ID ADH1_KLULA Reviewed; 350 AA. AC P20369; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 25-NOV-2008, entry version 57. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase I; GN Name=ADH1; OrderedLocusNames=KLLA0F21010g; OS Kluyveromyces lactis (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90273773; PubMed=2190430; DOI=10.1002/yea.320060304; RA Saliola M., Shuster J.R., Falcone C.; RT "The alcohol dehydrogenase system in the yeast, Kluyveromyces RT lactis."; RL Yeast 6:193-204(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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; CR382126; CAG98731.1; -; Genomic_DNA. DR PIR; S09475; S09475. DR RefSeq; XP_456023.1; -. DR HSSP; P39462; 1JVB. DR SMR; P20369; 4-350. DR GeneID; 2895056; -. DR KEGG; kla:KLLA0F21010g; -. DR HOGENOM; P20369; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:InterPro. DR InterPro; IPR013154; AlcDHase_GroES-like. DR InterPro; IPR002085; AlcDHase_SF_Zn. DR InterPro; IPR013149; AlcDHase_Zn-bd. DR InterPro; IPR002328; AlcDHase_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 Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; KW Zinc. FT CHAIN 1 350 Alcohol dehydrogenase 1. FT /FTId=PRO_0000160722. FT METAL 46 46 Zinc 1; catalytic. FT METAL 69 69 Zinc 1; catalytic. FT METAL 100 100 Zinc 2. FT METAL 103 103 Zinc 2. FT METAL 106 106 Zinc 2. FT METAL 114 114 Zinc 2. FT METAL 156 156 Zinc 1; catalytic. SQ SEQUENCE 350 AA; 37261 MW; 3D71BE2D5CC86119 CRC64; MAASIPETQK GVIFYENGGE LQYKDIPVPK PKANELLINV KYSGVCHTDL HAWKGDWPLP TKLPLVGGHE GAGVVVAMGE NVKGWKIGDF AGIKWLNGSC MSCEYCELSN ESNCPEADLS GYTHDGSFQQ YATADAVQAA KIPVGTDLAE VAPVLCAGVT VYKALKSANL KAGDWVAISG AAGGLGSLAV QYAKAMGYRV LGIDAGEEKA KLFKDLGGEY FIDFTKSKNI PEEVIEATKG GAHGVINVSV SEFAIEQSTN YVRSNGTVVL VGLPRDAKCK SDVFNQVVKS ISIVGSYVGN RADTREAIDF FSRGLVKAPI HVVGLSELPS IYEKMEKGAI VGRYVVDTSK //