ID A0A1U8BHY5_NELNU Unreviewed; 495 AA.
AC A0A1U8BHY5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-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};
GN Name=LOC104611053 {ECO:0000313|RefSeq:XP_010276269.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010276269.1};
RN [1] {ECO:0000313|RefSeq:XP_010276269.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_010276269.1; XM_010277967.2.
DR AlphaFoldDB; A0A1U8BHY5; -.
DR STRING; 4432.A0A1U8BHY5; -.
DR GeneID; 104611053; -.
DR KEGG; nnu:104611053; -.
DR eggNOG; KOG1383; Eukaryota.
DR InParanoid; A0A1U8BHY5; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000189703; Unplaced.
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 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:SF3; 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:UP000189703}.
FT MOD_RES 277
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 495 AA; 56166 MW; BEB8C9A0054A2E0F CRC64;
MVLSKTTSES DVSVHSTFAS RYVRASLPRF KMPENSIPKE AAYQIINDEL MLDGNPRLNL
ASFVTTWMEP ECDKLIMSAI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDSETAVG
VGTVGSSEAI MLAGLAFKRR WQNKRKAQGK PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
VKLREGYYVM DPAKAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLAE KNKKTGWNTP
IHVDAASGGF IAPFIYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RTKEDLPEEL
IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY RNIMENCREN AMVLKEGLEK
TGRFNIVSKD NGIPLVAFSL KDNSRHNEFE VSDMLRRFGW IVPAYTMPAD AQHVTVLRVV
IREDFSRTLA ERLVLDIQKV LHDLETLPAK ISANCEEKKQ RNGTIFHKKS AIETQREITT
AWKKFVMDKK ISGVC
//
