ID DHE3_THEMA Reviewed; 416 AA. AC P96110; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 146. DE RecName: Full=Glutamate dehydrogenase; DE Short=GDH; DE EC=1.4.1.3; GN Name=gdhA; Synonyms=gdh; OrderedLocusNames=TM_1015; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, AND RP CHARACTERIZATION. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=9680336; DOI=10.1007/s007920050014; RA Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M.; RT "Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga RT maritima: molecular characterization and phylogenetic implications."; RL Extremophiles 1:52-60(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=9135121; DOI=10.1006/jmbi.1996.0900; RA Knapp S., de Vos W.M., Rice D., Ladenstein R.; RT "Crystal structure of glutamate dehydrogenase from the hyperthermophilic RT eubacterium Thermotoga maritima at 3.0-A resolution."; RL J. Mol. Biol. 267:916-932(1997). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=9654452; DOI=10.1006/jmbi.1998.1870; RA Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., RA de Vos W.M.; RT "Engineering activity and stability of Thermotoga maritima glutamate RT dehydrogenase. I. Introduction of a six-residue ion-pair network in the RT hinge region."; RL J. Mol. Biol. 280:287-296(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=10366510; DOI=10.1006/jmbi.1999.2779; RA Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., RA de Vos W.M.; RT "Engineering activity and stability of Thermotoga maritima glutamate RT dehydrogenase. II: construction of a 16-residue ion-pair network at the RT subunit interface."; RL J. Mol. Biol. 289:357-369(1999). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10011}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10011}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius. Thermostable.; CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {ECO:0000305}. 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; Y09925; CAA71058.1; -; Genomic_DNA. DR EMBL; AE000512; AAD36092.1; -; Genomic_DNA. DR PIR; G72305; G72305. DR PIR; T45284; T45284. DR RefSeq; NP_228821.1; NC_000853.1. DR RefSeq; WP_004080520.1; NZ_CP011107.1. DR PDB; 1B26; X-ray; 3.00 A; A/B/C/D/E/F=1-416. DR PDB; 1B3B; X-ray; 3.10 A; A/B/C/D/E/F=2-416. DR PDB; 2TMG; X-ray; 2.90 A; A/B/C/D/E/F=2-416. DR PDBsum; 1B26; -. DR PDBsum; 1B3B; -. DR PDBsum; 2TMG; -. DR AlphaFoldDB; P96110; -. DR SMR; P96110; -. DR STRING; 243274.TM_1015; -. DR PaxDb; 243274-THEMA_09280; -. DR EnsemblBacteria; AAD36092; AAD36092; TM_1015. DR KEGG; tma:TM1015; -. DR eggNOG; COG0334; Bacteria. DR InParanoid; P96110; -. DR OrthoDB; 9803297at2; -. DR BRENDA; 1.4.1.3; 6331. DR EvolutionaryTrace; P96110; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IBA:GO_Central. DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA. DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central. DR CDD; cd01076; NAD_bind_1_Glu_DH; 1. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer. DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS. DR InterPro; IPR014362; Glu_DH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR033922; NAD_bind_Glu_DH. DR NCBIfam; NF040817; GdhA_Arch; 1. DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1. DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PIRSF; PIRSF000185; Glu_DH; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; NAD; NADP; Oxidoreductase; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9680336" FT CHAIN 2..416 FT /note="Glutamate dehydrogenase" FT /id="PRO_0000182764" FT ACT_SITE 105 FT CONFLICT 153 FT /note="M -> I (in Ref. 1; CAA71058)" FT /evidence="ECO:0000305" FT HELIX 6..20 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 25..32 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 35..45 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 51..62 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 80..97 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 103..109 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 117..130 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:2TMG" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:1B26" FT HELIX 150..164 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:1B3B" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:2TMG" FT TURN 183..187 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 188..203 FT /evidence="ECO:0007829|PDB:2TMG" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 212..216 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 220..231 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 255..264 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:1B3B" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 288..292 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 322..330 FT /evidence="ECO:0007829|PDB:2TMG" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 338..341 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 344..357 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 364..389 FT /evidence="ECO:0007829|PDB:2TMG" FT HELIX 393..411 FT /evidence="ECO:0007829|PDB:2TMG" SQ SEQUENCE 416 AA; 45821 MW; D7294929879CB4F2 CRC64; MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH VEVFTGYRVQ HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP FGGGKGGVRV DPKKLSRNEL ERLSRRFFSE IQVIIGPYND IPAPDVNTNA DVMAWYMDTY SMNVGHTVLG IVTGKPVELG GSKGREEATG RGVKVCAGLA MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV SDSRGGIYNP EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY FEWVQDLQSF FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL AIDRVAYATK KRGIYP //