ID D5UYD0_TSUPD Unreviewed; 488 AA. AC D5UYD0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 70. 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=Tpau_1616 {ECO:0000313|EMBL:ADG78237.1}; OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP OS 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040) OS (Corynebacterium paurometabolum). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae; OC Tsukamurella. OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG78237.1, ECO:0000313|Proteomes:UP000001213}; RN [1] {ECO:0000313|Proteomes:UP000001213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 / RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040 RC {ECO:0000313|Proteomes:UP000001213}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Tapia R., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., RA Woyke T., Wu D., Jando M., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Tsukamurella paurometabola DSM 20162."; RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADG78237.1, ECO:0000313|Proteomes:UP000001213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 / RC KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040 RC {ECO:0000313|Proteomes:UP000001213}; RX PubMed=21886861; RA Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F., RA Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M., Ivanova N., RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Tapia R., RA Han C., Land M., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., RA Yasawong M., Brambilla E.M., Rohde M., Sikorski J., Goker M., Detter J.C., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Tsukamurella paurometabola type strain (no. RT 33)."; RL Stand. Genomic Sci. 4:342-351(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; CP001966; ADG78237.1; -; Genomic_DNA. DR AlphaFoldDB; D5UYD0; -. DR STRING; 521096.Tpau_1616; -. DR KEGG; tpr:Tpau_1616; -. DR eggNOG; COG0076; Bacteria. DR HOGENOM; CLU_019582_2_2_11; -. DR Proteomes; UP000001213; 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 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:UP000001213}. FT MOD_RES 306 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 488 AA; 52847 MW; 65756B374C3A0B95 CRC64; MPREQGEITA ARGALPTGRF AGSVRRMSEF STPLDDDSVL MPAYSGRLGT EPVPRARLAD HETGPAEAYR FIHDELMLDG QSRMNLATFV TTWMEPQGQA LMAEAFDKNA IDHDEYPATS AIDARTVAIV AELFHAPGLD PADPLSATGT TTIGSSEAVM LAGLALKWRW RKARLAAGGD ASRPKLVLGS NVQVVWEKFC RYFDVEPVYL PIAPGRYTIT PEQVRDAVDA DTIGAVAILG TTFTGEYEDV AGICAALDAV AESGGPDVPV HVDAASGGFV APFLDPDLEW DFRLPRVASI NVSGHKFGLT YPGIGFVVFR DRAALDEDLV FRVNYLGGDM PTFTLNFSRP GAQIIGQYYN FVRLGRHGYT RVMESLRGTA TWLARQLAAQ PYLSVITDGS ALPVVTLHLA DDAPFTAFDV SHELRTCGWQ VPAYTMPADA QEVTVLRIVV REGFSGDLAG KLRDDFAAAL TRLSAADGRA APRSVFHY //