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P96110

- DHE3_THEMA

UniProt

P96110 - DHE3_THEMA

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Protein

Glutamate dehydrogenase

Gene

gdhA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

Temperature dependencei

Optimum temperature is 75 degrees Celsius. Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051

GO - Molecular functioni

  1. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-4406-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate dehydrogenase (EC:1.4.1.3)
Short name:
GDH
Gene namesi
Name:gdhA
Synonyms:gdh
Ordered Locus Names:TM_1015
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 416415Glutamate dehydrogenasePRO_0000182764Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi243274.TM1015.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2015
Helixi25 – 328
Beta strandi35 – 4511
Beta strandi51 – 6212
Beta strandi66 – 694
Beta strandi72 – 776
Helixi80 – 9718
Beta strandi103 – 1097
Helixi112 – 1143
Helixi117 – 13014
Helixi132 – 1343
Turni137 – 1393
Beta strandi140 – 1434
Helixi150 – 16415
Beta strandi171 – 1744
Helixi177 – 1793
Turni183 – 1875
Helixi188 – 20316
Turni208 – 2103
Beta strandi212 – 2165
Helixi220 – 23112
Beta strandi236 – 2416
Beta strandi246 – 2483
Helixi255 – 26410
Beta strandi265 – 2684
Beta strandi272 – 2776
Helixi279 – 2824
Beta strandi288 – 2925
Helixi301 – 3044
Beta strandi310 – 3134
Beta strandi316 – 3183
Helixi322 – 3309
Beta strandi334 – 3363
Helixi338 – 3414
Helixi344 – 35714
Helixi364 – 38926
Helixi393 – 41119

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B26X-ray3.00A/B/C/D/E/F1-416[»]
1B3BX-ray3.10A/B/C/D/E/F2-416[»]
2TMGX-ray2.90A/B/C/D/E/F2-416[»]
ProteinModelPortaliP96110.
SMRiP96110. Positions 5-413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96110.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
InParanoidiP96110.
KOiK00261.
OMAiTMELCQK.
OrthoDBiEOG65XN4D.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006095. 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]
PfamiPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000185. Glu_DH. 1 hit.
PRINTSiPR00082. GLFDHDRGNASE.
SMARTiSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P96110-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEKSLYEMA VEQFNRAASL MDLESDLAEV LRRPKRVLIV EFPVRMDDGH
60 70 80 90 100
VEVFTGYRVQ HNVARGPAKG GIRYHPDVTL DEVKALAFWM TWKTAVMNLP
110 120 130 140 150
FGGGKGGVRV DPKKLSRNEL ERLSRRFFSE IQVIIGPYND IPAPDVNTNA
160 170 180 190 200
DVMAWYMDTY SMNVGHTVLG IVTGKPVELG GSKGREEATG RGVKVCAGLA
210 220 230 240 250
MDVLGIDPKK ATVAVQGFGN VGQFAALLIS QELGSKVVAV SDSRGGIYNP
260 270 280 290 300
EGFDVEELIR YKKEHGTVVT YPKGERITNE ELLELDVDIL VPAALEGAIH
310 320 330 340 350
AGNAERIKAK AVVEGANGPT TPEADEILSR RGILVVPDIL ANAGGVTVSY
360 370 380 390 400
FEWVQDLQSF FWDLDQVRNA LEKMMKGAFN DVMKVKEKYN VDMRTAAYIL
410
AIDRVAYATK KRGIYP
Length:416
Mass (Da):45,821
Last modified:January 23, 2007 - v4
Checksum:iD7294929879CB4F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531M → I in CAA71058. (PubMed:9680336)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09925 Genomic DNA. Translation: CAA71058.1.
AE000512 Genomic DNA. Translation: AAD36092.1.
PIRiG72305.
T45284.
RefSeqiNP_228821.1. NC_000853.1.
YP_007977367.1. NC_021214.1.
YP_008991888.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36092; AAD36092; TM_1015.
GeneIDi18093702.
896847.
KEGGitma:TM1015.
tmi:THEMA_09280.
tmm:Tmari_1018.
PATRICi23936959. VBITheMar51294_1028.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09925 Genomic DNA. Translation: CAA71058.1 .
AE000512 Genomic DNA. Translation: AAD36092.1 .
PIRi G72305.
T45284.
RefSeqi NP_228821.1. NC_000853.1.
YP_007977367.1. NC_021214.1.
YP_008991888.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P96110.
SMRi P96110. Positions 5-413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1015.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36092 ; AAD36092 ; TM_1015 .
GeneIDi 18093702.
896847.
KEGGi tma:TM1015.
tmi:THEMA_09280.
tmm:Tmari_1018.
PATRICi 23936959. VBITheMar51294_1028.

Phylogenomic databases

eggNOGi COG0334.
InParanoidi P96110.
KOi K00261.
OMAi TMELCQK.
OrthoDBi EOG65XN4D.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-4406-MONOMER.

Miscellaneous databases

EvolutionaryTracei P96110.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi 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 ]
Pfami PF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000185. Glu_DH. 1 hit.
PRINTSi PR00082. GLFDHDRGNASE.
SMARTi SM00839. ELFV_dehydrog. 1 hit.
[Graphical view ]
PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, CHARACTERIZATION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Entry informationi

Entry nameiDHE3_THEMA
AccessioniPrimary (citable) accession number: P96110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 106 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3