Reviewed, UniProtKB/Swiss-Prot P07754 (ADH3_EMENI)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 3
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase III
      Short name=ADH III

Gene names

Name:	alcC
Synonyms:	adh3
ORF Names:	AN2286

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 – 352	352	Alcohol dehydrogenase 3		PRO_0000160721
Regions
	Nucleotide binding	180 – 186	7	NAD By similarity
	Nucleotide binding	273 – 275	3	NAD By similarity
Sites
	Metal binding	44	1	Zinc 1; catalytic By similarity
	Metal binding	67	1	Zinc 1; catalytic By similarity
	Metal binding	100	1	Zinc 2 By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	114	1	Zinc 2 By similarity
	Metal binding	156	1	Zinc 1; catalytic By similarity
	Binding site	204	1	NAD By similarity
	Binding site	209	1	NAD By similarity
	Binding site	345	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P07754-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: AFDE78FE442E3144	FASTA	352	37,126
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular analysis of a third Aspergillus nidulans alcohol dehydrogenase gene." McKnight L., Kato H., Upshall A., Parker M.D., O'Hara P.J., O'Hara S. EMBO J. 4:2093-2099(1985) [PubMed: 2998782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." 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. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X02764 Genomic DNA. Translation: CAA26541.1. AACD01000038 Genomic DNA. Translation: EAA64397.1.
PIR	A24648.
RefSeq	XP_659890.1.
3D structure databases
HSSP	HSSP built from PDB template 1JVB based on UniProtKB P39462.
ModBase	Search...
Genome annotation databases
GeneID	2874791.
KEGG	ani:AN2286.2.
Enzyme and pathway databases
BRENDA	1.1.1.1. 3859.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [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

ADH3_EMENI

Accession

Primary (citable) accession number: P07754
Secondary accession number(s): Q5BAZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	September 22, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)