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UniProtKB/Swiss-Prot entry P24295


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

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Entry information
Entry name DHE2_CLOSY
Primary accession number P24295
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
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 NAD-specific glutamate dehydrogenase
Synonyms NAD-GDH
EC 1.4.1.2
Gene name
Name: gdh
From
Clostridium symbiosum (Bacteroides symbiosus) [TaxID: 1512] 
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1587267 [NCBI, ExPASy, EBI, Israel, Japan]
Teller J.K., Smith R.M., McPherson M.J., Engel P.C., Guest J.R.;
"The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli.";
Eur. J. Biochem. 206:151-159(1992).
[2]
PRELIMINARY PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/0167-4838(91)90001-G; PubMed=1954226 [NCBI, ExPASy, EBI, Israel, Japan]
Lilley K.S., Baker P.J., Britton K.L., Stillman T.J., Brown P.E., Moir A.J.G., Engel P.C., Rice D.W., Bell J.E., Bell E.;
"The partial amino acid sequence of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity.";
Biochim. Biophys. Acta 1080:191-197(1991).
[3]
PARTIAL PROTEIN SEQUENCE, AND MODIFICATION OF SOME LYSINES.
PubMed=1633808 [NCBI, ExPASy, EBI, Israel, Japan]
Lilley K.S., Engel P.C.;
"The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.";
Eur. J. Biochem. 207:533-540(1992).
[4]
PROTEIN SEQUENCE OF 26-46; 154-158; 165-182 AND 325-339.
PubMed=8129708 [NCBI, ExPASy, EBI, Israel, Japan]
Syed S.E., Hornby D.P., Brown P.E., Fitton J.E., Engel P.C.;
"Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding.";
Biochem. J. 298:107-113(1994).
[5]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
DOI=10.1002/prot.340120109; PubMed=1553382 [NCBI, ExPASy, EBI, Israel, Japan]
Baker P.J., Britton K.L., Engel P.C., Farrants G.W., Lilley K.S., Rice D.W., Stillman T.J.;
"Subunit assembly and active site location in the structure of glutamate dehydrogenase.";
Proteins 12:75-86(1992).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1006/jmbi.1993.1665; PubMed=8263917 [NCBI, ExPASy, EBI, Israel, Japan]
Stillman T.J., Baker P.J., Britton K.L., Rice D.W.;
"Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis.";
J. Mol. Biol. 234:1131-1139(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1021/bi972024x; PubMed=9405044 [NCBI, ExPASy, EBI, Israel, Japan]
Baker P.J., Waugh M.L., Wang X.G., Stillman T.J., Turnbull A.P., Engel P.C., Rice D.W.;
"Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.";
Biochemistry 36:16109-16115(1997).
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
Z11747; CAA77805.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S22403; S22403.
3D structure databases
PDB
1AUP; X-ray; 2.50 A; A=1-450.[ExPASy / RCSB / EBI]
1BGV; X-ray; 1.90 A; A=1-450.[ExPASy / RCSB / EBI]
1HRD; X-ray; 1.96 A; A/B/C=1-450.[ExPASy / RCSB / EBI]
1K89; X-ray; 2.05 A; A=1-450.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AUP; -.
1BGV; -.
1HRD; -.
1K89; -.
ModBase P24295.
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 P24295.
Other
LinkHub P24295; -.
ProtoNet P24295.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   450  449     NAD-specific glutamate dehydrogenase. PRO_0000182738
ACT_SITE   126   126         
CONFLICT   43    43        Y -> S (in Ref. 4; AA sequence). 
CONFLICT   165   165        G -> V (in Ref. 4; AA sequence). 
CONFLICT   326   326        D -> A (in Ref. 4; AA sequence). 
HELIX   3    15  13      
TURN   16    18  3      
HELIX   20    31  12      
HELIX   34    38  5      
HELIX   41    45  5      
HELIX   48    52  5      
STRAND   56    66  11      
STRAND   72    83  12      
STRAND   85    95  11      
HELIX   101   117  17      
STRAND   119   121  3      
STRAND   124   130  7      
HELIX   138   152  15      
HELIX   153   155  3      
TURN   158   160  3      
STRAND   161   164  4      
HELIX   171   185  15      
HELIX   190   192  3      
STRAND   193   195  3      
HELIX   198   200  3      
TURN   204   208  5      
HELIX   209   224  16      
STRAND   233   236  4      
HELIX   241   253  13      
STRAND   259   262  4      
STRAND   265   268  4      
HELIX   276   288  13      
HELIX   294   300  7      
STRAND   303   306  4      
HELIX   310   312  3      
STRAND   316   319  4      
HELIX   329   337  9      
STRAND   342   344  3      
STRAND   347   349  3      
HELIX   353   361  9      
STRAND   366   368  3      
HELIX   370   373  4      
HELIX   376   390  15      
HELIX   396   420  25      
HELIX   427   446  20      
Sequence information
Length: 450 AA [This is the length of the unprocessed precursor] Molecular weight: 49296 Da [This is the MW of the unprocessed precursor] CRC64: 993BB613288974E6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKYVDRVIA EVEKKYADEP EFVQTVEEVL SSLGPVVDAH PEYEEVALLE RMVIPERVIE 

        70         80         90        100        110        120 
FRVPWEDDNG KVHVNTGYRV QFNGAIGPYK GGLRFAPSVN LSIMKFLGFE QAFKDSLTTL 

       130        140        150        160        170        180 
PMGGAKGGSD FDPNGKSDRE VMRFCQAFMT ELYRHIGPDI DVPAGDLGVG AREIGYMYGQ 

       190        200        210        220        230        240 
YRKIVGGFYN GVLTGKARSF GGSLVRPEAT GYGSVYYVEA VMKHENDTLV GKTVALAGFG 

       250        260        270        280        290        300 
NVAWGAAKKL AELGAKAVTL SGPDGYIYDP EGITTEEKIN YMLEMRASGR NKVQDYADKF 

       310        320        330        340        350        360 
GVQFFPGEKP WGQKVDIIMP CATQNDVDLE QAKKIVANNV KYYIEVANMP TTNEALRFLM 

       370        380        390        400        410        420 
QQPNMVVAPS KAVNAGGVLV SGFEMSQNSE RLSWTAEEVD SKLHQVMTDI HDGSAAAAER 

       430        440        450 
YGLGYNLVAG ANIVGFQKIA DAMMAQGIAW 

P24295 in FASTA format

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