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UniProtKB/Swiss-Prot entry P96110


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHE3_THEMA
Primary accession number P96110
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 63)
Name and origin of the protein
Protein name Glutamate dehydrogenase
Synonyms GDH
EC 1.4.1.3
Gene name
Name: gdhA
Synonyms: gdh
OrderedLocusNames: TM_1015
From
Thermotoga maritima [TaxID: 2336] [HAMAP proteome]
Taxonomy Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13, AND CHARACTERIZATION.
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
DOI=10.1007/s007920050014; PubMed=9680336 [NCBI, ExPASy, EBI, Israel, Japan]
Kort R., Liebl W., Labedan B., Forterre P., Eggen R.I.L., de Vos W.M.;
"Glutamate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: molecular characterization and phylogenetic implications.";
Extremophiles 1:52-60(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
DOI=10.1038/20601; PubMed=10360571 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima.";
Nature 399:323-329(1999).
[3]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1006/jmbi.1996.0900; PubMed=9135121 [NCBI, ExPASy, EBI, Israel, Japan]
Knapp S., de Vos W.M., Rice D., Ladenstein R.;
"Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0-A resolution.";
J. Mol. Biol. 267:916-932(1997).
[4]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
DOI=10.1006/jmbi.1998.1870; PubMed=9654452 [NCBI, ExPASy, EBI, Israel, Japan]
Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.;
"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region.";
J. Mol. Biol. 280:287-296(1998).
[5]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1006/jmbi.1999.2779; PubMed=10366510 [NCBI, ExPASy, EBI, Israel, Japan]
Lebbink J.H., Knapp S., van der Oost J., Rice D., Ladenstein R., de Vos W.M.;
"Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface.";
J. Mol. Biol. 289:357-369(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y09925; CAA71058.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000512; AAD36092.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G72305; G72305.
T45284; T45284.
RefSeq NP_228821.1; -.
3D structure databases
PDB
1B26; X-ray; 3.00 A; A/B/C/D/E/F=1-416.[ExPASy / RCSB / EBI]
1B3B; X-ray; 3.10 A; A/B/C/D/E/F=1-416.[ExPASy / RCSB / EBI]
2TMG; X-ray; 2.90 A; A/B/C/D/E/F=1-416.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B26; -.
1B3B; -.
2TMG; -.
ModBase P96110.
Enzyme and pathway databases
BioCyc TMAR243274:TM_1015-MON; -.
Family and domain databases
InterPro IPR006095; Glu/Leu/Phe/Val_DHase.
IPR006096; Glu/Leu/Phe/Val_DHase_C.
IPR006097; Glu/Leu/Phe/Val_DHase_dimer.
IPR014362; Glu_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11606:SF2; GLFV_DH; 1.
Pfam PF00208; ELFV_dehydrog; 1.
PF02812; ELFV_dehydrog_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000185; Glu_DH; 1.
PRINTS PR00082; GLFDHDRGNASE.
PROSITE PS00074; GLFV_DEHYDROGENASE; 1.
BLOCKS P96110.
Genome annotation databases
GeneID 896847; -.
GenomeReviews AE000512_GR; TM_1015.
KEGG tma:TM1015; -.
NMPDR fig|243274.1.peg.1005; -.
TIGR TM_1015; -.
Phylogenomic databases
HOGENOM P96110; -.
Other
ProtoNet P96110.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; NAD; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   416  415     Glutamate dehydrogenase. PRO_0000182764
ACT_SITE   105   105         
CONFLICT   153   153        M -> I (in Ref. 1; CAA71058). 
HELIX   6    20  15      
HELIX   25    32  8      
STRAND   35    45  11      
STRAND   51    62  12      
STRAND   66    74  9      
HELIX   80    97  18      
STRAND   102   109  8      
HELIX   112   114  3      
HELIX   117   130  14      
HELIX   131   133  3      
TURN   137   139  3      
STRAND   140   143  4      
HELIX   150   164  15      
HELIX   177   179  3      
TURN   183   187  5      
HELIX   188   203  16      
TURN   208   210  3      
STRAND   212   216  5      
HELIX   220   233  14      
STRAND   236   242  7      
STRAND   245   248  4      
HELIX   255   264  10      
STRAND   275   277  3      
HELIX   279   283  5      
STRAND   288   292  5      
HELIX   301   304  4      
STRAND   310   313  4      
STRAND   316   318  3      
HELIX   322   330  9      
STRAND   334   336  3      
HELIX   338   341  4      
HELIX   344   357  14      
HELIX   364   389  26      
HELIX   393   412  20      
Sequence information
Length: 416 AA [This is the length of the unprocessed precursor] Molecular weight: 45821 Da [This is the MW of the unprocessed precursor] CRC64: D7294929879CB4F2 [This is a checksum on the sequence]
        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 

P96110 in FASTA format

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