ID I1LCU6_SOYBN Unreviewed; 1032 AA.
AC I1LCU6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=GLYMA_10G205500 {ECO:0000313|EMBL:KRH34779.1};
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:KRH34779.1};
RN [1] {ECO:0000313|EMBL:KRH34779.1, ECO:0000313|EnsemblPlants:KRH34779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH34779};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH34779.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH34779}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH34779};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH34779.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH34779.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000843; KRH34779.1; -; Genomic_DNA.
DR AlphaFoldDB; I1LCU6; -.
DR SMR; I1LCU6; -.
DR STRING; 3847.I1LCU6; -.
DR PaxDb; 3847-GLYMA10G34970-1; -.
DR EnsemblPlants; KRH34779; KRH34779; GLYMA_10G205500.
DR Gramene; KRH34779; KRH34779; GLYMA_10G205500.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; I1LCU6; -.
DR OMA; KHIRISH; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000008827; Chromosome 10.
DR ExpressionAtlas; I1LCU6; baseline and differential.
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: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 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
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; 115843 MW; CA83AAADCBC07EA2 CRC64;
MTDITDDIAE EISFQSFDDD CRLLGNLLND ILQREVGTNL LDKIERTRVL AQSGCNMRQA
GIVNMAEMLE KQLASELSKM TLEEAFTLAR AFSHYLTLMG IAETHHRVRK GGNMAQIAKS
CDDIFNQLVQ GGVPPEELYD TVCKQEVEIV 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 IKNHNGHQEV MVGYSDSGKD AGRFTAAWEL YKAQEDVVAA
CNDYGIKVTL FHGRGGSIGR GGGPTYLAIQ SQPPGSVMGT LRSTEQGEMV EAKFGLPQIA
VRQLEIYTTA VLLATLRPPI PPREEKWRNV MEEISNISCQ CYRNVVYENP EFLAYFHEAT
PEAELGFLNI GSRPTRRKSS VGIGHLRAIP WLFAWTQTRF VLPAWLGVGA GLKGACEKGY
TEELKAMYKE WPFFQSTIDL IEMVLGKADI PIAKHYDEVL VSKERQELGH ELRSELMTAE
KFVMVISGHE KLQQNNRSLR RLIENRLPFL NPLNMLQVEI LKRLRRDDDN RKIRDALLIT
INGIAAGMKN TG
//
