FADH_PSEAE
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 03-AUG-2022, entry version 125.
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 (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 / 1C /
RC 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: Catalyzes the NAD(+)-dependent oxidation of formaldehyde and
CC acetaldehyde. {ECO:0000250|UniProtKB:P46154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH;
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 + H2O + NAD(+) = acetate + 2 H(+) + NADH;
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}.
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DR EMBL; AE004091; AAG08806.1; -; Genomic_DNA.
DR PIR; E82969; E82969.
DR RefSeq; NP_254108.1; NC_002516.2.
DR RefSeq; WP_003096788.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; Q9HTE3; -.
DR SMR; Q9HTE3; -.
DR STRING; 287.DR97_2798; -.
DR PaxDb; Q9HTE3; -.
DR EnsemblBacteria; AAG08806; AAG08806; 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 OMA; WAKAQSF; -.
DR PhylomeDB; Q9HTE3; -.
DR BioCyc; PAER208964:G1FZ6-5548-MON; -.
DR BRENDA; 1.2.1.46; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014184; HCHO_DH_non_GSH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02819; fdhA_non_GSH; 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"
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..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..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P46154"
FT BINDING 300..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P46154"
FT BINDING 337..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
