ID FALDH_PSEAE Reviewed; 399 AA. AC Q9HTE3; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 02-SEP-2026, entry version 140. DE RecName: Full=Glutathione-independent formaldehyde dehydrogenase {ECO:0000250|UniProtKB:P46154}; DE Short=FALDH; DE Short=FDH; DE EC=1.2.1.46 {ECO:0000250|UniProtKB:P46154}; GN Name=fdhA; OrderedLocusNames=PA5421; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Dehydrogenase that catalyzes the NAD(+)-dependent oxidation CC of formaldehyde and acetaldehyde. {ECO:0000250|UniProtKB:P46154}. CC -!- CATALYTIC ACTIVITY: CC Reaction=formaldehyde + NAD(+) + H2O = formate + NADH + 2 H(+); CC Xref=Rhea:RHEA:16425, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.46; CC Evidence={ECO:0000250|UniProtKB:P46154}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetaldehyde + NAD(+) + H2O = acetate + NADH + 2 H(+); CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P46154}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P46154}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P46154}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P46154}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {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; AE004091; AAG08806.1; -; Genomic_DNA. DR PIR; E82969; E82969. DR RefSeq; NP_254108.1; NC_002516.2. DR RefSeq; WP_003096788.1; NC_002516.2. DR AlphaFoldDB; Q9HTE3; -. DR SMR; Q9HTE3; -. DR STRING; 208964.PA5421; -. DR PaxDb; 208964-PA5421; -. DR GeneID; 880053; -. DR KEGG; pae:PA5421; -. DR PATRIC; fig|208964.12.peg.5681; -. DR PseudoCAP; PA5421; -. DR HOGENOM; CLU_026673_11_3_6; -. DR InParanoid; Q9HTE3; -. DR OrthoDB; 9773078at2; -. DR PhylomeDB; Q9HTE3; -. DR BioCyc; PAER208964:G1FZ6-5548-MONOMER; -. DR BRENDA; 1.2.1.46; 5087. DR Proteomes; UP000002438; Chromosome. DR AbasyAtlas; Q9HTE3; -. DR GO; GO:0140087; F:acetaldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0018467; F:formaldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd08282; PFDH_like; 1. DR FunFam; 3.40.50.720:FF:000166; Glutathione-independent formaldehyde dehydrogenase; 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; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR014184; HCHO_DH_non_GSH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02819; fdhA_non_GSH; 1. DR PANTHER; PTHR42813:SF3; GLUTATHIONE-INDEPENDENT FORMALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P46154" FT CHAIN 2..399 FT /note="Glutathione-independent formaldehyde dehydrogenase" FT /id="PRO_0000287742" FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 48 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 49 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 52 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 112 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P46154" 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|UniProtKB:P46154" FT BINDING 198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 218 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 223 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 263 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 268 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 270 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 300 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 337 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" FT BINDING 339 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P46154" SQ SEQUENCE 399 AA; 42008 MW; FE1FBAE68A90C9FC CRC64; MSGNRGVVYL GPGKVEVQNI PYPKMQDPQG RQIDHGVILR VVSTNICGSD QHMVRGRTTA PEGLVLGHEI TGEVVEIGRG VETMKIGDLV SVPFNVACGH CRTCKEQHTG VCLTVNPARA GGAYGYVDMG GWVGGQAEYV LVPYADFNLL KLPNREAAME KIRDLTCLSD ILPTGYHGAV TAGVGPGSTV YIAGAGPVGL AAAASARLLG AAVVIVGDVN PTRLAHAKKQ GFEIADLSKD TPLHEQIAAL LGEPEVDCAV DAVGFEARGH GHSGSQQEAP ATVLNSLMGI TRVAGKIGIP GLYVTEDPGA VDAAAKHGAL SIRFGLGWAK SHSFHTGQTP VMKYNRQLMQ AIMWDRIKIA DIVGVEVITL DDAPKGYGEF DAGVPKKFVI DPHNLFRAA //