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P24918

- NDUS1_NEUCR

UniProt

P24918 - NDUS1_NEUCR

Protein

NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial

Gene

nuo78

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.

    Catalytic activityi

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

    Cofactori

    Binds 1 2Fe-2S cluster per subunit.By similarity
    Binds 2 4Fe-4S clusters per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi68 – 681Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi79 – 791Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi82 – 821Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi96 – 961Iron-sulfur 1 (2Fe-2S)By similarity
    Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
    Metal bindingi132 – 1321Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi135 – 1351Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi185 – 1851Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi188 – 1881Iron-sulfur 3 (4Fe-4S)By similarity
    Metal bindingi232 – 2321Iron-sulfur 3 (4Fe-4S)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. ATP synthesis coupled electron transport Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    2Fe-2S, 4Fe-4S, 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 78 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
    Alternative name(s):
    Complex I-78kD
    Short name:
    CI-78kD
    Gene namesi
    Name:nuo78
    ORF Names:B17C10.90, NCU01765
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 6, Linkage Group II

    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 – 3333Mitochondrion1 PublicationAdd
    BLAST
    Chaini34 – 744711NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrialPRO_0000019974Add
    BLAST

    Interactioni

    Subunit structurei

    Complex I is composed of about 40 different subunits.

    Protein-protein interaction databases

    STRINGi5141.NCU01765.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP24918.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 112792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini251 – 307574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the complex I 75 kDa subunit family.Curated
    Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
    Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1034.
    HOGENOMiHOG000031442.
    KOiK03934.
    OrthoDBiEOG7KWSS1.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
    IPR010228. NADH_UbQ_OxRdtase_Gsu.
    IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
    IPR015405. NuoG_C.
    [Graphical view]
    PfamiPF09326. DUF1982. 1 hit.
    PF00111. Fer2. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF10588. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view]
    SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF54292. SSF54292. 1 hit.
    TIGRFAMsiTIGR01973. NuoG. 1 hit.
    PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
    PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00641. COMPLEX1_75K_1. 1 hit.
    PS00642. COMPLEX1_75K_2. 1 hit.
    PS00643. COMPLEX1_75K_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24918-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRSTLSRSA WRTGRHQAAR NASRAFSATA QRPAEVELTI DGKKVSIEAG    50
    SALIQACEKA GVTIPRYCYH EKLMIAGNCR MCLVEVEKVP KPVASCAWPV 100
    QPGMVVKTNS PLTHKAREGV MEFLLANHPL DCPICDQGGE CDLQDQSMRY 150
    GGDRGRFHEV GGKRAVEDKN MGPLIKTSMN RCIQCTRCVR FANDIAGAPE 200
    LGSTGRGNDL QIGTYLEKNL DSELSGNVID LCPVGALTSK PYAFRARPWE 250
    LKKTESIDVL DGLGSNIRVD TRGLEVMRIL PRLNDEVNEE WINDKTRFAC 300
    DGLKTQRLTI PLVRREGKFE PASWDQALTE IAHAYQTLNP QGNEFKAIAG 350
    QLTEVESLVA MKDLANRLGS ENLALDMPSG HKPLAHGVDV RSNYIFNSSI 400
    VGIESADVIL LVGTNPRHEA AVLNARIRKQ WLRSDLEIGV VGQTWDSTFE 450
    FEHLGTDHAA LQKALEGDFG KKLQSAKNPM IIVGSGVTDH GDANAFYETV 500
    GKFVDSNASN FLTEEWNGYN VLQRAASRVG AFEVGFTVPS AEIAQTKPKF 550
    VWLLGADEFN EADIPKDAFI VYQGHHGDRG AQIADIVLPG AAYTEKAGTY 600
    VNTEGRVQMT RAATGLPGAA RTDWKILRAV SEYLGVRLPY DDVAQLRDRM 650
    VEISPALSSY DIIEPPSLQQ LSKVQLVEQN QGATATNEPL KKVIENFYFT 700
    DAISRSSPTM ARCSAAKKTG DPRTNFMAPG MEEDRPMGQI AYGA 744
    Length:744
    Mass (Da):81,602
    Last modified:June 1, 2001 - v2
    Checksum:iD842DDCE80510929
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti125 – 1251L → P in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti152 – 1521G → R in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti164 – 1641R → Q in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti340 – 3401P → A in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti379 – 38810SGHKPLAHGV → FGPQTSCSWC in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti493 – 4931A → R in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti527 – 5348SRVGAFEV → PESAPSRL in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti666 – 6672PS → SL in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti722 – 7221P → S in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti727 – 7293MAP → IGS in CAA40828. (PubMed:1832016)Curated
    Sequence conflicti740 – 7401I → Y in CAA40828. (PubMed:1832016)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57602 mRNA. Translation: CAA40828.1.
    AL355926 Genomic DNA. Translation: CAB91229.1.
    CM002237 Genomic DNA. Translation: EAA27952.3.
    PIRiS17664.
    T49428.
    RefSeqiXP_957188.2. XM_952095.2.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000001842; EFNCRP00000001842; EFNCRG00000001840.
    GeneIDi3873340.
    KEGGincr:NCU01765.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57602 mRNA. Translation: CAA40828.1 .
    AL355926 Genomic DNA. Translation: CAB91229.1 .
    CM002237 Genomic DNA. Translation: EAA27952.3 .
    PIRi S17664.
    T49428.
    RefSeqi XP_957188.2. XM_952095.2.

    3D structure databases

    ProteinModelPortali P24918.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU01765.1.

    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 EFNCRT00000001842 ; EFNCRP00000001842 ; EFNCRG00000001840 .
    GeneIDi 3873340.
    KEGGi ncr:NCU01765.

    Phylogenomic databases

    eggNOGi COG1034.
    HOGENOMi HOG000031442.
    KOi K03934.
    OrthoDBi EOG7KWSS1.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR001041. 2Fe-2S_ferredoxin-type.
    IPR012675. Beta-grasp_dom.
    IPR006656. Mopterin_OxRdtase.
    IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
    IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
    IPR010228. NADH_UbQ_OxRdtase_Gsu.
    IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
    IPR015405. NuoG_C.
    [Graphical view ]
    Pfami PF09326. DUF1982. 1 hit.
    PF00111. Fer2. 1 hit.
    PF00384. Molybdopterin. 1 hit.
    PF10588. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54292. SSF54292. 1 hit.
    TIGRFAMsi TIGR01973. NuoG. 1 hit.
    PROSITEi PS51085. 2FE2S_FER_2. 1 hit.
    PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
    PS00641. COMPLEX1_75K_1. 1 hit.
    PS00642. COMPLEX1_75K_2. 1 hit.
    PS00643. COMPLEX1_75K_3. 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], PROTEIN SEQUENCE OF 34-64.
      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 nameiNDUS1_NEUCR
    AccessioniPrimary (citable) accession number: P24918
    Secondary accession number(s): Q7RV66, Q9P6E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 137 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3