Reviewed, UniProtKB/Swiss-Prot Q09669 (ADH4_SCHPO)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 4
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase IV

Gene names

Name:	adh4
ORF Names:	SPAC5H10.06c

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	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in ethanol oxidation in mitochondria. Ref.4
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Zinc By similarity.
Subcellular location	Mitochondrion matrix Ref.4 Ref.3.
Induction	Induced in response to zinc deficiency. Ref.5
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to zinc ion starvation Ref.5 Inferred from expression pattern. Source: GeneDB_SPombe glucose catabolic process to ethanol Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Ref.5 Inferred from expression pattern. Source: GeneDB_SPombe zinc ion homeostasis Ref.5 Inferred from expression pattern. Source: GeneDB_SPombe
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alcohol dehydrogenase activity, metal ion-independent Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe 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
	Transit peptide	1 – 29	29	Mitochondrion Potential
	Chain	30 – 422	393	Alcohol dehydrogenase 4		PRO_0000087818

Sequences

	Sequence		Length	Mass (Da)
	Q09669-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C70B56632DBC658E	FASTA	422	45,527
	10 20 30 40 50 60 MSILRSPFRL IRSPARFFPS LFHSSCNQSF TNGLKHQSTS SKAMPVSAFY IPSFNLFGKG 70 80 90 100 110 120 CLAEAAKQIK MSGFKNTLIV TDPGIIKVGL YDKVKALLEE QSITVHLYDG VQPNPTVGNV 130 140 150 160 170 180 NQGLEIVKKE NCDSMVSIGG GSAHDCAKGI ALLATNGGKI ADYEGVDKSS KPQLPLIAIN 190 200 210 220 230 240 TTAGTASEMT RFAIITEETR HIKMAIIDKH TMPILSVNDP ETMYGLPPSL TAATGMDALT 250 260 270 280 290 300 HAVEAYVSTA ANPITDACAV KCIELVNKYL KRAVDNGKDE EARDNMAYAE FLGGMAFNNA 310 320 330 340 350 360 SLGYVHAMAH QLGGFYGIPH GVCNAVLLAH VQKFNSRDPR ANARLGDIAF HLGCEEHTAE 370 380 390 400 410 420 AALDRISQLV LEVKIRPHLV DLGVKEKDFD VLVDHAMKDA CGATNPIQPT HDEVKAIFKS AM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"A distinct type of alcohol dehydrogenase, adh4+, complements ethanol fermentation in an adh1-deficient strain of Schizosaccharomyces pombe." Sakurai M., Tohda H., Kumagai H., Giga-Hama Y. FEMS Yeast Res. 4:649-654(2004) [PubMed: 15040954] [Abstract] Cited for: IDENTIFICATION.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"Identification of a mitochondrial alcohol dehydrogenase in Schizosaccharomyces pombe: new insights into energy metabolism." Crichton P.G., Affourtit C., Moore A.L. Biochem. J. 401:459-464(2007) [PubMed: 16999687] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"Response of Schizosaccharomyces pombe to zinc deficiency." Dainty S.J., Kennedy C.A., Watt S., Baehler J., Whitehall S.K. Eukaryot. Cell 7:454-464(2008) [PubMed: 18203864] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA89956.1.
PIR	S55484.
RefSeq	NP_592819.1.
3D structure databases
SMR	Q09669. Positions 48-422.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09669.
Genome annotation databases
GeneID	2542714.
GenomeReviews	Gene locus adh4 in contig CU329670_GR.
KEGG	spo:SPAC5H10.06c.
NMPDR	fig|4896.1.peg.2789.
Organism-specific databases
GeneDB_Spombe	SPAC5H10.06c.
Phylogenomic databases
eggNOG	fuNOG07707.
HOGENOM	HBG742415.
OMA	GRIQDYE.
OrthoDB	EOG9G1NZS.
PhylomeDB	Q09669.
Enzyme and pathway databases
BRENDA	1.1.1.1. 653.
Gene expression databases
ArrayExpress	Q09669.
Family and domain databases
InterPro	IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view]
Pfam	PF00465. Fe-ADH. 1 hit. [Graphical view]
PROSITE	PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADH4_SCHPO

Accession

Primary (citable) accession number: Q09669

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)