ID ADH1_PICST Reviewed; 348 AA. AC O00097; A3LNN7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 16-JUN-2009, entry version 52. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase I; DE AltName: Full=ADH 2; GN Name=ADH1; Synonyms=ADH2; ORFNames=PICST_68558; OS Pichia stipitis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia. OX NCBI_TaxID=4924; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; RX MEDLINE=98207839; PubMed=9546172; RA Cho J.Y., Jeffries T.W.; RT "Pichia stipitis genes for alcohol dehydrogenase with fermentative and RT respiratory functions."; RL Appl. Environ. Microbiol. 64:1350-1358(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542; RX MEDLINE=99019018; PubMed=9802210; RX DOI=10.1002/(SICI)1097-0061(1998100)14:14<1311::AID-YEA315>3.3.CO;2-K; RA Passoth V., Schaefer B., Liebel B., Weierstall T., Klinner U.; RT "Molecular cloning of alcohol dehydrogenase genes of the yeast Pichia RT stipitis and identification of the fermentative ADH."; RL Yeast 14:1311-1325(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose- RT fermenting yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). CC -!- FUNCTION: Converts ethanol to acetaldehyde and plays a major role CC in xylose fermentation. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). 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; AF008245; AAC49991.1; -; Genomic_DNA. DR EMBL; Y13397; CAA73827.1; -; Genomic_DNA. DR EMBL; CP000496; ABN64893.1; -; Genomic_DNA. DR RefSeq; XP_001382922.1; -. DR HSSP; P39462; 1JVB. DR SMR; O00097; 2-348. DR GeneID; 4836752; -. DR KEGG; pic:PICST_68558; -. DR OMA; O00097; ATDGGPH. DR BRENDA; 1.1.1.1; 81766. 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 Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; KW Zinc. FT CHAIN 1 348 Alcohol dehydrogenase 1. FT /FTId=PRO_0000160727. FT NP_BIND 178 184 NAD (By similarity). FT NP_BIND 269 271 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 341 341 NAD (By similarity). SQ SEQUENCE 348 AA; 36520 MW; 49C06B545D5350F4 CRC64; MSVPTTQKAV VFESNGGPLL YKDIPVPTPK PNEILINVKY SGVCHTDLHA WKGDWPLDTK LPLVGGHEGA GVVVGIGSNV TGWELGDYAG IKWLNGSCLN CEFCQHSDEP NCAKADLSGY THDGSFQQYA TADAVQAARL PKGTDLAQAA PILCAGITVY KALKTAQIQP GNWVCISGAG GGLGSLAIQY AKAMGFRVIA IDGGEEKGEF VKSLGAEAYV DFTVSKDIVK DIQTATDGGP HAAINVSVSE KAIAQSCQYV RSTGTVVLVG LPAGAKVVAP VFDAVVKSIS IRGSYVGNRA DSAEAIDFFT RGLIKCPIKV VGLSELPKVY ELMEAGKVIG RYVVDTSK //