Reviewed, UniProtKB/Swiss-Prot P96110 (DHE3_THEMA)

Names and origin

Protein names

Recommended name:
    Glutamate dehydrogenase
      Short name=GDH
    EC=1.4.1.3

Gene names

Name:	gdhA
Synonyms:	gdh
Ordered Locus Names:	TM_1015

Organism

Thermotoga maritima [Complete proteome] [HAMAP]

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.
Subunit structure	Homohexamer.
Sequence similarities	Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 75 degrees Celsius. Thermostable.

Ontologies

Keywords
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro glutamate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 416

415

Glutamate dehydrogenase

PRO_0000182764

Sites

Active site

105

1

Experimental info

Sequence conflict

153

1

M → I in CAA71058. Ref.1

Secondary structure

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416

Helix Strand Turn

Details...

Helix

6 – 20

15

Helix

25 – 32

8

Beta strand

35 – 45

11

Beta strand

51 – 62

12

Beta strand

66 – 74

9

Helix

80 – 97

18

Beta strand

102 – 109

8

Helix

112 – 114

3

Helix

117 – 130

14

Helix

131 – 133

3

Turn

137 – 139

3

Beta strand

140 – 143

4

Helix

150 – 164

15

Helix

177 – 179

3

Turn

183 – 187

5

Helix

188 – 203

16

Turn

208 – 210

3

Beta strand

212 – 216

5

Helix

220 – 233

14

Beta strand

236 – 242

7

Beta strand

245 – 248

4

Helix

255 – 264

10

Beta strand

275 – 277

3

Helix

279 – 283

5

Beta strand

288 – 292

5

Helix

301 – 304

4

Beta strand

310 – 313

4

Beta strand

316 – 318

3

Helix

322 – 330

9

Beta strand

334 – 336

3

Helix

338 – 341

4

Helix

344 – 357

14

Helix

364 – 389

26

Helix

393 – 412

20

Sequences

	Sequence		Length	Mass (Da)
	P96110-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: D7294929879CB4F2	FASTA	416	45,821
	10 20 30 40 50 60 MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH VEVFTGYRVQ 70 80 90 100 110 120 HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP FGGGKGGVRV DPKKLSRNEL 130 140 150 160 170 180 ERLSRRFFSE IQVIIGPYND IPAPDVNTNA DVMAWYMDTY SMNVGHTVLG IVTGKPVELG 190 200 210 220 230 240 GSKGREEATG RGVKVCAGLA MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV 250 260 270 280 290 300 SDSRGGIYNP EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH 310 320 330 340 350 360 AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY FEWVQDLQSF 370 380 390 400 410 FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL AIDRVAYATK KRGIYP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications." Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M. Extremophiles 1:52-60(1997) [PubMed: 9680336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CHARACTERIZATION. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]	"Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0-A resolution." Knapp S., de Vos W.M., Rice D., Ladenstein R. J. Mol. Biol. 267:916-932(1997) [PubMed: 9135121] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[4]	"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region." Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M. J. Mol. Biol. 280:287-296(1998) [PubMed: 9654452] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
[5]	"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface." Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M. J. Mol. Biol. 289:357-369(1999) [PubMed: 10366510] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y09925 Genomic DNA. Translation: CAA71058.1.
AE000512 Genomic DNA. Translation: AAD36092.1.

PIR

G72305.
T45284.

RefSeq

NP_228821.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B26	X-ray	3.00	A/B/C/D/E/F	1-416	[»]
1B3B	X-ray	3.10	A/B/C/D/E/F	2-416	[»]
2TMG	X-ray	2.90	A/B/C/D/E/F	2-416	[»]

ModBase

Search...

Genome annotation databases

GeneID

896847.

GenomeReviews

Gene locus TM_1015 in contig AE000512_GR.

KEGG

tma:TM1015.

NMPDR

fig|243274.1.peg.1005.

TIGR

TM_1015.

Phylogenomic databases

HOGENOM

HBG590661.

OMA

ENMIHAS.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1015-MONOMER.

BRENDA

1.4.1.3. 16699.

Family and domain databases

InterPro

IPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11606:SF2. GLFV_DH. 1 hit.

Pfam

PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000185. Glu_DH. 1 hit.

PRINTS

PR00082. GLFDHDRGNASE.

SMART

SM00839. ELFV_dehydrog. 1 hit.
[Graphical view]

PROSITE

PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHE3_THEMA

Accession

Primary (citable) accession number: P96110

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 75 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)