Reviewed, UniProtKB/Swiss-Prot P00332 (ADH_SCHPO)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase
    EC=1.1.1.1

Gene names

Name:	adh1
Synonyms:	adh
ORF Names:	SPCC13B11.01

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alcohol metabolic process Inferred by curator. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	Alcohol dehydrogenase		PRO_0000160729
Regions
	Nucleotide binding	180 – 186	7	NAD By similarity
	Nucleotide binding	271 – 273	3	NAD By similarity
Sites
	Metal binding	46	1	Zinc 1; catalytic
	Metal binding	69	1	Zinc 1; catalytic
	Metal binding	100	1	Zinc 2
	Metal binding	103	1	Zinc 2
	Metal binding	106	1	Zinc 2
	Metal binding	114	1	Zinc 2
	Metal binding	156	1	Zinc 1; catalytic
	Binding site	204	1	NAD By similarity
	Binding site	209	1	NAD By similarity
	Binding site	343	1	NAD By similarity
Amino acid modifications
	Modified residue	205	1	Phosphothreonine Ref.4
	Modified residue	250	1	Phosphothreonine Ref.4
Experimental info
	Sequence conflict	237	1	A → C Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P00332-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: F80BE1341F727CC5	FASTA	350	37,396
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J01341 Genomic DNA. No translation available. CU329672 Genomic DNA. Translation: CAA21782.1. AB001834 mRNA. Translation: BAA19458.1.
PIR	DEZPA. A00341.
RefSeq	NP_588244.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P00332.
Genome annotation databases
GeneID	2538902.
GenomeReviews	Gene locus adh1 in contig CU329672_GR.
KEGG	spo:SPCC13B11.01.
NMPDR	fig|4896.1.peg.582.
Organism-specific databases
GeneDB_Spombe	SPCC13B11.01.
Phylogenomic databases
HOGENOM	HBG753318.
OMA	VGDMVGN.
OrthoDB	EOG95HTDV.
Enzyme and pathway databases
BRENDA	1.1.1.1. 653.
Gene expression databases
ArrayExpress	P00332.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADH_SCHPO

Accession

Primary (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 15, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)