ID FRMA_SYNY3 Reviewed; 369 AA. AC P73138; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 146. 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; OrderedLocusNames=sll0990; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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 --------------------------------------------------------------------------- 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; BA000022; BAA17164.1; -; Genomic_DNA. DR PIR; S75250; S75250. DR AlphaFoldDB; P73138; -. DR SMR; P73138; -. DR STRING; 1148.gene:10498026; -. DR PaxDb; 1148-1652241; -. DR EnsemblBacteria; BAA17164; BAA17164; BAA17164. DR KEGG; syn:sll0990; -. DR eggNOG; COG1062; Bacteria. DR InParanoid; P73138; -. DR PhylomeDB; P73138; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central. DR CDD; cd08300; alcohol_DH_class_III; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR014183; ADH_3. 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 NCBIfam; TIGR02818; adh_III_F_hyde; 1. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..369 FT /note="S-(hydroxymethyl)glutathione dehydrogenase" FT /id="PRO_0000160778" 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; 39211 MW; C8A337424F2F1680 CRC64; MKSRAAVAFE VGKPLQIVEI DVAPPQQGEV LVKITHTGVC HTDAFTLSGD DPEGLFPVVL GHEGAGIVVE VGEGVTSVQL GDHVIPLYTA ECGKCLFCRS GKTNLCVAVR ATQGKGVMPD GTSRFSYNGQ SLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN TAKVQPGDSV AVFGLGGIGL AVVQGARQAK AGRIIAIDTN PAKFELAKQM GATDCINPKD HDQPIQQVIV EMTGWGVDHS FECIGNVEVM RSALECAHRG WGQSVIIGVA GAGQEISTRP FQLVTGRKWM GTAFGGVKGR SQLPGMVEQS MRGEIQLAPF VTHTMELKDI NQAFDLMHDG KSIRSVIHY //