FRMA_PHODP
ID FRMA_PHODP Reviewed; 369 AA.
AC P39450;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284;
DE AltName: Full=Alcohol dehydrogenase class-3;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase class-III;
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE Short=GSH-FDH;
DE EC=1.1.1.-;
GN Name=frmA;
OS Photobacterium damsela subsp. piscicida (Pasteurella piscicida).
OG Plasmid R {ECO:0000303|PubMed:8052160}.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=38294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8052160; DOI=10.1111/j.1348-0421.1994.tb01741.x;
RA Kim E.H., Aoki T.;
RT "The transposon-like structure of IS26-tetracycline, and kanamycin
RT resistance determinant derived from transferable R plasmid of fish
RT pathogen, Pasteurella piscicida.";
RL Microbiol. Immunol. 38:31-38(1994).
RN [2]
RP IDENTIFICATION, AND CONCEPTUAL TRANSLATION.
RA Rudd K.E., Bairoch A.;
RL Unpublished observations (NOV-1994).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 -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03719.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D16172; BAA03719.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; YP_003023972.1; NC_012919.1.
DR RefSeq; YP_908417.1; NC_008612.1.
DR RefSeq; YP_908601.1; NC_008613.1.
DR AlphaFoldDB; P39450; -.
DR SMR; P39450; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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 InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 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 Cytoplasm; Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.
FT CHAIN 1..369
FT /note="S-(hydroxymethyl)glutathione dehydrogenase"
FT /id="PRO_0000160777"
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 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 39094 MW; ACAEA4581048901C CRC64;
MKSRAAVAFG PGLPLEIVEI DVAPPKKGEV LVKISHTGVC HTDAYTLSGD DPEGLFPVVL
GHEGAGVVVE VGEGVTSVKP GDHVIPLYTA ECGECDFCTS GKTNLCVAVR ETQGKGVMPD
ATSRFFVNGQ PLYHYMGCST FSEYTVVAEV SLAKINPQAN AEQVCLLGCG VTTGIGAVHN
TAKVQEGDSV AVFGLGGIGL AVVQGARQAK AGRIFAIDTN PSKFELAKQF GATDCINPND
YDKPVQQVLV EMTKWGVDHT FECIGNVNVM RSALESAHRG WGQSVIIGVA GAGKEISTRP
FQLVTGRVWK GTAFGGVKGR TQLPGMVEDA MSGKIELAPF VTHTMELDKI NEAFDLMHDG
KSIRTVIHY
