ID   Q6Q2Z9_SOYBN            Unreviewed;      1032 AA.
AC   Q6Q2Z9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   Name=PEPC17 {ECO:0000313|EMBL:AAS67005.1};
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 {ECO:0000313|EMBL:AAS67005.1};
RN   [1] {ECO:0000313|EMBL:AAS67005.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15299132; DOI=10.1104/pp.104.042762;
RA   Sullivan S., Jenkins G.I., Nimmo H.G.;
RT   "Roots, cycles and leaves. Expression of the phosphoenolpyruvate
RT   carboxylase kinase gene family in soybean.";
RL   Plant Physiol. 135:2078-2087(2004).
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         Evidence={ECO:0000256|ARBA:ARBA00001071};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; AY563043; AAS67005.1; -; mRNA.
DR   RefSeq; NP_001237378.1; NM_001250449.1.
DR   AlphaFoldDB; Q6Q2Z9; -.
DR   GeneID; 547755; -.
DR   KEGG; gmx:547755; -.
DR   OrthoDB; 355614at2759; -.
DR   ExpressionAtlas; Q6Q2Z9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
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:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
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   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAS67005.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyruvate {ECO:0000313|EMBL:AAS67005.1}.
FT   REGION          356..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1032 AA;  115764 MW;  24F41F8E919C8E84 CRC64;
     MTDITGDIAE EISFQSFDDD CRLLGNLLND ILQREVGTNL LDKIERTRVL AQSGCNMRQA
     GIVNMAEMLE KQLASELSKM TLEEAFTLAR AFSHYLTLMG IAETHHRVRK GGNMAQIAKS
     CDDIFNQLVQ GGVPPEELYD TVCKREVEIV LTAHPTQINR RTLQFKHIRI AHLLDYNDRP
     DLSTEDREMV IEDLVREITS IWQTDELRRQ KPTPVDEARA GFNIVEQSLW KAVPHYLRRV
     SNALKKHTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT KDVSLLSRWM AIDLYIREVD
     SLRFELSMNQ CSDRLSRLAH EILEAKHENR RENWNQSANR SLTLPTQLPA RAHLPSIAEN
     GESRHPRLDI PAPDYMQSNH KDGGVSVSST TSKLANPNTR LPGTSSANSS ASSAALGQKK
     LYAESQTGKS TFQKLLEPML PQLPGIAPYR IVLGNVKDKL EKSRRRLEIL LEDVACDYDP
     LDYYETSDQL LEPLLLCYES LQSCGSGVLA DGRLADLIRR VATFGMVLMK LDLRQESGRH
     AEALDAITQY LDMGTYSEWD EEKKLDFLTR ELKGKRPLVP VSIEVHPDVK EVLDTFRIAA
     ELGSDSLGAY VISMASNASD VLAVELLQKD ARLAAIGELG KACPGGTLRV VPLFETVKDL
     RGAGSVIRKL LSIDWYHEHI VKNHNGHQEV MVGYSDSGKD AGRFTAAWEL YKAQEDVVAA
     CNDYGIKVTL FHGRGGSIGR GGGPTYLAIQ SQPPGSVMGT LRSTEQGEMV EAKFGLPQIA
     VRQLEIYTTA VLLATLRPPI PPREEKWRNV MEEISNISCQ CDRNVVYENP EFLAYFHEAT
     PEAELGFLNI GSRPTRRKSS VGIGHLRAIP WLFAWTQTRF VLPAWLGVGA GLKGACEKGY
     TEELKAMYKE WPFFQSTIDL IEMVLGKADI PIAKHYDEVL VTKERQELGH ELRSELMTAE
     KFVMVISGHE KLQQNNRSLR RLIENRLPFL NPLNMLQVEI LKRLRRDDDN RKIRDALLIT
     INGIAAGMKN TG
//