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Database: UniProt/TrEMBL
Entry: B4FUE3_MAIZE
LinkDB: B4FUE3_MAIZE
Original site: B4FUE3_MAIZE 
ID   B4FUE3_MAIZE            Unreviewed;       488 AA.
AC   B4FUE3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
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=100273302 {ECO:0000313|EnsemblPlants:Zm00001eb081550_P003};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF85736.1};
RN   [1] {ECO:0000313|EMBL:ACF85736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF85736.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EnsemblPlants:Zm00001eb081550_P003, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb081550_P003,
RC   ECO:0000313|Proteomes:UP000007305};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb081550_P003}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb081550_P003};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) 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; BT040731; ACF85736.1; -; mRNA.
DR   RefSeq; NP_001141215.1; NM_001147743.1.
DR   AlphaFoldDB; B4FUE3; -.
DR   EnsemblPlants; Zm00001eb081550_T003; Zm00001eb081550_P003; Zm00001eb081550.
DR   GeneID; 100273302; -.
DR   Gramene; Zm00001eb081550_T003; Zm00001eb081550_P003; Zm00001eb081550.
DR   KEGG; zma:100273302; -.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; B4FUE3; 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   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   1: Evidence at protein level;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B4FUE3};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   488 AA;  54572 MW;  38993E7A6DBEB4D2 CRC64;
     MALALSTCRT CRSSRYELGE KSVSKDAAYQ IIHDELLLDS SPRLNLASFV TTWMEPECDK
     LILEGINKNY ADMDEYPVTT ELQNRCVNII ARLFHAPVGA SEKAVGVGTV GSSEAIMLAG
     LAFKRRWQNR RRAAGQPCDR PNIVTGANVQ VCWEKFARYF EVELKEVRLR EGCYVMDPDE
     AVRMVDDNTI CVAAILGSTL TGEFEDVRRL NDLLAANNRR TGWDTPIHVD AASGGFIAPF
     LYPDLEWDFR LPLVKSINVS GHKYGLVYAG VGWVVWRSKE DLPDELIFHI NYLGADQPTF
     TLNFSKGSSQ IIAQYYQFLR LGFEGYRNVM ENCMESARTL REGLERTGRF TIISKEQGVP
     LVAFTFKAKD ETPLAFKLSA ELRRFGWIVP AYTMPANLEH MAVLRVVVRE DFGRPLAERF
     LSHVRMALEE LDHAAKGGPV PKMRLTIELG PPARGSGEEA SARVVKREAV VPVHRSVSLA
     GGKTKGVC
//
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