FADH_PSEPU
ID FADH_PSEPU Reviewed; 399 AA.
AC P46154;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glutathione-independent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE EC=1.2.1.46 {ECO:0000269|PubMed:6526822, ECO:0000269|PubMed:9059646};
DE AltName: Full=Formaldehyde dismutase;
DE EC=1.2.98.1 {ECO:0000269|PubMed:6526822, ECO:0000269|PubMed:9059646};
GN Name=fdhA;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=C-83;
RX PubMed=8169197; DOI=10.1128/jb.176.9.2483-2491.1994;
RA Ito K., Takahashi M., Yoshimoto T., Tsuru D.;
RT "Cloning and high-level expression of the glutathione-independent
RT formaldehyde dehydrogenase gene from Pseudomonas putida.";
RL J. Bacteriol. 176:2483-2491(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=C-83;
RX PubMed=6526822; DOI=10.1093/oxfordjournals.jbchem.a134988;
RA Ogushi S., Ando M., Tsuru D.;
RT "Formaldehyde dehydrogenase from Pseudomonas putida: a zinc
RT metalloenzyme.";
RL J. Biochem. 96:1587-1591(1984).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9059646;
RA Oppenheimer N.J., Henehan G.T., Huete-Perez J.A., Ito K.;
RT "P. putida formaldehyde dehydrogenase. An alcohol dehydrogenase
RT masquerading as an aldehyde dehydrogenase.";
RL Adv. Exp. Med. Biol. 414:417-423(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC, AND
RP SUBUNIT.
RX PubMed=12445786; DOI=10.1016/s0022-2836(02)01066-5;
RA Tanaka N., Kusakabe Y., Ito K., Yoshimoto T., Nakamura K.T.;
RT "Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida:
RT the structural origin of the tightly bound cofactor in nicotinoprotein
RT dehydrogenases.";
RL J. Mol. Biol. 324:519-533(2002).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formaldehyde and
CC acetaldehyde, and, to a lesser extent, long-chain alcohols, but is
CC inactive against propionaldehyde, butyraldehyde, methanol and ethanol.
CC Can also catalyze the dismutation of a wide range of aldehydes such as
CC formaldehyde. {ECO:0000269|PubMed:6526822, ECO:0000269|PubMed:9059646}.
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; Evidence={ECO:0000269|PubMed:6526822,
CC ECO:0000269|PubMed:9059646};
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:0000269|PubMed:6526822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 formaldehyde + H2O = formate + H(+) + methanol;
CC Xref=Rhea:RHEA:19221, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:17790; EC=1.2.98.1;
CC Evidence={ECO:0000269|PubMed:6526822, ECO:0000269|PubMed:9059646};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:6526822};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12445786,
CC ECO:0000269|PubMed:6526822};
CC -!- ACTIVITY REGULATION: Inactivated by bipyridine and p-
CC chloromercuribenzoate. {ECO:0000269|PubMed:6526822}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for formaldehyde;
CC pH dependence:
CC Optimum pH is 8.9. Active from pH 5 to 10.;
CC Temperature dependence:
CC Thermostable up to 60 degrees Celsius.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12445786}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; D21201; BAA04743.1; -; Genomic_DNA.
DR PIR; A55577; A55577.
DR PDB; 1KOL; X-ray; 1.65 A; A/B=2-399.
DR PDBsum; 1KOL; -.
DR AlphaFoldDB; P46154; -.
DR SMR; P46154; -.
DR STRING; 1240350.AMZE01000028_gene1932; -.
DR ChEMBL; CHEMBL1293291; -.
DR eggNOG; COG1063; Bacteria.
DR BRENDA; 1.2.1.46; 5092.
DR EvolutionaryTrace; P46154; -.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047895; F:formaldehyde dismutase 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..399
FT /note="Glutathione-independent formaldehyde dehydrogenase"
FT /id="PRO_0000160757"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 48..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0007744|PDB:1KOL"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 268..270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 300..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT BINDING 337..339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12445786,
FT ECO:0007744|PDB:1KOL"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1KOL"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:1KOL"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:1KOL"
SQ SEQUENCE 399 AA; 42082 MW; EBBA418C97E76A9F CRC64;
MSGNRGVVYL GSGKVEVQKI DYPKMQDPRG KKIEHGVILK VVSTNICGSD QHMVRGRTTA
QVGLVLGHEI TGEVIEKGRD VENLQIGDLV SVPFNVACGR CRSCKEMHTG VCLTVNPARA
GGAYGYVDMG DWTGGQAEYL LVPYADFNLL KLPDRDKAME KIRDLTCLSD ILPTGYHGAV
TAGVGPGSTV YVAGAGPVGL AAAASARLLG AAVVIVGDLN PARLAHAKAQ GFEIADLSLD
TPLHEQIAAL LGEPEVDCAV DAVGFEARGH GHEGAKHEAP ATVLNSLMQV TRVAGKIGIP
GLYVTEDPGA VDAAAKIGSL SIRFGLGWAK SHSFHTGQTP VMKYNRALMQ AIMWDRINIA
EVVGVQVISL DDAPRGYGEF DAGVPKKFVI DPHKTFSAA
