Reviewed, UniProtKB/Swiss-Prot P08843 (ADH1_EMENI)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I
      Short name=ADH I

Gene names

Name:	alcA
ORF Names:	AN8979

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	350 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 – 350	350	Alcohol dehydrogenase 1		PRO_0000160719
Regions
	Nucleotide binding	178 – 184	7	NAD By similarity
	Nucleotide binding	271 – 273	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	98	1	Zinc 2 By similarity
	Metal binding	101	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 2 By similarity
	Metal binding	154	1	Zinc 1; catalytic By similarity
	Binding site	202	1	NAD By similarity
	Binding site	207	1	NAD By similarity
	Binding site	343	1	NAD By similarity
Experimental info
	Sequence conflict	2	1	S → C in AAA33291. Ref.1
	Sequence conflict	146	1	L → V in AAA33291. Ref.1
	Sequence conflict	233 – 239	7	KAATPDG → RHGRGC in AAA33291. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P08843-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 730F216F16217AC4	FASTA	350	37,153
	10 20 30 40 50 60 MSIPTMQWAQ VAEKVGGPLV YKQIPVPKPG PDQILVKIRY SGVCHTDLHA MMGHWPIPVK 70 80 90 100 110 120 MPLVGGHEGA GIVVAKGELV HEFEIGDQAG IKWLNGSCGE CEFCRQSDDP LCARAQLSGY 130 140 150 160 170 180 TVDGTFQQYA LGKASHASKI PAGVPLDAAA PVLCAGITVY KGLKEAGVRP GQTVAIVGAG 190 200 210 220 230 240 GGLGSLAQQY AKAMGIRVVA VDGGDEKRAM CESLGTETYV DFTKSKDLVA DVKAATPDGL 250 260 270 280 290 300 GAHAVILLAV SEKPFQQATE YVRSRGTIVA IGLPPDAYLK APVINTVVRM ITIKGSYVGN 310 320 330 340 350 RQDGVEALDF FARGLIKAPF KTAPLKDLPK IYELMEQGRI AGRYVLEMPE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the cis-acting control regions of two coordinately controlled genes involved in ethanol utilization in Aspergillus nidulans." Gwynne D.I., Buxton F.P., Sibley S., Davies R.W., Lockington R.A., Scazzocchio C., Sealy-Lewis H.M. Gene 51:205-216(1987) [PubMed: 3297923] [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	M16196 Genomic DNA. Translation: AAA33291.1. AACD01000168 Genomic DNA. Translation: EAA64311.1.
PIR	A29054.
RefSeq	XP_682248.1.
3D structure databases
HSSP	HSSP built from PDB template 1JVB based on UniProtKB P39462.
ModBase	Search...
Genome annotation databases
GeneID	2868277.
KEGG	ani:AN8979.2.
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

ADH1_EMENI

Accession

Primary (citable) accession number: P08843
Secondary accession number(s): Q5ARV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	May 1, 2007
Last modified:	September 22, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)