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Reviewed, UniProtKB/Swiss-Prot P00332 (ADH_SCHPO)

Last modified November 25, 2008. Version 79. 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

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase
    EC=1.1.1.1
Gene names
Name: adh1
Synonyms: adh
ORF Names: SPCC13B11.01
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

An alcohol + NAD(+) = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Ontologies

Keywords

   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processcellular alcohol metabolic process

Inferred by curator. Source: GeneDB_SPombe

oxidation reduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Alcohol dehydrogenase
PRO_0000160729

Sites

Metal binding461Zinc 1; catalytic
Metal binding691Zinc 1; catalytic
Metal binding1001Zinc 2
Metal binding1031Zinc 2
Metal binding1061Zinc 2
Metal binding1141Zinc 2
Metal binding1561Zinc 1; catalytic

Amino acid modifications

Modified residue2051Phosphothreonine
Modified residue2501Phosphothreonine

Experimental info

Sequence conflict2371A → C Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P00332-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: F80BE1341F727CC5

FASTA35037,396
        10         20         30         40         50         60 
MTIPDKQLAA VFHTHGGPEN VKFEEVPVAE PGQDEVLVNI KYTGVCHTDL HALQGDWPLP 

        70         80         90        100        110        120 
AKMPLIGGHE GAGVVVKVGA GVTRLKIGDR VGVKWMNSSC GNCEYCMKAE ETICPHIQLS 

       130        140        150        160        170        180 
GYTVDGTFQH YCIANATHAT IIPESVPLEV AAPIMCAGIT CYRALKESKV GPGEWICIPG 

       190        200        210        220        230        240 
AGGGLGHLAV QYAKAMAMRV VAIDTGDDKA ELVKSFGAEV FLDFKKEADM IEAVKAATNG 

       250        260        270        280        290        300 
GAHGTLVLST SPKSYEQAAG FARPGSTMVT VSMPAGAKLG ADIFWLTVKM LKICGSHVGN 

       310        320        330        340        350 
RIDSIEALEY VSRGLVKPYY KVQPFSTLPD VYRLMHENKI AGRIVLDLSK

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References

« Hide 'large scale' references
[1]"The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe."
Russell P.R., Hall B.D.
J. Biol. Chem. 258:143-149(1983) [PubMed: 6294096] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38366 / 972.
[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. 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.
[3]"S.pombe adh 3' region."
Kawamukai M.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-350.
[4]"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 THR-205 AND THR-250, MASS SPECTROMETRY.

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Cross-references

Sequence databases

J01341 Genomic DNA. No translation available.
CU329672 Genomic DNA. Translation: CAA21782.1.
AB001834 mRNA. Translation: BAA19458.1.
PIRDEZPA. A00341.
RefSeqNP_588244.1.

3D structure databases

HSSPHSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBaseSearch...

Genome annotation databases

GeneID2538902.
KEGGspo:SPCC13B11.01.
NMPDRfig|4896.1.peg.582.

Organism-specific databases

GeneDB_SpombeSPCC13B11.01.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000175-MON.

Gene expression databases

ArrayExpressP00332.

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR002328. AlcDHase_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProDomPD004105. DapB. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADH_SCHPO
AccessionPrimary (citable) accession number: P00332
Secondary accession number(s): Q9URT7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 11, 2001
Last modified: November 25, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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