DRLLVSEDLW SFGEQLRTMY EETKELLLQV AGHRDLLEGD PYLKQRLRLR DSYITTLNVC
     QAYTLKRIRD PNYNVKLRPH ISKESIEISK PADELITLNP TSEYAPGLED TLILTMKGIA
     AGLQNTG