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UniProtKB/Swiss-Prot entry P36624


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

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Entry information
Entry name DHSO_SCHPO
Primary accession number P36624
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name Putative sorbitol dehydrogenase
Synonyms EC 1.1.1.14
L-iditol 2-dehydrogenase
Protein tms1
Gene name
Name: tms1
ORFNames: SPBC1773.05c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-360.
STRAIN=ATCC 38366 / 972;
PubMed=8223615 [NCBI, ExPASy, EBI, Israel, Japan]
Wagner P., Grimaldi M., Jenkins J.R.;
"Putative dehydrogenase tms1 suppresses growth arrest induced by a p53 tumour mutant in fission yeast.";
Eur. J. Biochem. 217:731-736(1993).
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
CU329671; CAA21910.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X74422; CAA52443.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39670; S35981.
RefSeq NP_595120.1; -.
3D structure databases
HSSP O96496; 1E3J. [HSSP ENTRY / PDB]
ModBase P36624.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003219-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC1773.05c; -.
Gene expression databases
ArrayExpress P36624; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0003939; Molecular function: L-iditol 2-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0033554; Biological process: cellular response to stress (inferred from expression pattern from GeneDB_SPombe).
GO:0019407; Biological process: hexitol catabolic process (inferred by curator from GeneDB_SPombe).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
ProDom PD040557; GroES_related; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00059; ADH_ZINC; 1.
ProtoNet P36624.
Genome annotation databases
GeneID 2540119; -.
KEGG spo:SPBC1773.05c; -.
NMPDR fig|4896.1.peg.986; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   360  360     Putative sorbitol dehydrogenase. PRO_0000160823
METAL   42    42        Zinc; catalytic (By similarity). 
METAL   67    67        Zinc; catalytic (By similarity). 
METAL   68    68        Zinc; catalytic (By similarity). 
Sequence information
Length: 360 AA [This is the length of the unprocessed precursor] Molecular weight: 38851 Da [This is the MW of the unprocessed precursor] CRC64: ADEB3DDBA163224C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPAEKAFVL RKKMDTAIED RPGQTLTDDH QVKVAIKATG ICGSDVHYWK EGGIGDFILK 

        70         80         90        100        110        120 
KPMILGHESA GVVVEVGKGV SSLKPGDPVA VEPGCVCRLC DYCRSGRYNL CPHMEFAATP 

       130        140        150        160        170        180 
PYDGTLRTYY ITTEDFCTKL PKQISVEEGA LFEPMSVAVH AMTRGNLKCG SRVLVMGCGT 

       190        200        210        220        230        240 
VGLLMMAVAK AYGAIDIVAV DASPSRVEFA QKYVGAKPFT PIAAKENESL PDYAQRYKQA 

       250        260        270        280        290        300 
IIEKYGEFDF AVDATGVGIC IHTAVLALKR GGTFVQAGNG KPVIDFPINH IINYEINVLG 

       310        320        330        340        350        360 
SFRYAHGCYK QSLFLVSNGL VDVKPLITHR FAFKDALKAY ETVASGEEGV LKVIIGGPDA 

P36624 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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