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UniProtKB/Swiss-Prot entry Q9P6C8


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

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Entry information
Entry name ADH1_NEUCR
Primary accession number Q9P6C8
Secondary accession number Q7RV68
Integrated into Swiss-Prot on June 1, 2001
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 61)
Name and origin of the protein
Protein name Alcohol dehydrogenase 1
Synonyms EC 1.1.1.1
Alcohol dehydrogenase I
Gene name
Name: adh-1
ORFNames: B17C10.210, NCU01754
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1093/nar/gkg293; PubMed=12655011 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
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
AL355926; CAB91241.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000005; EAA27941.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T49440; T49440.
RefSeq XP_957177.1; -.
3D structure databases
HSSP P39462; 1JVB. [HSSP ENTRY / PDB]
ModBase Q9P6C8.
Enzyme and pathway databases
BioCyc NCRA-XX3-01:NCRA-XX3-01-005464-MON; -.
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 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.
ProtoNet Q9P6C8.
Genome annotation databases
GeneID 3873329; -.
KEGG ncr:NCU01754; -.
NMPDR fig|5141.1.peg.6126; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   353  353     Alcohol dehydrogenase 1. PRO_0000160726
METAL   47    47        Zinc 1; catalytic (By similarity). 
METAL   70    70        Zinc 1; catalytic (By similarity). 
METAL   101   101        Zinc 2 (By similarity). 
METAL   104   104        Zinc 2 (By similarity). 
METAL   107   107        Zinc 2 (By similarity). 
METAL   115   115        Zinc 2 (By similarity). 
METAL   157   157        Zinc 1; catalytic (By similarity). 
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 37443 Da [This is the MW of the unprocessed precursor] CRC64: 66B71D891324C854 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPQFEIPEQQ WAQVVEKKGG PVVFKQIPVQ KPGPDEVLIN VKYSGVCHTD LHAMKGDWPL 

        70         80         90        100        110        120 
ATKMPLVGGH EGAGVVVAKG ELVTEVEVGD HAGIKWLNGS CLACSFCMQA DEPLCPHALL 

       130        140        150        160        170        180 
SGYTVDGSFQ QYAIAKAAHV AKIPKGCDLE TTAPVLCAGI TVYKGLKESG VRPGQCVAIV 

       190        200        210        220        230        240 
GAGGGLGSMA IQYANAMGLH AIAIDGGEEK GKNCRELGAQ AYVDFTTTKD LVADVKAATP 

       250        260        270        280        290        300 
DGLGPHAVIL LAVSEKPFHQ AVDYVRSRGT IICIGLPAGA KFQAPVFDTV IRMITIKGSY 

       310        320        330        340        350 
VGNRQDTQEA LDFFARGLIK VPIKTVGLSK LQEVYDLMEE GKIVGRYVVD TSK 

Q9P6C8 in FASTA format

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