FADH_PARDE
ID FADH_PARDE Reviewed; 375 AA.
AC P45382;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, 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=GSH-FDH;
DE EC=1.1.1.-;
GN Name=flhA;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
RX PubMed=7798140; DOI=10.1128/jb.177.1.247-251.1995;
RA Ras J., van Ophem P.W., Reijnders W.N.M., van Spanning R.J.M., Duine J.A.,
RA Stouthamer A.H., Harms N.;
RT "Isolation, sequencing, and mutagenesis of the gene encoding NAD- and
RT glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus
RT denitrificans, in which GD-FALDH is essential for methylotrophic growth.";
RL J. Bacteriol. 177:247-251(1995).
CC -!- FUNCTION: Essential for the oxidation of formaldehyde produced during
CC methylotrophic growth.
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 -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U34346; AAC44551.1; -; Genomic_DNA.
DR EMBL; L36327; AAA65962.1; -; Genomic_DNA.
DR AlphaFoldDB; P45382; -.
DR SMR; P45382; -.
DR KEGG; ag:AAC44551; -.
DR BioCyc; MetaCyc:MON-4081; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..375
FT /note="S-(hydroxymethyl)glutathione dehydrogenase"
FT /id="PRO_0000160779"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
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 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 39919 MW; D3A41572C1F26424 CRC64;
MRTRAAVALE AGKPLEVMEV NLEGPKAGEV MVEIKATGIC HTDEFTLSGA DPEGLFPSIL
GHEGAGVVVE VGPGVTSVKP GNHVIPLYTP ECRQCASCLS GKTNLCTAIR ATQGQGLMPD
GTSRFSMLDG TPIFHYMGCS TFSNYTVLPE IAVAKVREDA PFDKICYIGC GVTTGIGAVI
NTAKVEIGAK AVVFGLGGIG LNVLQGLRLA GADMIIGVDL NDDKKPMAEH FGMTHFINPK
NCENVVQEIV NLTKTPFDQI GGADYSFDCT GNVKVMRDAL ECTHRGWGQS IIIGVAPAGA
EISTRPFQLV TGRVWKGTAF GGARGRTDVP QIVDWYMDGK IEIDPMITHT LSLDDINKGF
DLMHAGESIR SVVLY
