DHE3_THEMA
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 25-MAY-2022, entry version 138.
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; Thermotogae; Thermotogales; Thermotogaceae; 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}.
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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.THEMA_09280; -.
DR EnsemblBacteria; AAD36092; AAD36092; TM_1015.
DR KEGG; tma:TM1015; -.
DR eggNOG; COG0334; Bacteria.
DR InParanoid; P96110; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 1184827at2; -.
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 InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR014362; Glu_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 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
