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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //