ID ADH1_CANAX Reviewed; 350 AA. AC P43067; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 03-MAY-2023, entry version 106. DE RecName: Full=Alcohol dehydrogenase 1; DE EC=1.1.1.1; DE AltName: Full=40 kDa allergen; DE AltName: Full=Allergen Can a 1; DE AltName: Full=Allergen Can a I; DE AltName: Allergen=Cand a 1; GN Name=ADH1; Synonyms=CAD; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8686375; RX DOI=10.1002/(sici)1097-0061(199602)12:2<115::aid-yea889>3.0.co;2-e; RA Bertram G., Swoboda R.K., Gooday G.W., Gow N.A.R., Brown A.J.P.; RT "Structure and regulation of the Candida albicans ADH1 gene encoding an RT immunogenic alcohol dehydrogenase."; RL Yeast 12:115-127(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=B311A; RA Pendrak M.L., Klotz S.A., Smith R.L.; RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-313. RX PubMed=1777830; DOI=10.1111/j.1365-2222.1991.tb03195.x; RA Shen H.D., Choo K.B., Lee H.H., Hsieh J.C., Lin W.L., Lee W.R., Han S.H.; RT "The 40-kilodalton allergen of Candida albicans is an alcohol RT dehydrogenase: molecular cloning and immunological analysis using RT monoclonal antibodies."; RL Clin. Exp. Allergy 21:675-681(1991). CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X81694; CAA57342.1; -; Genomic_DNA. DR EMBL; U15924; AAA53300.1; -; mRNA. DR PIR; S63781; S52153. DR AlphaFoldDB; P43067; -. DR SMR; P43067; -. DR Allergome; 177; Cand a 1. DR Allergome; 3173; Cand a 1.0101. DR MoonDB; P43067; Curated. DR MoonProt; P43067; -. DR VEuPathDB; FungiDB:C5_05050W_A; -. DR VEuPathDB; FungiDB:CAWG_04871; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd08297; CAD3; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1. DR PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-RELATED; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. DR COMPLUYEAST-2DPAGE; P43067; -. PE 1: Evidence at protein level; KW Allergen; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1..350 FT /note="Alcohol dehydrogenase 1" FT /id="PRO_0000160717" FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 180..186 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 209 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 271..273 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 343 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT CONFLICT 39 FT /note="H -> N (in Ref. 2; AAA53300)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="R -> W (in Ref. 2; AAA53300)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="A -> T (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="F -> L (in Ref. 2; AAA53300)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="D -> A (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="R -> S (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="D -> E (in Ref. 2; AAA53300)" FT /evidence="ECO:0000305" SQ SEQUENCE 350 AA; 36879 MW; C3DFE2E70F42D634 CRC64; MSEQIPKTQK AVVFDTNGGQ LVYKDYPVPT PKPNELLIHV KYSGVCHTDL HARKGDWPLA TKLPLVGGHE GAGVVVGMGE NVKGWKIGDF AGIKWLNGSC MSCEFCQQGA EPNCGEADLS GYTHDGSFEQ YATADAVQAA KIPAGTDLAN VAPILCAGVT VYKALKTADL AAGQWVAISG AGGGLGSLAV QYARAMGLRV VAIDGGDEKG EFVKSLGAEA YVDFTKDKDI VEAVKKATDG GPHGAINVSV SEKAIDQSVE YVRPLGKVVL VGLPAHAKVT APVFDAVVKS IEIKGSYVGN RKDTAEAIDF FSRGLIKCPI KIVGLSDLPE VFKLMEEGKI LGRYVLDTSK //