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Reviewed, UniProtKB/Swiss-Prot P24295 (DHE2_CLOSY)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NAD-specific glutamate dehydrogenase
      Short name=NAD-GDH
    EC=1.4.1.2
Gene names
Name: gdh
OrganismClostridium symbiosum (Bacteroides symbiosus)
Taxonomic identifier1512 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

Pathway

Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 1/5.

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.

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Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glutamate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 450449NAD-specific glutamate dehydrogenase
PRO_0000182738

Sites

Active site1261

Experimental info

Sequence conflict431Y → S AA sequence Ref.4
Sequence conflict1651G → V AA sequence Ref.4
Sequence conflict3261D → A AA sequence Ref.4

Secondary structure

1 ............................................................................ 450
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P24295-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 993BB613288974E6

FASTA45049,296
        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

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References

[1]"The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli."
Teller J.K., Smith R.M., McPherson M.J., Engel P.C., Guest J.R.
Eur. J. Biochem. 206:151-159(1992) [PubMed: 1587267] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The partial amino acid sequence of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity."
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.
Biochim. Biophys. Acta 1080:191-197(1991) [PubMed: 1954226] [Abstract]
Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
[3]"The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate."
Lilley K.S., Engel P.C.
Eur. J. Biochem. 207:533-540(1992) [PubMed: 1633808] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, MODIFICATION OF SOME LYSINES.
[4]"Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding."
Syed S.E., Hornby D.P., Brown P.E., Fitton J.E., Engel P.C.
Biochem. J. 298:107-113(1994) [PubMed: 8129708] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-46; 154-158; 165-182 AND 325-339.
[5]"Subunit assembly and active site location in the structure of glutamate dehydrogenase."
Baker P.J., Britton K.L., Engel P.C., Farrants G.W., Lilley K.S., Rice D.W., Stillman T.J.
Proteins 12:75-86(1992) [PubMed: 1553382] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
[6]"Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis."
Stillman T.J., Baker P.J., Britton K.L., Rice D.W.
J. Mol. Biol. 234:1131-1139(1993) [PubMed: 8263917] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]"Determinants of substrate specificity in the superfamily of amino acid dehydrogenases."
Baker P.J., Waugh M.L., Wang X.G., Stillman T.J., Turnbull A.P., Engel P.C., Rice D.W.
Biochemistry 36:16109-16115(1997) [PubMed: 9405044] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

Z11747 Genomic DNA. Translation: CAA77805.1.
PIRS22403.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AUPX-ray2.50A2-450[»]
1BGVX-ray1.90A2-450[»]
1HRDX-ray1.96A/B/C2-449[»]
1K89X-ray2.05A2-449[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.1.2. 20537.

Family and domain databases

InterProIPR006095. Glu/Leu/Phe/Val_DH.
IPR006096. Glu/Leu/Phe/Val_DH_C.
IPR006097. Glu/Leu/Phe/Val_DH_dimer.
IPR014362. Glu_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11606:SF2. GLFV_DH. 1 hit.
PfamPF00208. ELFV_dehydrog. 1 hit.
PF02812. ELFV_dehydrog_N. 1 hit.
[Graphical view]
PIRSFPIRSF000185. Glu_DH. 1 hit.
PRINTSPR00082. GLFDHDRGNASE.
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDHE2_CLOSY
AccessionPrimary (citable) accession number: P24295
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 70 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents