ADH1_CANAX
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-AUG-2022, entry version 103.
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}.
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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 COMPLUYEAST-2DPAGE; 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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
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
