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Protein

Glutathione-independent formaldehyde dehydrogenase

Gene

fdhA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of formaldehyde and acetoaldehyde as well as long-chain alcohols but is inactive against propionaldehyde, butyraldehyde, methanol and ethanol. Can also catalyze the dismutation of a wide range of aldehydes such as formaldehyde.2 Publications

Catalytic activityi

Formaldehyde + NAD+ + H2O = formate + NADH.2 Publications
An alcohol + NAD+ = an aldehyde or ketone + NADH.2 Publications
2 formaldehyde + H2O = formate + methanol.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.
  • NAD+Note: Contains a tightly but non-covalently bound NAD cofactor required for formaldehyde dismutase activity.

Enzyme regulationi

Inactivated by bipyridine and p-chloromercuribenzoate.1 Publication

Kineticsi

  1. KM=0.25 mM for formaldehyde

    pH dependencei

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

    Temperature dependencei

    Thermostable up to 60 degrees Celsius.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi47Zinc 1; catalytic1
    Metal bindingi68Zinc 1; catalytic1
    Metal bindingi98Zinc 21
    Metal bindingi101Zinc 21
    Metal bindingi104Zinc 21
    Metal bindingi112Zinc 21
    Metal bindingi177Zinc 1; catalytic1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BRENDAi1.2.1.46. 5092.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione-independent formaldehyde dehydrogenase (EC:1.2.1.462 Publications)
    Short name:
    FALDH
    Short name:
    FDH
    Alternative name(s):
    Formaldehyde dismutase (EC:1.2.98.12 Publications)
    Gene namesi
    Name:fdhA
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1293291.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00001607572 – 399Glutathione-independent formaldehyde dehydrogenaseAdd BLAST398

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Structurei

    Secondary structure

    1399
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 11Combined sources8
    Beta strandi14 – 20Combined sources7
    Beta strandi37 – 45Combined sources9
    Helixi48 – 54Combined sources7
    Beta strandi70 – 77Combined sources8
    Beta strandi89 – 91Combined sources3
    Beta strandi94 – 96Combined sources3
    Beta strandi99 – 101Combined sources3
    Helixi102 – 105Combined sources4
    Helixi109 – 111Combined sources3
    Beta strandi113 – 115Combined sources3
    Beta strandi117 – 120Combined sources4
    Beta strandi122 – 124Combined sources3
    Beta strandi136 – 144Combined sources9
    Helixi145 – 148Combined sources4
    Helixi155 – 160Combined sources6
    Helixi162 – 165Combined sources4
    Helixi166 – 169Combined sources4
    Helixi171 – 181Combined sources11
    Beta strandi189 – 193Combined sources5
    Helixi197 – 208Combined sources12
    Beta strandi212 – 219Combined sources8
    Helixi221 – 229Combined sources9
    Beta strandi233 – 236Combined sources4
    Beta strandi239 – 241Combined sources3
    Helixi243 – 251Combined sources9
    Beta strandi252 – 254Combined sources3
    Beta strandi256 – 261Combined sources6
    Helixi274 – 276Combined sources3
    Helixi282 – 290Combined sources9
    Beta strandi296 – 299Combined sources4
    Helixi313 – 316Combined sources4
    Helixi324 – 329Combined sources6
    Beta strandi333 – 338Combined sources6
    Helixi341 – 353Combined sources13
    Helixi359 – 363Combined sources5
    Beta strandi365 – 368Combined sources4
    Helixi370 – 372Combined sources3
    Helixi373 – 382Combined sources10
    Beta strandi387 – 390Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KOLX-ray1.65A/B2-399[»]
    ProteinModelPortaliP46154.
    SMRiP46154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46154.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni172 – 338Cofactor-bindingAdd BLAST167

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR014184. HCHO_DH_non_GSH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02819. fdhA_non_GSH. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P46154-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSGNRGVVYL GSGKVEVQKI DYPKMQDPRG KKIEHGVILK VVSTNICGSD
    60 70 80 90 100
    QHMVRGRTTA QVGLVLGHEI TGEVIEKGRD VENLQIGDLV SVPFNVACGR
    110 120 130 140 150
    CRSCKEMHTG VCLTVNPARA GGAYGYVDMG DWTGGQAEYL LVPYADFNLL
    160 170 180 190 200
    KLPDRDKAME KIRDLTCLSD ILPTGYHGAV TAGVGPGSTV YVAGAGPVGL
    210 220 230 240 250
    AAAASARLLG AAVVIVGDLN PARLAHAKAQ GFEIADLSLD TPLHEQIAAL
    260 270 280 290 300
    LGEPEVDCAV DAVGFEARGH GHEGAKHEAP ATVLNSLMQV TRVAGKIGIP
    310 320 330 340 350
    GLYVTEDPGA VDAAAKIGSL SIRFGLGWAK SHSFHTGQTP VMKYNRALMQ
    360 370 380 390
    AIMWDRINIA EVVGVQVISL DDAPRGYGEF DAGVPKKFVI DPHKTFSAA
    Length:399
    Mass (Da):42,082
    Last modified:January 23, 2007 - v3
    Checksum:iEBBA418C97E76A9F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D21201 Genomic DNA. Translation: BAA04743.1.
    PIRiA55577.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D21201 Genomic DNA. Translation: BAA04743.1.
    PIRiA55577.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KOLX-ray1.65A/B2-399[»]
    ProteinModelPortaliP46154.
    SMRiP46154.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    ChEMBLiCHEMBL1293291.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.2.1.46. 5092.

    Miscellaneous databases

    EvolutionaryTraceiP46154.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR014184. HCHO_DH_non_GSH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02819. fdhA_non_GSH. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFADH_PSEPU
    AccessioniPrimary (citable) accession number: P46154
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.