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P00332 (ADH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Alcohol dehydrogenase
PRO_0000160729

Regions

Nucleotide binding180 – 1867NAD By similarity
Nucleotide binding271 – 2733NAD By similarity

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
Binding site2041NAD By similarity
Binding site2091NAD By similarity
Binding site3431NAD By similarity

Amino acid modifications

Modified residue2051Phosphothreonine Ref.4
Modified residue2501Phosphothreonine Ref.4

Experimental info

Sequence conflict2371A → C in J01341. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00332 [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

« Hide

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: 972 / ATCC 24843.
[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: 972 / ATCC 24843.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J01341 Genomic DNA. No translation available.
CU329672 Genomic DNA. Translation: CAA21782.1.
AB001834 mRNA. Translation: BAA19458.1.
PIRDEZPA. A00341.
RefSeqNP_588244.1. NM_001023234.1.

3D structure databases

ProteinModelPortalP00332.
SMRP00332. Positions 2-350.
ModBaseSearch...

Protein-protein interaction databases

STRINGP00332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC13B11.01.1; SPCC13B11.01.1:pep; SPCC13B11.01.
GeneID2538902.
GenomeReviewsGene locus adh1 in contig CU329672_GR.
KEGGspo:SPCC13B11.01.
NMPDRfig|4896.1.peg.582.

Organism-specific databases

GeneDB_SpombeSPCC13B11.01.

Phylogenomic databases

eggNOGfuNOG04605.
GeneTreeEFGT00050000001793.
HOGENOMHBG753318.
OMAKSNESNC.
OrthoDBEOG4Q5CZM.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP00332.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK13953.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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: December 14, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents