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P46154 (FADH_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione-independent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
EC=1.2.1.46
Gene names
Name:fdhA
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of long-chain alcohols but is inactive against ethanol.

Catalytic activity

Formaldehyde + NAD+ + H2O = formate + NADH.

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.25 mM for formaldehyde

pH dependence:

Optimum pH is 8.9. Active from pH 5 to 10.

Temperature dependence:

Thermostable up to 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 399398Glutathione-independent formaldehyde dehydrogenase
PRO_0000160757

Regions

Region172 – 338167Cofactor-binding

Sites

Metal binding471Zinc 1; catalytic
Metal binding681Zinc 1; catalytic
Metal binding981Zinc 2
Metal binding1011Zinc 2
Metal binding1041Zinc 2
Metal binding1121Zinc 2
Metal binding1771Zinc 1; catalytic

Secondary structure

1 ............................................................................ 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46154 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EBBA418C97E76A9F

FASTA39942,082
        10         20         30         40         50         60 
MSGNRGVVYL GSGKVEVQKI DYPKMQDPRG KKIEHGVILK VVSTNICGSD QHMVRGRTTA 

        70         80         90        100        110        120 
QVGLVLGHEI TGEVIEKGRD VENLQIGDLV SVPFNVACGR CRSCKEMHTG VCLTVNPARA 

       130        140        150        160        170        180 
GGAYGYVDMG DWTGGQAEYL LVPYADFNLL KLPDRDKAME KIRDLTCLSD ILPTGYHGAV 

       190        200        210        220        230        240 
TAGVGPGSTV YVAGAGPVGL AAAASARLLG AAVVIVGDLN PARLAHAKAQ GFEIADLSLD 

       250        260        270        280        290        300 
TPLHEQIAAL LGEPEVDCAV DAVGFEARGH GHEGAKHEAP ATVLNSLMQV TRVAGKIGIP 

       310        320        330        340        350        360 
GLYVTEDPGA VDAAAKIGSL SIRFGLGWAK SHSFHTGQTP VMKYNRALMQ AIMWDRINIA 

       370        380        390 
EVVGVQVISL DDAPRGYGEF DAGVPKKFVI DPHKTFSAA

« Hide

References

[1]"Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida."
Ito K., Takahashi M., Yoshimoto T., Tsuru D.
J. Bacteriol. 176:2483-2491(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: C-83.
[2]"Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases."
Tanaka N., Kusakabe Y., Ito K., Yoshimoto T., Nakamura K.T.
J. Mol. Biol. 324:519-533(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D21201 Genomic DNA. Translation: BAA04743.1.
PIRA55577.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KOLX-ray1.65A/B2-399[»]
ProteinModelPortalP46154.
SMRP46154. Positions 3-398.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.46. 5163.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR011032. GroES-like.
IPR014184. HCHO_DH_non_GSH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF01262. AlaDh_PNT_C. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
TIGRFAMsTIGR02819. fdhA_non_GSH. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1293291.
EvolutionaryTraceP46154.

Entry information

Entry nameFADH_PSEPU
AccessionPrimary (citable) accession number: P46154
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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