Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Formate dehydrogenase

Gene
N/A
Organism
Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD+-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.UniRule annotation1 Publication

Catalytic activityi

Formate + NAD+ = CO2 + NADH.UniRule annotation2 Publications

Kineticsi

kcat is 10 sec(-1) with formate as substrate.2 Publications

Manual assertion based on experiment ini

  1. KM=7.5 mM for formate1 Publication
  2. KM=7.0 mM for formate1 Publication
  3. KM=0.11 mM for NAD+1 Publication
  4. KM=60 µM for NAD+1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei123Substrate; via amide nitrogenUniRule annotation1 Publication1
    Binding sitei147SubstrateUniRule annotation1 Publication1
    Binding sitei148NADUniRule annotation1 Publication1
    Binding sitei222NADUniRule annotation1 Publication1
    Binding sitei283NAD; via carbonyl oxygenUniRule annotation1 Publication1
    Sitei285Important for catalytic activityUniRule annotation1 Publication1
    Binding sitei309NADUniRule annotation1 Publication1
    Sitei333Important for catalytic activityUniRule annotation1 Publication1
    Binding sitei381NADUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi202 – 203NADUniRule annotation1 Publication2
    Nucleotide bindingi257 – 261NADUniRule annotation1 Publication5
    Nucleotide bindingi333 – 336NADUniRule annotation1 Publication4

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.2.1.2. 5085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenase1 PublicationUniRule annotation (EC:1.2.1.2UniRule annotation2 Publications)
    Short name:
    FDHUniRule annotation
    Alternative name(s):
    NAD-dependent formate dehydrogenase1 PublicationUniRule annotation
    OrganismiPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
    Taxonomic identifieri33067 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi256C → S or M: High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000760272 – 401Formate dehydrogenaseAdd BLAST400

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Structurei

    Secondary structure

    1401
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 7Combined sources5
    Beta strandi21 – 23Combined sources3
    Turni54 – 56Combined sources3
    Helixi57 – 59Combined sources3
    Helixi61 – 66Combined sources6
    Beta strandi70 – 75Combined sources6
    Helixi83 – 88Combined sources6
    Beta strandi92 – 97Combined sources6
    Helixi106 – 111Combined sources6
    Beta strandi117 – 123Combined sources7
    Helixi130 – 135Combined sources6
    Beta strandi139 – 142Combined sources4
    Turni144 – 147Combined sources4
    Helixi148 – 163Combined sources16
    Helixi166 – 174Combined sources9
    Helixi180 – 184Combined sources5
    Beta strandi194 – 198Combined sources5
    Helixi202 – 211Combined sources10
    Helixi212 – 214Combined sources3
    Beta strandi217 – 221Combined sources5
    Helixi228 – 234Combined sources7
    Beta strandi237 – 241Combined sources5
    Helixi242 – 245Combined sources4
    Helixi246 – 248Combined sources3
    Beta strandi250 – 254Combined sources5
    Turni260 – 264Combined sources5
    Helixi268 – 271Combined sources4
    Beta strandi278 – 282Combined sources5
    Helixi286 – 288Combined sources3
    Helixi291 – 299Combined sources9
    Beta strandi302 – 309Combined sources8
    Beta strandi312 – 315Combined sources4
    Helixi321 – 323Combined sources3
    Helixi335 – 337Combined sources3
    Helixi339 – 358Combined sources20
    Helixi364 – 366Combined sources3
    Beta strandi367 – 370Combined sources4
    Beta strandi371 – 373Combined sources3
    Helixi377 – 381Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GO1X-ray2.10A1-401[»]
    2GUGX-ray2.28A/B/C/D1-401[»]
    2NACX-ray1.80A/B2-394[»]
    2NADX-ray2.05A/B2-394[»]
    ProteinModelPortaliP33160.
    SMRiP33160.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33160.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni3 – 147CatalyticUniRule annotation1 PublicationAdd BLAST145
    Regioni148 – 334Coenzyme-bindingUniRule annotation1 PublicationAdd BLAST187
    Regioni335 – 382CatalyticUniRule annotation1 PublicationAdd BLAST48

    Sequence similaritiesi

    Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.UniRule annotation

    Family and domain databases

    CDDicd05302. FDH. 1 hit.
    Gene3Di3.40.50.720. 2 hits.
    HAMAPiMF_03210. Formate_dehydrogenase. 1 hit.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR029753. D-isomer_DH_CS.
    IPR029752. D-isomer_DH_CS1.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR033689. FDH_NAD-dep.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P33160-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKVLCVLYD DPVDGYPKTY ARDDLPKIDH YPGGQTLPTP KAIDFTPGQL
    60 70 80 90 100
    LGSVSGELGL RKYLESNGHT LVVTSDKDGP DSVFERELVD ADVVISQPFW
    110 120 130 140 150
    PAYLTPERIA KAKNLKLALT AGIGSDHVDL QSAIDRNVTV AEVTYCNSIS
    160 170 180 190 200
    VAEHVVMMIL SLVRNYLPSH EWARKGGWNI ADCVSHAYDL EAMHVGTVAA
    210 220 230 240 250
    GRIGLAVLRR LAPFDVHLHY TDRHRLPESV EKELNLTWHA TREDMYPVCD
    260 270 280 290 300
    VVTLNCPLHP ETEHMINDET LKLFKRGAYI VNTARGKLCD RDAVARALES
    310 320 330 340 350
    GRLAGYAGDV WFPQPAPKDH PWRTMPYNGM TPHISGTTLT AQARYAAGTR
    360 370 380 390 400
    EILECFFEGR PIRDEYLIVQ GGALAGTGAH SYSKGNATGG SEEAAKFKKA

    V
    Length:401
    Mass (Da):44,136
    Last modified:January 23, 2007 - v3
    Checksum:i6B3EBA21F03A89A2
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti78D → S (PubMed:1954846).Curated1
    Sequence conflicti139 – 140TV → VT (PubMed:1954846).Curated2
    Sequence conflicti146C → V (PubMed:1954846).Curated1
    Sequence conflicti216 – 217VH → HV (PubMed:1954846).Curated2
    Sequence conflicti328N → D (PubMed:1954846).Curated1

    Sequence databases

    PIRiJU0334.

    Cross-referencesi

    Sequence databases

    PIRiJU0334.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GO1X-ray2.10A1-401[»]
    2GUGX-ray2.28A/B/C/D1-401[»]
    2NACX-ray1.80A/B2-394[»]
    2NADX-ray2.05A/B2-394[»]
    ProteinModelPortaliP33160.
    SMRiP33160.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.2.1.2. 5085.

    Miscellaneous databases

    EvolutionaryTraceiP33160.

    Family and domain databases

    CDDicd05302. FDH. 1 hit.
    Gene3Di3.40.50.720. 2 hits.
    HAMAPiMF_03210. Formate_dehydrogenase. 1 hit.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR029753. D-isomer_DH_CS.
    IPR029752. D-isomer_DH_CS1.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR033689. FDH_NAD-dep.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFDH_PSESR
    AccessioniPrimary (citable) accession number: P33160
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 102 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.