ID A0Q8J3_FRATN Unreviewed; 448 AA. AC A0Q8J3; DT 09-JAN-2007, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 100. 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 OrderedLocusNames=FTN_1701 {ECO:0000313|EMBL:ABK90558.1}; GN ORFNames=AW25_287 {ECO:0000313|EMBL:AJI60776.1}; OS Francisella tularensis subsp. novicida (strain U112). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=401614 {ECO:0000313|EMBL:ABK90558.1, ECO:0000313|Proteomes:UP000000762}; RN [1] {ECO:0000313|EMBL:ABK90558.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=U112 {ECO:0000313|EMBL:ABK90558.1}; RA Brittnacher M., Rohmer L., Zhou Y., Abmayr S., D'Argenio D., Bovee D., RA Chang J., Chen J., Drees B., Ernst R., Fong C., Forsman M., Gallagher L., RA Gallis B., Gillett W., Goodlett D., Guina T., Guenthner D., Haugen E., RA Hayden H., Jacobs M., Kang A., Larson Freeman T., Levy R., Lim R., RA Manoil C., Olson M.V., Radey M., Shaffer S., Svensson K., Taylor G., RA Wasnick M., Kaul R., Miller S.I.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000000762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|Proteomes:UP000000762}; RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102; RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M., RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C., RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J., RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A., RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V., RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.; RT "Comparison of Francisella tularensis genomes reveals evolutionary events RT associated with the emergence of human pathogenic strains."; RL Genome Biol. 8:R102.1-R102.16(2007). RN [3] {ECO:0000313|EMBL:AJI60776.1, ECO:0000313|Proteomes:UP000031872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=U112 {ECO:0000313|EMBL:AJI60776.1, RC ECO:0000313|Proteomes:UP000031872}; RX PubMed=25931589; RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G., RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O., RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S., RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.; RT "Genome sequencing of 18 francisella strains to aid in assay development RT and testing."; RL Genome Announc. 3:0-0(2015). 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; CP000439; ABK90558.1; -; Genomic_DNA. DR EMBL; CP009633; AJI60776.1; -; Genomic_DNA. DR RefSeq; WP_003041366.1; NZ_CP009633.1. DR AlphaFoldDB; A0Q8J3; -. DR KEGG; ftn:FTN_1701; -. DR KEGG; ftx:AW25_287; -. DR BioCyc; FTUL401614:G1G75-1761-MONOMER; -. DR Proteomes; UP000000762; Chromosome. DR Proteomes; UP000031872; 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}. FT MOD_RES 266 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 448 AA; 50828 MW; B5798B19FE0FA0D4 CRC64; MALHGKKDTI NNLDFFEQSL PKFKLPLNSQ DPLEVYQEIK DELMLDGNSK QNLATFCQTE VDDFIHKLMD DCIDKNMIDK DEYPQTAEIE SRCVNILANL WNSSAENAIG CSTTGSSEAA MLGGMAMKWR WRDKMKAQGK DYTKPNLVTG PVQVCWHKFA RYWDIELREI PMSNESLIMT PEAVLERCDE NTIGVVPTLG VTFTGQYEPV EQVCKALDDF ERQTGIDIPV HVDAASGGFL APFVEPELKW DFRLPRVKSI NSSGHKFGLS PLGVGWVIWA DKKYLPDDLI FNVNYLGGNM PTFALNFSRP GGQIVAQYYN FVRLGFEGYK KVHQLCYDVA EYIAKELRKM EIFEIIHAGE GGIPAVSWSL KATKEYSLFD ISEKVRAKGW QIAAYTMPTN REDLVVMRVL VRRGFSYDLA QLMIRDLVAV INSLEGKLKI LKRSSFAH //