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UniProtKB/Swiss-Prot entry Q09845


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

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Entry information
Entry name GPD2_SCHPO
Primary accession number Q09845
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name Glycerol-3-phosphate dehydrogenase [NAD+] 2
Synonym EC 1.1.1.8
Gene name
Name: gpd2
ORFNames: SPAC23D3.04c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8825100 [NCBI, ExPASy, EBI, Israel, Japan]
Ohmiya R., Yamada H., Nakashima K., Aiba H., Mizuno T.;
"Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth.";
Mol. Microbiol. 18:963-973(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
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
D50797; BAA09425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAA91239.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC6053; JC6053.
RefSeq NP_594542.1; -.
3D structure databases
ModBase Q09845.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-002639-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC23D3.04c; -.
Gene expression databases
ArrayExpress Q09845; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from GeneDB_SPombe).
GO:0004367; Molecular function: glycerol-3-phosphate dehydrogenase (NAD+) activity (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006114; Biological process: glycerol biosynthetic process (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR013328; DHase_multihelical.
IPR016040; NAD(P)-bd.
IPR017751; NAD-dep_Gly3P_DH_euk.
IPR006168; NAD-dep_Gly3P_DHase.
IPR011128; NAD-dep_Gly3P_DHase_N.
IPR006109; NAD_Gly3P_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:1.10.1040.10; Opine_DH; 1.
PANTHER PTHR11728; NAD_Gly3P_DH; 1.
Pfam PF07479; NAD_Gly3P_dh_C; 1.
PF01210; NAD_Gly3P_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS PR00077; GPDHDRGNASE.
ProDom PD001278; NAD_Gly3P_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00957; NAD_G3PDH; 1.
BLOCKS Q09845.
ProtoNet Q09845.
Genome annotation databases
GeneID 2541502; -.
KEGG spo:SPAC23D3.04c; -.
NMPDR fig|4896.1.peg.4512; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   373  373     Glycerol-3-phosphate dehydrogenase [NAD+] 2. PRO_0000138096
NP_BIND   31    36  6     NAD (By similarity). 
REGION   300   301  2     Substrate binding (By similarity). 
ACT_SITE   236   236        Proton acceptor (By similarity). 
BINDING   123   123        NAD (By similarity). 
BINDING   146   146        NAD; via amide nitrogen (By similarity). 
BINDING   146   146        Substrate (By similarity). 
BINDING   179   179        NAD; via amide nitrogen (By similarity). 
BINDING   300   300        NAD (By similarity). 
BINDING   329   329        NAD (By similarity). 
MOD_RES   15    15        Phosphoserine. 
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 40874 Da [This is the MW of the unprocessed precursor] CRC64: 7C3AFBC3DFFB470E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVAALNKLS ALSGSIQKSF SPKLISVGII GSGNWGTAIA KICGENAKAH PDIFHPQVHM 

        70         80         90        100        110        120 
WMYEEKIQHE GKECNLTEVF NTTHENVKYL KGIKCPSNVF ANPDIRDVGS RSDILVWVLP 

       130        140        150        160        170        180 
HQFVVRICNQ LKGCLKKDAV AISCIKGVSV TKDRVRLFSD IIEENTGMYC GVLSGANIAS 

       190        200        210        220        230        240 
EVAQEKFCET TIGYLPNSSV NPRYTPKTIQ ALFNRPYFRV NIVEDVPGVA LGGALKNIVA 

       250        260        270        280        290        300 
VAAGIIDGLE LGDNTKSAVM RIGLLEMQKF GRMFFDCKPL TMSEESCGIA DLITTCLGGR 

       310        320        330        340        350        360 
NHKCAVAFVK TGKPMHVVEQ ELLDGQKLQG AATAKEVYEF LDNQNKVSEF PLFTAVYRIV 

       370 
YEGLPPNKLL EAI 

Q09845 in FASTA format

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