NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2998782 [NCBI, ExPASy, EBI, Israel, Japan]
McKnight L., Kato H., Upshall A., Parker M.D., O'Hara P.J., O'Hara S.;
"Identification and molecular analysis of a third Aspergillus nidulans alcohol dehydrogenase gene.";
EMBO J. 4:2093-2099(1985).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC 4;
DOI=10.1038/nature04341; PubMed=16372000 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

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

X02764; CAA26541.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000038; EAA64397.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24648; A24648.

RefSeq

XP_659890.1; -.

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

ModBase

P07754.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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.

PROSITE

PS00059; ADH_ZINC; 1.

Genome annotation databases

GeneID

2874791; -.

KEGG

ani:AN2286.2; -.

Other

ProtoNet

P07754.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 352`	`352`	`Alcohol dehydrogenase 3.`	`PRO_0000160721`
`NP_BIND`	`180 186`	`7`	`NAD (By similarity).`
`NP_BIND`	`273 275`	`3`	`NAD (By similarity).`
`METAL`	`44 44`		`Zinc 1; catalytic (By similarity).`
`METAL`	`67 67`		`Zinc 1; catalytic (By similarity).`
`METAL`	`100 100`		`Zinc 2 (By similarity).`
`METAL`	`103 103`		`Zinc 2 (By similarity).`
`METAL`	`106 106`		`Zinc 2 (By similarity).`
`METAL`	`114 114`		`Zinc 2 (By similarity).`
`METAL`	`156 156`		`Zinc 1; catalytic (By similarity).`
`BINDING`	`204 204`		`NAD (By similarity).`
`BINDING`	`209 209`		`NAD (By similarity).`
`BINDING`	`345 345`		`NAD (By similarity).`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 37126 Da [This is the MW of the unprocessed precursor]

CRC64: AFDE78FE442E3144 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVPEVQWAQ VVEKAGTPPV YKQVPVPKPG PDEILVKMRY SGVCHTDLHA MKGDWPLPSK 

        70         80         90        100        110        120 
MPLIGGHEGA GVVVAKGELV KDEDFKIGDR AGIKWLNGSC LSCEMCMQAD EPLCPHASLS 

       130        140        150        160        170        180 
GYTVDGTFQQ YTIGKAALAS KIPDNVPLDA AAPILCAGIT VYKGLKESGA RPGQTVAIVG 

       190        200        210        220        230        240 
AGGGLGSLAQ QYAKAMGLRT IAIDSGDEKK AMCEQLGAEV FIDFSKSADV VADVKAATPG 

       250        260        270        280        290        300 
GLGAHAVILL AVAEKPFQQA TEYVRSHGSV VAIGLPANAF LKAPVFTTVV RMINIKGSYV 

       310        320        330        340        350 
GNRQDGVEAL DFFARGLIKA PFKKAPLQDL PQIFELMGQG KIAGRYVLEI PE

P07754 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools