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P33160

- FDH_PSESR

UniProt

P33160 - FDH_PSESR

Protein

Formate dehydrogenase

Gene
N/A
Organism
Pseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Formate + NAD+ = CO2 + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei285 – 2851By similarity
    Binding sitei309 – 3091NADBy similarity
    Active sitei333 – 3331Proton donorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi202 – 2032NADBy similarity
    Nucleotide bindingi283 – 2853NADBy similarity
    Nucleotide bindingi333 – 3364NADBy similarity

    GO - Molecular functioni

    1. formate dehydrogenase (NAD+) activity Source: UniProtKB-EC
    2. NAD binding Source: InterPro
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi1.2.1.2. 5085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenase (EC:1.2.1.2)
    Alternative name(s):
    NAD-dependent formate dehydrogenase
    Short name:
    FDH
    OrganismiPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
    Taxonomic identifieri33067 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi256 – 2561C → S or M: High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 401400Formate dehydrogenasePRO_0000076027Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    401
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Beta strandi21 – 233
    Turni54 – 563
    Helixi57 – 593
    Helixi61 – 666
    Beta strandi70 – 756
    Helixi83 – 886
    Beta strandi92 – 976
    Helixi106 – 1116
    Beta strandi117 – 1237
    Helixi130 – 1356
    Beta strandi139 – 1424
    Turni144 – 1474
    Helixi148 – 16316
    Helixi166 – 1749
    Helixi180 – 1845
    Beta strandi194 – 1985
    Helixi202 – 21110
    Helixi212 – 2143
    Beta strandi217 – 2215
    Helixi228 – 2347
    Beta strandi237 – 2415
    Helixi242 – 2454
    Helixi246 – 2483
    Beta strandi250 – 2545
    Turni260 – 2645
    Helixi268 – 2714
    Beta strandi278 – 2825
    Helixi286 – 2883
    Helixi291 – 2999
    Beta strandi302 – 3098
    Beta strandi312 – 3154
    Helixi321 – 3233
    Helixi335 – 3373
    Helixi339 – 35820
    Helixi364 – 3663
    Beta strandi367 – 3704
    Beta strandi371 – 3733
    Helixi377 – 3815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33160.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 147146CatalyticAdd
    BLAST
    Regioni148 – 334187Coenzyme-bindingAdd
    BLAST
    Regioni335 – 40167CatalyticAdd
    BLAST

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    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

    MAKVLCVLYD DPVDGYPKTY ARDDLPKIDH YPGGQTLPTP KAIDFTPGQL    50
    LGSVSGELGL RKYLESNGHT LVVTSDKDGP DSVFERELVD ADVVISQPFW 100
    PAYLTPERIA KAKNLKLALT AGIGSDHVDL QSAIDRNVTV AEVTYCNSIS 150
    VAEHVVMMIL SLVRNYLPSH EWARKGGWNI ADCVSHAYDL EAMHVGTVAA 200
    GRIGLAVLRR LAPFDVHLHY TDRHRLPESV EKELNLTWHA TREDMYPVCD 250
    VVTLNCPLHP ETEHMINDET LKLFKRGAYI VNTARGKLCD RDAVARALES 300
    GRLAGYAGDV WFPQPAPKDH PWRTMPYNGM TPHISGTTLT AQARYAAGTR 350
    EILECFFEGR PIRDEYLIVQ GGALAGTGAH SYSKGNATGG SEEAAKFKKA 400
    V 401
    Length:401
    Mass (Da):44,136
    Last modified:January 23, 2007 - v3
    Checksum:i6B3EBA21F03A89A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 781D → S(PubMed:1954846)Curated
    Sequence conflicti139 – 1402TV → VT(PubMed:1954846)Curated
    Sequence conflicti146 – 1461C → V(PubMed:1954846)Curated
    Sequence conflicti216 – 2172VH → HV(PubMed:1954846)Curated
    Sequence conflicti328 – 3281N → D(PubMed:1954846)Curated

    Sequence databases

    PIRiJU0334.

    Cross-referencesi

    Sequence databases

    PIRi JU0334.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GO1 X-ray 2.10 A 1-401 [» ]
    2GUG X-ray 2.28 A/B/C/D 1-401 [» ]
    2NAC X-ray 1.80 A/B 2-394 [» ]
    2NAD X-ray 2.05 A/B 2-394 [» ]
    ProteinModelPortali P33160.
    SMRi P33160. Positions 2-392.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 1.2.1.2. 5085.

    Miscellaneous databases

    EvolutionaryTracei P33160.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00065. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101: cloning, expression, and study of the genetic structure."
      Tishkov V.I., Galkin A.G., Egorov A.M.
      Dokl. Akad. Nauk SSSR 317:745-748(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "NAD-dependent formate dehydrogenase from methylotrophic bacteria Pseudomonas sp. 101. I. Amino acid sequence."
      Popov V.O., Shumilin I.A., Ustinnikova T.B., Lamzin V.S., Egorov T.A.
      Bioorg. Khim. 16:324-335(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-394.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    4. "Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements."
      Tishkov V.I., Galkin A.G., Marchenko G.N., Egorova O.A., Sheluho D.V., Kulakova L.B., Dementieva L.A., Egorov A.M.
      Biochem. Biophys. Res. Commun. 192:976-981(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-256.

    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: October 1, 2014
    This is version 88 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

    External Data

    Dasty 3