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FADH_METMR
ID   FADH_METMR              Reviewed;         390 AA.
AC   P47734;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 91.
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;
GN   Name=fdh;
OS   Methylobacter marinus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylobacter.
OX   NCBI_TaxID=34058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A45;
RX   PubMed=7926692; DOI=10.1111/j.1574-6968.1994.tb07125.x;
RA   Speer B.S., Chistoserdova L., Lidstrom M.E.;
RT   "Sequence of the gene for a NAD(P)-dependent formaldehyde dehydrogenase
RT   (class III alcohol dehydrogenase) from a marine methanotroph Methylobacter
RT   marinus A45.";
RL   FEMS Microbiol. Lett. 121:349-355(1994).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: The enzyme is equally active with NAD and NADP.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA65728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L33464; AAA65728.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P47734; -.
DR   SMR; P47734; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR027399; ADH_N_assoc.
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; PF13823; ADH_N_assoc; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..390
FT                   /note="S-(hydroxymethyl)glutathione dehydrogenase"
FT                   /id="PRO_0000160787"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
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"
SQ   SEQUENCE   390 AA;  42221 MW;  3926BE73EDF5713F CRC64;
     MKALCWHGKY DVRVDTVPDP IIVDPTDAIV KITATAICGS DLHLYDGYMP TMESGDILGH
     EPMGEVVEVG SEVTSLKTGD RVVVPFTISC GHCFFCEKTL YSCCDTSNPN ADMARKAMGH
     SPAGIFGYSH MLGGFAGGQA EYLRVPYADV GPIKITSDLP DDKVLFLSDI FPTGYMAAEN
     AQIEPGDTVA VWGCGPVAQF VIQSCWMLGA GRVIAIDRVP ERLTMAQEHG KAEIIDFEEE
     DVYDRLMAMT NGRGPDCCID AVGCEAHGAG SFDAVLDKAK AALYLGTDRP HVLREAIMCC
     RKGGTVSIPG VYVGLLDQLP MGAAMNKGLT LKMGQTHVQR YLEPLLEKIE EDQIDPSFVI
     THSLGLDEGP QAYKTFRDKE DGCIKVVLKP
 
 
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