ID A6L734_PHOV8 Unreviewed; 482 AA. AC A6L734; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 97. 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=BVU_3895 {ECO:0000313|EMBL:ABR41498.1}; OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Phocaeicola. OX NCBI_TaxID=435590 {ECO:0000313|EMBL:ABR41498.1, ECO:0000313|Proteomes:UP000002861}; RN [1] {ECO:0000313|EMBL:ABR41498.1, ECO:0000313|Proteomes:UP000002861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / RC NCTC 11154 {ECO:0000313|Proteomes:UP000002861}; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., RA Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). 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; CP000139; ABR41498.1; -; Genomic_DNA. DR RefSeq; WP_012055931.1; NC_009614.1. DR AlphaFoldDB; A6L734; -. DR STRING; 435590.BVU_3895; -. DR PaxDb; 435590-BVU_3895; -. DR KEGG; bvu:BVU_3895; -. DR PATRIC; fig|435590.9.peg.3999; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_019582_2_1_10; -. DR BioCyc; BVUL435590:G1G59-4031-MONOMER; -. DR Proteomes; UP000002861; 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:UP000002861}. FT MOD_RES 276 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 482 AA; 54642 MW; E31D4BB75B53CE7A CRC64; MKECNCDLRD GDAKTAVFGS NEMLQPAPVD TIPMEPTTPQ IAYQMVKDET FAQTQPRLNL ATFVTTYMDD YATKLMNEAI SINYIDETEY PRIAVMNAKC INIMANLWNS PEQAKWKTGA LAIGSSEACM LGGVAAWLRW KDKRKAQGKP TDKPNFVISS GFQVVWEKFA QLWQIEMRQV PLTLDKTTLD PEEALKMCDE NTICIVPIQG VTWTGLNDDV EALDKALDAY NAKTGYDIPI HVDAATGGFI LPFLNPDTKW DFRLKWVLSI STSGHKFGLV YPGLGWVVWK DKKYLPDAMS FSVNYLGANI TQVGLNFSRP AAQILGQYYQ FIRLGFQGYK AIQYNSMEIT KYIHSEIAKM APFVNYSDDV VNPLFIWYMK PEYAKNAKWT LYDLQAKLQQ SGWMVPAYTL PENIQNYVVM RVVVRQGFSR DMADMLLNDI KNAICEFEKL EYPTPTRIAQ DKNIAVKGTV FTHNAHSNAA KK //