ID F2CTV3_HORVV Unreviewed; 496 AA.
AC F2CTV3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 80.
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|EMBL:BAJ86274.1};
RN [1] {ECO:0000313|EMBL:BAJ86274.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Shoot {ECO:0000313|EMBL:BAJ86274.1};
RX PubMed=21415278; DOI=10.1104/pp.110.171579;
RA Matsumoto T., Tanaka T., Sakai H., Amano N., Kanamori H., Kurita K.,
RA Kikuta A., Kamiya K., Yamamoto M., Ikawa H., Fujii N., Hori K., Itoh T.,
RA Sato K.;
RT "Comprehensive sequence analysis of 24,783 barley full-length cDNAs derived
RT from 12 clone libraries.";
RL Plant Physiol. 156:20-28(2011).
RN [2] {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 [3] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0393690.1}
RP IDENTIFICATION.
RC STRAIN=subsp. vulgare
RC {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.4HG0393690.1};
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 EMBL; AK355055; BAJ86274.1; -; mRNA.
DR AlphaFoldDB; F2CTV3; -.
DR SMR; F2CTV3; -.
DR PaxDb; 4513-MLOC_63275-3; -.
DR EnsemblPlants; HORVU.MOREX.r3.4HG0393690.1; HORVU.MOREX.r3.4HG0393690.1; HORVU.MOREX.r3.4HG0393690.
DR Gramene; HORVU.MOREX.r2.4HG0327490.1; HORVU.MOREX.r2.4HG0327490.1; HORVU.MOREX.r2.4HG0327490.
DR Gramene; HORVU.MOREX.r2.4HG0327490.1.mrna1; HORVU.MOREX.r2.4HG0327490.1.mrna1; HORVU.MOREX.r2.4HG0327490.1.
DR Gramene; HORVU.MOREX.r3.4HG0393690.1; HORVU.MOREX.r3.4HG0393690.1; HORVU.MOREX.r3.4HG0393690.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_019582_2_2_1; -.
DR OMA; HHELANS; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000011116; Chromosome 4H.
DR ExpressionAtlas; F2CTV3; baseline and differential.
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 CDD; cd06450; DOPA_deC_like; 1.
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:SF35; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 2: Evidence at transcript level;
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 496 AA; 56104 MW; B34A5013733F87FF CRC64;
MVLSRAASDT DVSVHSTFAS RYVRSSLPRY RMPENSIPKE AAYQIINDEL MLDGNPRLNL
ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFHA PLGESETAVG
VGTVGSSEAI MLAGLAFKRR WQNKRKAEGK PFDKPNIITG ANVQVCWEKF ARYFEVELKE
VKLREGYYVM DPEQAVEMVD ENTICVAAIL GSTLNGEFED VKRINDLLED KNKQTGWETP
IHVDAASGGF IAPFLYPELE WDFRLPWVKS INVSGHKYGL VYPGIGWCVW RSKEDLPDEL
IFHINYLGTD QPTFTLNFSK GSSQVIAQYY QLIRHGFEGY RNIMENCQEN AMVVKEGLEK
TGRFNIVSKD EGVPLVAFSL KDHSRHDEFE ISDMLRRFGW IVPAYTMPAD AQHVTVLRVV
IREEFSRTLA ERLVIDIDTV MAQLDVLPSK LTPPALGLLP ATLPKTVAKK TELETQKSVA
AAWKEFVLAK KTNGVC
//
