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UniProtKB/Swiss-Prot entry P08843


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADH1_EMENI
Primary accession number P08843
Secondary accession number Q5ARV1
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on May 1, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 60)
Name and origin of the protein
Protein name Alcohol dehydrogenase 1
Synonyms EC 1.1.1.1
Alcohol dehydrogenase I
ADH I
Gene name
Name: alcA
ORFNames: AN8979
From
Emericella nidulans (Aspergillus nidulans) [TaxID: 162425] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(87)90309-X; PubMed=3297923 [NCBI, ExPASy, EBI, Israel, Japan]
Gwynne D.I., Buxton F.P., Sibley S., Davies R.W., Lockington R.A., Scazzocchio C., Sealy-Lewis H.M.;
"Comparison of the cis-acting control regions of two coordinately controlled genes involved in ethanol utilization in Aspergillus nidulans.";
Gene 51:205-216(1987).
[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
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
M16196; AAA33291.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AACD01000168; EAA64311.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29054; A29054.
RefSeq XP_682248.1; -.
3D structure databases
HSSP P39462; 1JVB. [HSSP ENTRY / PDB]
ModBase P08843.
Ontologies
GO
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 UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
Genome annotation databases
GeneID 2868277; -.
KEGG ani:AN8979.2; -.
Other
ProtoNet P08843.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   350  350     Alcohol dehydrogenase 1. PRO_0000160719
NP_BIND   178   184  7     NAD (By similarity). 
NP_BIND   271   273  3     NAD (By similarity). 
METAL   44    44        Zinc 1; catalytic (By similarity). 
METAL   67    67        Zinc 1; catalytic (By similarity). 
METAL   98    98        Zinc 2 (By similarity). 
METAL   101   101        Zinc 2 (By similarity). 
METAL   104   104        Zinc 2 (By similarity). 
METAL   112   112        Zinc 2 (By similarity). 
METAL   154   154        Zinc 1; catalytic (By similarity). 
BINDING   202   202        NAD (By similarity). 
BINDING   207   207        NAD (By similarity). 
BINDING   343   343        NAD (By similarity). 
CONFLICT   2     2        S -> C (in Ref. 1; AAA33291). 
CONFLICT   146   146        L -> V (in Ref. 1; AAA33291). 
CONFLICT   233   239        KAATPDG -> RHGRGC (in Ref. 1; AAA33291). 
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 37153 Da [This is the MW of the unprocessed precursor] CRC64: 730F216F16217AC4 [This is a checksum on the sequence]
        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 

P08843 in FASTA format

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