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Protein

NADP-specific glutamate dehydrogenase

Gene

gdh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei113 – 1131PROSITE-ProRule annotation

GO - Molecular functioni

  1. glutamate dehydrogenase (NADP+) activity Source: PomBase

GO - Biological processi

  1. ammonia assimilation cycle Source: PomBase
  2. glutamate biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-specific glutamate dehydrogenase (EC:1.4.1.4)
Short name:
NADP-GDH
Alternative name(s):
NADP-dependent glutamate dehydrogenase
Gene namesi
Name:gdh1
ORF Names:SPCC622.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC622.12c.
PomBaseiSPCC622.12c.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. mitochondrion Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451NADP-specific glutamate dehydrogenasePRO_0000182794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei252 – 2521Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78804.
PaxDbiP78804.
PRIDEiP78804.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

BioGridi275719. 42 interactions.
MINTiMINT-4691289.
STRINGi4896.SPCC622.12c-1.

Structurei

3D structure databases

ProteinModelPortaliP78804.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243799.
InParanoidiP78804.
KOiK00262.
OMAiKGKSEHE.
OrthoDBiEOG7XSTPW.
PhylomeDBiP78804.

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.

P78804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPYEPEFQ QAYKEIVGSI ESSKLFEVHP ELKRVLPIIS IPERVLEFRV
60 70 80 90 100
TWEDDKGNCR VNTGYRVQFN SALGPYKGGL RFHPSVNLSI LKFLGFEQIF
110 120 130 140 150
KNALTGLPMG GGKGGSDFDP KGKSDNEIRR FSQAFMRQLF RYIGPQTDVP
160 170 180 190 200
AGDIGVTGFV VMHMFGEYKR LRNEYSGVVT GKHMLTGGSN IRPEATGYGV
210 220 230 240 250
VYYVKHMIEH RTKGAETLKG KRVAISGSGN VAQYAALKCI QEGAIVKSIS
260 270 280 290 300
DSKGVLIAKT AEGLVPEEIH EIMALKEKRA SIADSASLCK KHHYIAGARP
310 320 330 340 350
WTNVGEIDIA LPCATQNEVS GEEAAALIKQ GCRYVAEGSN MGSSAEAVEV
360 370 380 390 400
FEKSRASGEG CWLAPGKAAN AGGVAVSGLE MAQNAQFSTW THAEVDAKLA
410 420 430 440 450
GIMQNIFEQS TDVASKYCDS GSNNIPSLVD GANIAGFLKV ATAMQAVGDW

W
Length:451
Mass (Da):48,790
Last modified:August 1, 1999 - v2
Checksum:iDC05673E6A3433F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21868.1.
D89153 mRNA. Translation: BAA13815.1.
PIRiT41492.
RefSeqiNP_588184.1. NM_001023174.2.

Genome annotation databases

EnsemblFungiiSPCC622.12c.1; SPCC622.12c.1:pep; SPCC622.12c.
GeneIDi2539147.
KEGGispo:SPCC622.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21868.1.
D89153 mRNA. Translation: BAA13815.1.
PIRiT41492.
RefSeqiNP_588184.1. NM_001023174.2.

3D structure databases

ProteinModelPortaliP78804.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275719. 42 interactions.
MINTiMINT-4691289.
STRINGi4896.SPCC622.12c-1.

Proteomic databases

MaxQBiP78804.
PaxDbiP78804.
PRIDEiP78804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC622.12c.1; SPCC622.12c.1:pep; SPCC622.12c.
GeneIDi2539147.
KEGGispo:SPCC622.12c.

Organism-specific databases

EuPathDBiFungiDB:SPCC622.12c.
PomBaseiSPCC622.12c.

Phylogenomic databases

eggNOGiCOG0334.
HOGENOMiHOG000243799.
InParanoidiP78804.
KOiK00262.
OMAiKGKSEHE.
OrthoDBiEOG7XSTPW.
PhylomeDBiP78804.

Enzyme and pathway databases

ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).

Miscellaneous databases

NextBioi20800319.
PROiP78804.

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]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-447.
    Strain: PR745.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDHE4_SCHPO
AccessioniPrimary (citable) accession number: P78804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: August 1, 1999
Last modified: April 29, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.