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P24917

- NDUV1_NEUCR

UniProt

P24917 - NDUV1_NEUCR

Protein

NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial

Gene

nuo-51

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

    Catalytic activityi

    NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
    NADH + acceptor = NAD+ + reduced acceptor.

    Cofactori

    Binds 1 FMN.Curated
    Binds 1 4Fe-4S cluster.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi391 – 3911Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi394 – 3941Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi397 – 3971Iron-sulfur (4Fe-4S)Sequence Analysis
    Metal bindingi437 – 4371Iron-sulfur (4Fe-4S)Sequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi96 – 10510NADBy similarity
    Nucleotide bindingi212 – 25948FMNBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. FMN binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. NAD binding Source: InterPro
    5. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    4Fe-4S, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

    Protein family/group databases

    TCDBi3.D.1.6.2. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
    Alternative name(s):
    Complex I-51kD
    Short name:
    CI-51kD
    Gene namesi
    Name:nuo-51
    ORF Names:B10H18.210, NCU04044
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 5, Linkage Group VI

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. respiratory chain Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionAdd
    BLAST
    Chaini28 – 493466NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrialPRO_0000019980Add
    BLAST

    Interactioni

    Subunit structurei

    Complex I is composed of about 40 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.

    Protein-protein interaction databases

    STRINGi5141.NCU04044.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP24917.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the complex I 51 kDa subunit family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1894.
    HOGENOMiHOG000251534.
    KOiK03942.
    OMAiKWSFMNP.
    OrthoDBiEOG7M3J8B.

    Family and domain databases

    InterProiIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
    IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
    IPR011537. NADH-UbQ_OxRdtase_suF.
    IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
    IPR019554. Soluble_ligand-bd.
    [Graphical view]
    PfamiPF01512. Complex1_51K. 1 hit.
    PF10589. NADH_4Fe-4S. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view]
    SMARTiSM00928. NADH_4Fe-4S. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01959. nuoF_fam. 1 hit.
    PROSITEiPS00644. COMPLEX1_51K_1. 1 hit.
    PS00645. COMPLEX1_51K_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24917-1 [UniParc]FASTAAdd to Basket

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    MLSRTAAPTK ASARTLSRAA AEQCRTFATV QDGSANPVRH YGGLKDQDRI    50
    FQNLYGRYPP DLKHAKKMGD WHKTKEILLK GHDWIIGEVK ASGLRGRGGA 100
    GFPSGLKWSF MNFKDWDKDD KPRYLVVNAD EGEPGTCKDR EIMRKDPHKL 150
    VEGCLVAGRA MNATAAYIYI RGEFIQEAAI LQNAINEAYA DGLIGKNACG 200
    SGYDFDVYLH RGAGAYVCGE ETSLIESLEG KPGKPRLKPP FPAAVGLFGC 250
    PSTVANVETV AVAPTICRRG GNWFAGFGRE RNQGTKLFCI SGHVNNPCTV 300
    EEEMSIPMRE LIDKHCGGVR GGWDNLLAVI PGGSSTPILP KHICDTQLMD 350
    FDALKDSQSG LGTAALIVMD KSTDVVRAIS RLSHFYRHES CGQCTPCREG 400
    SKWTEQIMKR FEKGQGRERE IDMLQELTKQ VEGHTICALG EAFAWPIQGL 450
    IRHFRPELEA RIRKFAQENG GEALAGGWQR NARQQGKLVS PGM 493
    Length:493
    Mass (Da):54,241
    Last modified:June 7, 2005 - v2
    Checksum:i351B01F00602B06E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti260 – 2612VA → AV in CAA39676. (PubMed:1832016)Curated
    Sequence conflicti442 – 4421A → R in CAA39676. (PubMed:1832016)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56227 mRNA. Translation: CAA39676.1.
    BX897678 Genomic DNA. Translation: CAE85605.1.
    CM002241 Genomic DNA. Translation: EAA28423.1.
    PIRiS17663.
    RefSeqiXP_957659.1. XM_952566.1.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000003696; EFNCRP00000003696; EFNCRG00000003692.
    GeneIDi3873830.
    KEGGincr:NCU04044.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56227 mRNA. Translation: CAA39676.1 .
    BX897678 Genomic DNA. Translation: CAE85605.1 .
    CM002241 Genomic DNA. Translation: EAA28423.1 .
    PIRi S17663.
    RefSeqi XP_957659.1. XM_952566.1.

    3D structure databases

    ProteinModelPortali P24917.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU04044.1.

    Protein family/group databases

    TCDBi 3.D.1.6.2. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000003696 ; EFNCRP00000003696 ; EFNCRG00000003692 .
    GeneIDi 3873830.
    KEGGi ncr:NCU04044.

    Phylogenomic databases

    eggNOGi COG1894.
    HOGENOMi HOG000251534.
    KOi K03942.
    OMAi KWSFMNP.
    OrthoDBi EOG7M3J8B.

    Family and domain databases

    InterProi IPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
    IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
    IPR011537. NADH-UbQ_OxRdtase_suF.
    IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
    IPR019554. Soluble_ligand-bd.
    [Graphical view ]
    Pfami PF01512. Complex1_51K. 1 hit.
    PF10589. NADH_4Fe-4S. 1 hit.
    PF10531. SLBB. 1 hit.
    [Graphical view ]
    SMARTi SM00928. NADH_4Fe-4S. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01959. nuoF_fam. 1 hit.
    PROSITEi PS00644. COMPLEX1_51K_1. 1 hit.
    PS00645. COMPLEX1_51K_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structures of two subunits of NADH: ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus."
      Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.-A., van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H.
      Biochim. Biophys. Acta 1090:133-138(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 74-ORS-6a / FGSC 4200.
    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 nameiNDUV1_NEUCR
    AccessioniPrimary (citable) accession number: P24917
    Secondary accession number(s): Q7RV82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 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