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Q07103

- FDH_NEUCR

UniProt

Q07103 - FDH_NEUCR

Protein

Formate dehydrogenase

Gene

fdh

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Formate + NAD+ = CO2 + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei259 – 2591By similarity
    Binding sitei283 – 2831NADBy similarity
    Active sitei312 – 3121Proton donorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi175 – 1762NADBy similarity
    Nucleotide bindingi257 – 2593NADBy similarity
    Nucleotide bindingi312 – 3154NADBy 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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Formate dehydrogenase (EC:1.2.1.2)
    Alternative name(s):
    NAD-dependent formate dehydrogenase
    Short name:
    FDH
    Gene namesi
    Name:fdh
    ORF Names:99H12.160, NCU03813
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 2, Linkage Group V

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: EnsemblFungi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Formate dehydrogenasePRO_0000076026Add
    BLAST

    Proteomic databases

    PRIDEiQ07103.

    Expressioni

    Developmental stagei

    Developmentally regulated. Expressed only during conidiation and early germination.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi5141.NCU03813.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07103.
    SMRiQ07103. Positions 3-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi364 – 37411Ala-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1052.
    HOGENOMiHOG000136703.
    KOiK00122.
    OMAiGCRRVEN.
    OrthoDBiEOG769ZV3.

    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.

    Q07103-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKVLAVLYD GGKHGEEVPE LLGTIQNELG LRKWLEDQGH TLVTTCDKDG    50
    ENSTFDKELE DAEIIITTPF HPGYLTAERL ARAKKLKLAV TAGIGSDHVD 100
    LNAANKTNGG ITVAEVTGSN VVSVAEHVLM TILVLVRNFV PAHEQIQEGR 150
    WDVAEAAKNE FDLEGKVVGT VGVGRIGERV LRRLKPFDCK ELLYYDYQPL 200
    SAEKEAEIGC RRVADLEEML AQCDVVTINC PLHEKTQGLF NKELISKMKK 250
    GSWLVNTARG AIVVKEDVAE ALKSGHLRGY GGDVWFPQPA PQDHPLRYAK 300
    NPFGGGNAMV PHMSGTSLDA QKRYAAGTKA IIESYLSGKH DYRPEDLIVY 350
    GGDYATKSYG ERERAKAAAA AAKSA 375
    Length:375
    Mass (Da):40,957
    Last modified:February 1, 1995 - v1
    Checksum:i3073CB95FB204968
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13964 Genomic DNA. Translation: AAA99900.1.
    AL451018 Genomic DNA. Translation: CAC18252.1.
    CM002240 Genomic DNA. Translation: EAA31966.1.
    PIRiA47117.
    RefSeqiXP_961202.1. XM_956109.2.
    UniGeneiNcr.7835.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000003500; EFNCRP00000003500; EFNCRG00000003496.
    GeneIDi3877330.
    KEGGincr:NCU03813.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13964 Genomic DNA. Translation: AAA99900.1 .
    AL451018 Genomic DNA. Translation: CAC18252.1 .
    CM002240 Genomic DNA. Translation: EAA31966.1 .
    PIRi A47117.
    RefSeqi XP_961202.1. XM_956109.2.
    UniGenei Ncr.7835.

    3D structure databases

    ProteinModelPortali Q07103.
    SMRi Q07103. Positions 3-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU03813.1.

    Proteomic databases

    PRIDEi Q07103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000003500 ; EFNCRP00000003500 ; EFNCRG00000003496 .
    GeneIDi 3877330.
    KEGGi ncr:NCU03813.

    Phylogenomic databases

    eggNOGi COG1052.
    HOGENOMi HOG000136703.
    KOi K00122.
    OMAi GCRRVEN.
    OrthoDBi EOG769ZV3.

    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. "Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa."
      Chow C.M., RajBhandary U.L.
      J. Bacteriol. 175:3703-3709(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    3. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiFDH_NEUCR
    AccessioniPrimary (citable) accession number: Q07103
    Secondary accession number(s): Q7RVC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3