ID F5YXP1_MYCSD Unreviewed; 461 AA. AC F5YXP1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 66. 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=gadB {ECO:0000313|EMBL:AEF37245.1}; GN OrderedLocusNames=JDM601_3245 {ECO:0000313|EMBL:AEF37245.1}; OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacter. OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF37245.1, ECO:0000313|Proteomes:UP000009224}; RN [1] {ECO:0000313|EMBL:AEF37245.1, ECO:0000313|Proteomes:UP000009224} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF37245.1, RC ECO:0000313|Proteomes:UP000009224}; RX PubMed=21685274; DOI=10.1128/JB.05291-11; RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z., RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.; RT "Complete genome sequence of a novel clinical isolate, the nontuberculous RT Mycobacterium strain JDM601."; RL J. Bacteriol. 193:4300-4301(2011). 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|ARBA:ARBA00000018, CC 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; CP002329; AEF37245.1; -; Genomic_DNA. DR RefSeq; WP_013830174.1; NC_015576.1. DR AlphaFoldDB; F5YXP1; -. DR STRING; 875328.JDM601_3245; -. DR KEGG; mjd:JDM601_3245; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_019582_2_2_11; -. DR OrthoDB; 3401800at2; -. DR Proteomes; UP000009224; Chromosome. 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: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:UP000009224}. FT MOD_RES 277 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 461 AA; 50924 MW; 04410B07E8FA6F35 CRC64; MTHSHPSVPA HTIAPAYTGR LFTSPVPALR MPDESMEPQA AYRFIHDELM LDGSSRLNLA TFVTTWMDPE ASALMAESFD KNMIDKDEYP ATAAIEQRCV SMVADLFHAE NLRDDDPASA IGVSTVGSSE AVMLGGLALK WRWRAKVGDW QGRTPNLVMG SNVQVVWEKF CRYFDVEPRY LPMAQGRYVI TPEQVVDAVD ENTIGVVAIL GTTYTGELEP VEAICAALDK LAAGGGPDVP VHVDAASGGF VVPFLHPDLK WDFRLPRVVS INVSGHKYGL TYPGIGFVVW RGADYLPEEL VFRVNYLGGD MPTFTLNFSR PGNQVVGQYY NFLRLGRSGY TEVMRTLSDT ARWLSHQLAD SEHFEVISDG SAIPVVSCRL AGKRGYTEFD VSHELRTFGW QVPAYTMPEG AEDVAVLRVV VREGLSADLA RALFDDTMKA VTALDRLKPG GHFDDQQHFS H //