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 27-MAR-2024, entry version 135.
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.Q02909; -.
DR PaxDb; 3847-GLYMA20G09810-1; -.
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; TRRDAKH; -.
DR OrthoDB; 355614at2759; -.
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 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, 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
//
