ID   FADH_CANMA              Reviewed;         381 AA.
AC   Q06099;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE            EC=1.1.1.284;
DE   AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE            Short=GSH-FDH;
DE            Short=FALDH;
DE            Short=FDH;
DE            Short=FLD;
DE            EC=1.1.1.-;
GN   Name=FDH1; Synonyms=ADH1;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=899;
RX   MEDLINE=93083986; PubMed=1339376; DOI=10.1016/0378-1119(92)90052-Q;
RA   Sasnauskas K., Jomantiene R., Januska A., Lebediene E., Lebedys J.,
RA   Janulaitis A.;
RT   "Cloning and analysis of a Candida maltosa gene which confers
RT   resistance to formaldehyde in Saccharomyces cerevisiae.";
RL   Gene 122:207-211(1992).
CC   -!- FUNCTION: Confers resistance to formaldehyde.
CC   -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S-
CC       formylglutathione + NAD(P)H.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily.
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; M58332; AAA34344.1; -; Genomic_DNA.
DR   PIR; JN0447; JN0447.
DR   HSSP; P11766; 1M6H.
DR   BRENDA; 1.1.1.284; 3846.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase ...; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR014183; ADH_3.
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   TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    381       S-(hydroxymethyl)glutathione
FT                                dehydrogenase.
FT                                /FTId=PRO_0000160781.
FT   METAL        49     49       Zinc 1; catalytic (By similarity).
FT   METAL        71     71       Zinc 1; catalytic (By similarity).
FT   METAL       101    101       Zinc 2 (By similarity).
FT   METAL       104    104       Zinc 2 (By similarity).
FT   METAL       107    107       Zinc 2 (By similarity).
FT   METAL       115    115       Zinc 2 (By similarity).
FT   METAL       178    178       Zinc 1; catalytic (By similarity).
SQ   SEQUENCE   381 AA;  40075 MW;  F09E01BC65DAD0C7 CRC64;
     MSESTVGKPI TCKAAVAWEA AKPLSIEDVT VAPPKRHEVR IKLYDTGVCH TDAYTLSGVD
     PEGAFPVILG HEGAGIVESI GEGVTNVKVG DHVIALYTPE CGECKFCKSG KTNLCGKIRA
     TQGKGVMPDG TSRFTCKGKE ILHFMGCSTF SQYTVVADIS VVAINPKAEF DKACLLGCGI
     TTGYGAATIT ANVQKGDNVA VFGGGIVGLS VIQGCAERGA AQIILVDISD KKEEWGQKLG
     ATAFVNPTKL PEGTTIVDKL IEMTDGGCDF TFDCTGNVGV MRNALEACHK GWGTSVIIGV
     AAAGKEISTR PFQLVTGRTW KGAAFGGVKG RSQLPGIVNN YLDGKLKVEE FITHREPLAA
     INKAFEEMHA GDCIRAVVDL S
//