ID   Q1I1D8_CITSI            Unreviewed;       494 AA.
AC   Q1I1D8;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:AAZ05070.1};
RN   [1] {ECO:0000313|EMBL:AAZ05070.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kanellis A.K., Pasentsis K.;
RT   "Cloning and characterization of Citrus sinensis flavedo glutamate
RT   decarboxylase induced by low oxygen stress.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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; DQ001727; AAZ05070.1; -; mRNA.
DR   RefSeq; NP_001275838.1; NM_001288909.1.
DR   AlphaFoldDB; Q1I1D8; -.
DR   GeneID; 102612842; -.
DR   KEGG; cit:102612842; -.
DR   OrthoDB; 2783360at2759; -.
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:SF41; 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}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   494 AA;  56196 MW;  73AA8CDCA37FC5A5 CRC64;
     MVLSKTFSES DESIHSTFAS RYVRNSLPRF TMPENSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLMMAAI NKNYVDMDEY PVTTELQNRC VNIIARLFNA PLEDSETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PFDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLSEGYYVM DPAKAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLTE KNKETGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVVW RNKEDLPEEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGFEGY RNVMENCHEN AMVLKEGLEK
     TGRFNIVSKD EGVPLVAFSL KDNKRHDEFE VAELLRRFGW IVPAYTMPAD AQHITVLRVV
     IREDFSRTLA ERLVLDITKV LHELDSLPSK VLVPASEQNG RNGKKTEIET QREVTTYWRK
     FVSERKANNK NKIC
//