ID FADH_PSEAE Reviewed; 399 AA. AC Q9HTE3; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=Glutathione-independent formaldehyde dehydrogenase; DE Short=FALDH; DE Short=FDH; DE EC=1.2.1.46; GN Name=fdhA; OrderedLocusNames=PA5421; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; 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., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Catalyzes the oxidation of long-chain alcohols but is CC inactive against ethanol (By similarity). CC -!- CATALYTIC ACTIVITY: Formaldehyde + NAD(+) + H(2)O = formate + CC NADH. CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE004091; AAG08806.1; -; Genomic_DNA. DR PIR; E82969; E82969. DR RefSeq; NP_254108.1; -. DR HSSP; P46154; 1KOL. DR SMR; Q9HTE3; 3-398. DR GeneID; 880053; -. DR GenomeReviews; AE004091_GR; PA5421. DR KEGG; pae:PA5421; -. DR PseudoCAP; PA5421; -. DR HOGENOM; Q9HTE3; -. DR OMA; Q9HTE3; VACGRCR. DR BioCyc; PAER208964:PA5421-MON; -. DR BRENDA; 1.2.1.46; 354. DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR014184; HCHO_DH_non_GSH. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR TIGRFAMs; TIGR02819; fdhA_non_GSH; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 399 Glutathione-independent formaldehyde FT dehydrogenase. FT /FTId=PRO_0000287742. FT REGION 172 338 Cofactor-binding. FT METAL 47 47 Zinc 1; catalytic (By similarity). FT METAL 68 68 Zinc 1; catalytic (By similarity). FT METAL 98 98 Zinc 2 (By similarity). FT METAL 101 101 Zinc 2 (By similarity). FT METAL 104 104 Zinc 2 (By similarity). FT METAL 112 112 Zinc 2 (By similarity). FT METAL 177 177 Zinc 1; catalytic (By similarity). 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 //