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Database: UniProt
Entry: A0A287IK43_HORVV
LinkDB: A0A287IK43_HORVV
Original site: A0A287IK43_HORVV 
ID   A0A287IK43_HORVV        Unreviewed;       499 AA.
AC   A0A287IK43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509 {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0171750.1, ECO:0000313|Proteomes:UP000011116};
RN   [1] {ECO:0000313|Proteomes:UP000011116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   The International Barley Genome Sequencing Consortium;
RA   Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA   Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
RN   [2] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0171750.1}
RP   IDENTIFICATION.
RC   STRAIN=subsp. vulgare
RC   {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.2HG0171750.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2022) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|RuleBase:RU361171};
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   AlphaFoldDB; A0A287IK43; -.
DR   PaxDb; 4513-MLOC_73968-2; -.
DR   EnsemblPlants; HORVU.MOREX.r3.2HG0171750.1; HORVU.MOREX.r3.2HG0171750.1; HORVU.MOREX.r3.2HG0171750.
DR   Gramene; HORVU.MOREX.r2.2HG0141870.1; HORVU.MOREX.r2.2HG0141870.1; HORVU.MOREX.r2.2HG0141870.
DR   Gramene; HORVU.MOREX.r3.2HG0171750.1; HORVU.MOREX.r3.2HG0171750.1; HORVU.MOREX.r3.2HG0171750.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000011116; Chromosome 2H.
DR   ExpressionAtlas; A0A287IK43; baseline.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF13; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
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:UP000011116}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   499 AA;  55731 MW;  E5DF85EFEBA999B7 CRC64;
     MVLTHVQSDE AAASAAVFAS RYVQEPVPSY ELGEKSISKD AAYQIIHDEL LLDGSPRLNL
     ASFVTTWMEP ECDRLILEGM NKNYADMDEY PVTTELQNRC VNIIARLFNA PVGTGETAVG
     VGTVGSSEAI MLAGLAFKRR WQNRRKAEGK PHDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSEGCYVM DPDKAVEMVD ENTICVAAIL GSTLTGEFED VKRLNDLLVA KNKQTRWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYPGVGWVIW RNREDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQIIAQYY QFLRLGFEGY KNVMENCVES ARTLREGLLR
     TGRFDVISKE DGVPLVAFTF RGIRDGSPAF KLSANLRRFG WIVPAYTMPA NLEHMTVLRV
     VVREDFGRPL AERFLSHVRM ALSELDLAAK GPVPKMRLTI ELGPARSAEE EASVRVVKRE
     AVSGHRSVSL VSGKTKGVC
//
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