ID ADH1_EMENI Reviewed; 350 AA. AC P08843; Q5ARV1; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 16-JUN-2009, entry version 65. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase I; DE Short=ADH I; GN Name=alcA; ORFNames=AN8979; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87248079; PubMed=3297923; DOI=10.1016/0378-1119(87)90309-X; RA Gwynne D.I., Buxton F.P., Sibley S., Davies R.W., Lockington R.A., RA Scazzocchio C., Sealy-Lewis H.M.; RT "Comparison of the cis-acting control regions of two coordinately RT controlled genes involved in ethanol utilization in Aspergillus RT nidulans."; RL Gene 51:205-216(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC 4; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M16196; AAA33291.1; -; Genomic_DNA. DR EMBL; AACD01000168; EAA64311.1; -; Genomic_DNA. DR PIR; A29054; A29054. DR RefSeq; XP_682248.1; -. DR HSSP; P39462; 1JVB. DR GeneID; 2868277; -. DR KEGG; ani:AN8979.2; -. DR BRENDA; 1.1.1.1; 3859. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR002328; ADH_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1 350 Alcohol dehydrogenase 1. FT /FTId=PRO_0000160719. FT NP_BIND 178 184 NAD (By similarity). FT NP_BIND 271 273 NAD (By similarity). FT METAL 44 44 Zinc 1; catalytic (By similarity). FT METAL 67 67 Zinc 1; catalytic (By similarity). FT METAL 98 98 Zinc 2 (By similarity). FT METAL 101 101 Zinc 2 (By similarity). FT METAL 104 104 Zinc 2 (By similarity). FT METAL 112 112 Zinc 2 (By similarity). FT METAL 154 154 Zinc 1; catalytic (By similarity). FT BINDING 202 202 NAD (By similarity). FT BINDING 207 207 NAD (By similarity). FT BINDING 343 343 NAD (By similarity). FT CONFLICT 2 2 S -> C (in Ref. 1; AAA33291). FT CONFLICT 146 146 L -> V (in Ref. 1; AAA33291). FT CONFLICT 233 239 KAATPDG -> RHGRGC (in Ref. 1; AAA33291). SQ SEQUENCE 350 AA; 37153 MW; 730F216F16217AC4 CRC64; MSIPTMQWAQ VAEKVGGPLV YKQIPVPKPG PDQILVKIRY SGVCHTDLHA MMGHWPIPVK MPLVGGHEGA GIVVAKGELV HEFEIGDQAG IKWLNGSCGE CEFCRQSDDP LCARAQLSGY TVDGTFQQYA LGKASHASKI PAGVPLDAAA PVLCAGITVY KGLKEAGVRP GQTVAIVGAG GGLGSLAQQY AKAMGIRVVA VDGGDEKRAM CESLGTETYV DFTKSKDLVA DVKAATPDGL GAHAVILLAV SEKPFQQATE YVRSRGTIVA IGLPPDAYLK APVINTVVRM ITIKGSYVGN RQDGVEALDF FARGLIKAPF KTAPLKDLPK IYELMEQGRI AGRYVLEMPE //