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
