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Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 2

Gene

gpd2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231NADBy similarity
Binding sitei146 – 1461NAD; via amide nitrogenBy similarity
Binding sitei146 – 1461SubstrateBy similarity
Binding sitei179 – 1791NAD; via amide nitrogenBy similarity
Active sitei236 – 2361Proton acceptorBy similarity
Binding sitei300 – 3001NADBy similarity
Binding sitei329 – 3291NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 366NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • glycerol-3-phosphate catabolic process Source: InterPro
  • glycerol biosynthetic process Source: PomBase
  • NADH oxidation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_326669. Synthesis of PA.
REACT_332761. Triglyceride Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 2 (EC:1.1.1.8)
Gene namesi
Name:gpd2
ORF Names:SPAC23D3.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC23D3.04c.
PomBaseiSPAC23D3.04c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • glycerol-3-phosphate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Glycerol-3-phosphate dehydrogenase [NAD(+)] 2PRO_0000138096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09845.
PaxDbiQ09845.

Interactioni

Protein-protein interaction databases

BioGridi278004. 12 interactions.
MINTiMINT-4695674.
STRINGi4896.SPAC23D3.04c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09845.
SMRiQ09845. Positions 26-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni300 – 3012Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246855.
InParanoidiQ09845.
KOiK00006.
OMAiEVANDNF.
OrthoDBiEOG7V76H7.
PhylomeDBiQ09845.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVAALNKLS ALSGSIQKSF SPKLISVGII GSGNWGTAIA KICGENAKAH
60 70 80 90 100
PDIFHPQVHM WMYEEKIQHE GKECNLTEVF NTTHENVKYL KGIKCPSNVF
110 120 130 140 150
ANPDIRDVGS RSDILVWVLP HQFVVRICNQ LKGCLKKDAV AISCIKGVSV
160 170 180 190 200
TKDRVRLFSD IIEENTGMYC GVLSGANIAS EVAQEKFCET TIGYLPNSSV
210 220 230 240 250
NPRYTPKTIQ ALFNRPYFRV NIVEDVPGVA LGGALKNIVA VAAGIIDGLE
260 270 280 290 300
LGDNTKSAVM RIGLLEMQKF GRMFFDCKPL TMSEESCGIA DLITTCLGGR
310 320 330 340 350
NHKCAVAFVK TGKPMHVVEQ ELLDGQKLQG AATAKEVYEF LDNQNKVSEF
360 370
PLFTAVYRIV YEGLPPNKLL EAI
Length:373
Mass (Da):40,874
Last modified:February 1, 1996 - v1
Checksum:i7C3AFBC3DFFB470E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50797 Genomic DNA. Translation: BAA09425.1.
CU329670 Genomic DNA. Translation: CAA91239.1.
PIRiJC6053.
RefSeqiNP_594542.1. NM_001019971.2.

Genome annotation databases

EnsemblFungiiSPAC23D3.04c.1; SPAC23D3.04c.1:pep; SPAC23D3.04c.
GeneIDi2541502.
KEGGispo:SPAC23D3.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50797 Genomic DNA. Translation: BAA09425.1.
CU329670 Genomic DNA. Translation: CAA91239.1.
PIRiJC6053.
RefSeqiNP_594542.1. NM_001019971.2.

3D structure databases

ProteinModelPortaliQ09845.
SMRiQ09845. Positions 26-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278004. 12 interactions.
MINTiMINT-4695674.
STRINGi4896.SPAC23D3.04c-1.

Proteomic databases

MaxQBiQ09845.
PaxDbiQ09845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23D3.04c.1; SPAC23D3.04c.1:pep; SPAC23D3.04c.
GeneIDi2541502.
KEGGispo:SPAC23D3.04c.

Organism-specific databases

EuPathDBiFungiDB:SPAC23D3.04c.
PomBaseiSPAC23D3.04c.

Phylogenomic databases

eggNOGiCOG0240.
HOGENOMiHOG000246855.
InParanoidiQ09845.
KOiK00006.
OMAiEVANDNF.
OrthoDBiEOG7V76H7.
PhylomeDBiQ09845.

Enzyme and pathway databases

ReactomeiREACT_326669. Synthesis of PA.
REACT_332761. Triglyceride Biosynthesis.

Miscellaneous databases

NextBioi20802601.
PROiQ09845.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth."
    Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T.
    Mol. Microbiol. 18:963-973(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGPD2_SCHPO
AccessioniPrimary (citable) accession number: Q09845
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 27, 2015
This is version 119 of the entry and version 1 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.