FADH_CANMA
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 03-AUG-2022, entry version 98.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284;
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE Short=FLD;
DE Short=GSH-FDH;
DE EC=1.1.1.-;
GN Name=FDH1; Synonyms=ADH1;
OS Candida maltosa (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=899;
RX 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 resistance to
RT formaldehyde in Saccharomyces cerevisiae.";
RL Gene 122:207-211(1992).
CC -!- FUNCTION: Confers resistance to formaldehyde.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; M58332; AAA34344.1; -; Genomic_DNA.
DR PIR; JN0447; JN0447.
DR AlphaFoldDB; Q06099; -.
DR SMR; Q06099; -.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 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
FT /note="S-(hydroxymethyl)glutathione dehydrogenase"
FT /id="PRO_0000160781"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
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
