ID I1KRN2_SOYBN Unreviewed; 471 AA.
AC I1KRN2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
GN ORFNames=GLYMA_08G091300 {ECO:0000313|EMBL:KRH42466.1};
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:KRH42466.1};
RN [1] {ECO:0000313|EMBL:KRH42466.1, ECO:0000313|EnsemblPlants:KRH42466}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH42466};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42466.1};
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:KRH42466}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH42466};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH42466.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42466.1};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CM000841; KRH42466.1; -; Genomic_DNA.
DR AlphaFoldDB; I1KRN2; -.
DR SMR; I1KRN2; -.
DR STRING; 3847.I1KRN2; -.
DR PaxDb; 3847-GLYMA08G09650-1; -.
DR EnsemblPlants; KRH42466; KRH42466; GLYMA_08G091300.
DR Gramene; KRH42466; KRH42466; GLYMA_08G091300.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_2_1; -.
DR InParanoid; I1KRN2; -.
DR Proteomes; UP000008827; Chromosome 8.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR Gene3D; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010107; Glutamate_decarboxylase.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF41; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 471 AA; 53622 MW; A42EA2C27E3B081B CRC64;
MVFPRPPSES DLFLHSNFAS RYARDSLPRF SMPEDSMPKE AAYQNIHDEL QLDAIPKLNL
ASFVTTSMEE ECNKLIMESI NKNYVDMDEY PITTDLHNRC LNMIARMFHA EIGENENAIG
AGTVGSSEAI MLAGLAFKKK WQNKRKAEGK PYDKPNLVTG SNVQVCWEKF ARYFEVELRE
VEVREGYYVM DPAKAVELVD ENTICVAAIL GSTYNGEFED VKLLNDLLLE KNKQTGARMG
FQTPMVKSIN VSGHKYGLVY AGIGWVIWRT KDDLPEDLVF HINYLGADQP TFTLNFSKGS
SQIIAQYYQL IRLGQEGYRN IMENCRENAM VLKEDLEKSG HFNILSKDDG VPVVAFSLKD
RSRYDEFKIS EMLRRHGWIV PAYPMPPAAQ HINVLRVVIR AEFSRTLAER LVLDIHSVLD
ELEKVHPSKV TKNTKEENKL LVENGVKNTA LDAHSEIIAQ ESNKRQKIMV A
//
