ID ADH1_EMENI STANDARD; PRT; 349 AA. AC P08843; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Alcohol dehydrogenase I (EC 1.1.1.1) (ADH I). GN Name=alcA; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. 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). 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: Cytoplasmic. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M16196; AAA33291.1; -. DR PIR; A29054; A29054. DR HSSP; P39462; 1JVB. DR InterPro; IPR002328; ADH_zinc. DR InterPro; IPR002085; Adh_zn_family. DR InterPro; IPR011032; GroES_like. DR Pfam; PF00107; ADH_zinc_N; 1. DR PROSITE; PS00059; ADH_ZINC; 1. KW Metal-binding; Multigene family; NAD; Oxidoreductase; Zinc. FT METAL 44 44 Zinc 1 (catalytic). FT METAL 67 67 Zinc 1 (catalytic). FT METAL 98 98 Zinc 2. FT METAL 101 101 Zinc 2. FT METAL 104 104 Zinc 2. FT METAL 112 112 Zinc 2. FT METAL 154 154 Zinc 1 (catalytic). SQ SEQUENCE 349 AA; 37181 MW; 23AB655D459E7B2C CRC64; MCIPTMQWAQ VAEKVGGPLV YKQIPVPKPG PDQILVKIRY SGVCHTDLHA MMGHWPIPVK MPLVGGHEGA GIVVAKGELV HEFEIGDQAG IKWLNGSCGE CEFCRQSDDP LCARAQLSGY TVDGTFQQYA LGKASHASKI PAGVPVDAAA PVLCAGITVY KGLKEAGVRP GQTVAIVGAG GGLGSLAQQY AKAMGIRVVA VDGGDEKRAM CESLGTETYV DFTKSKDLVA DVRHGRGCLG AHAVILLAVS EKPFQQATEY VRSRGTIVAI GLPPDAYLKA PVINTVVRMI TIKGSYVGNR QDGVEALDFF ARGLIKAPFK TAPLKDLPKI YELMEQGRIA GRYVLEMPE //