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Reviewed, UniProtKB/Swiss-Prot P78804 (DHE4_SCHPO)

Last modified January 19, 2010. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    NADP-specific glutamate dehydrogenase
      Short name=NADP-GDH
    EC=1.4.1.4
Alternative name(s):
    NADP-dependent glutamate dehydrogenase
Gene names
Name: gdh1
ORF Names: SPCC622.12c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH.

Subunit structure

Homohexamer By similarity.

Sequence similarities

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

Ontologies

Keywords
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

glutamate dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451NADP-specific glutamate dehydrogenase
PRO_0000182794

Sites

Active site1131 By similarity

Amino acid modifications

Modified residue2521Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
P78804-1 [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: DC05673E6A3433F5

FASTA45148,790
        10         20         30         40         50         60 
MSTPYEPEFQ QAYKEIVGSI ESSKLFEVHP ELKRVLPIIS IPERVLEFRV TWEDDKGNCR 

        70         80         90        100        110        120 
VNTGYRVQFN SALGPYKGGL RFHPSVNLSI LKFLGFEQIF KNALTGLPMG GGKGGSDFDP 

       130        140        150        160        170        180 
KGKSDNEIRR FSQAFMRQLF RYIGPQTDVP AGDIGVTGFV VMHMFGEYKR LRNEYSGVVT 

       190        200        210        220        230        240 
GKHMLTGGSN IRPEATGYGV VYYVKHMIEH RTKGAETLKG KRVAISGSGN VAQYAALKCI 

       250        260        270        280        290        300 
QEGAIVKSIS DSKGVLIAKT AEGLVPEEIH EIMALKEKRA SIADSASLCK KHHYIAGARP 

       310        320        330        340        350        360 
WTNVGEIDIA LPCATQNEVS GEEAAALIKQ GCRYVAEGSN MGSSAEAVEV FEKSRASGEG 

       370        380        390        400        410        420 
CWLAPGKAAN AGGVAVSGLE MAQNAQFSTW THAEVDAKLA GIMQNIFEQS TDVASKYCDS 

       430        440        450 
GSNNIPSLVD GANIAGFLKV ATAMQAVGDW W 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-447.
Strain: PR745.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA21868.1.
D89153 mRNA. Translation: BAA13815.1.
PIRT41492.
RefSeqNP_588184.1.

3D structure databases

SMRP78804. Positions 3-450.
ModBaseSearch...

Protein-protein interaction databases

STRINGP78804.

Genome annotation databases

GeneID2539147.
GenomeReviewsGene locus gdh1 in contig CU329672_GR.
KEGGspo:SPCC622.12c.
NMPDRfig|4896.1.peg.522.

Organism-specific databases

GeneDB_SpombeSPCC622.12c.

Phylogenomic databases

eggNOGfuNOG07140.
HOGENOMHBG590661.
OMAWEVKADI.
OrthoDBEOG9Z0CP1.
PhylomeDBP78804.

Enzyme and pathway databases

BRENDA1.4.1.4. 653.

Gene expression databases

ArrayExpressP78804.

Family and domain databases

InterProIPR006095. 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]
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.
SMARTSM00839. ELFV_dehydrog. 1 hit.
[Graphical view]
PROSITEPS00074. GLFV_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHE4_SCHPO
AccessionPrimary (citable) accession number: P78804
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: August 1, 1999
Last modified: January 19, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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