ID NDUS1_NEUCR Reviewed; 744 AA.
AC P24918; Q7RV66; Q9P6E0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 24-JAN-2024, entry version 185.
DE RecName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-78kD;
DE Short=CI-78kD;
DE Flags: Precursor;
GN Name=nuo78; ORFNames=B17C10.90, NCU01765;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-64.
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=1832016; DOI=10.1016/0167-4781(91)90049-r;
RA Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.-A.,
RA van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H.;
RT "Primary structures of two subunits of NADH: ubiquinone reductase from
RT Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble
RT NAD-reducing hydrogenase of Alcaligenes eutrophus.";
RL Biochim. Biophys. Acta 1090:133-138(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone. This is
CC the largest subunit of complex I and it is a component of the iron-
CC sulfur (IP) fragment of the enzyme. It may form part of the active site
CC crevice where NADH is oxidized.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; X57602; CAA40828.1; -; mRNA.
DR EMBL; AL355926; CAB91229.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27952.3; -; Genomic_DNA.
DR PIR; S17664; S17664.
DR PIR; T49428; T49428.
DR RefSeq; XP_957188.3; XM_952095.3.
DR AlphaFoldDB; P24918; -.
DR SMR; P24918; -.
DR STRING; 367110.P24918; -.
DR TCDB; 3.D.1.6.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; 5141-EFNCRP00000001842; -.
DR EnsemblFungi; EAA27952; EAA27952; NCU01765.
DR GeneID; 3873340; -.
DR KEGG; ncr:NCU01765; -.
DR VEuPathDB; FungiDB:NCU01765; -.
DR HOGENOM; CLU_000422_11_6_1; -.
DR InParanoid; P24918; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NDUFS1-like_C.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; NAD; Oxidoreductase; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1832016"
FT CHAIN 34..744
FT /note="NADH-ubiquinone oxidoreductase 78 kDa subunit,
FT mitochondrial"
FT /id="PRO_0000019974"
FT DOMAIN 34..112
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 112..151
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 251..307
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 135
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 141
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 182
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 125
FT /note="L -> P (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> R (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="R -> Q (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="P -> A (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..388
FT /note="SGHKPLAHGV -> FGPQTSCSWC (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="A -> R (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 527..534
FT /note="SRVGAFEV -> PESAPSRL (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 666..667
FT /note="PS -> SL (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="P -> S (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 727..729
FT /note="MAP -> IGS (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="I -> Y (in Ref. 1; CAA40828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 81602 MW; D842DDCE80510929 CRC64;
MLRSTLSRSA WRTGRHQAAR NASRAFSATA QRPAEVELTI DGKKVSIEAG SALIQACEKA
GVTIPRYCYH EKLMIAGNCR MCLVEVEKVP KPVASCAWPV QPGMVVKTNS PLTHKAREGV
MEFLLANHPL DCPICDQGGE CDLQDQSMRY GGDRGRFHEV GGKRAVEDKN MGPLIKTSMN
RCIQCTRCVR FANDIAGAPE LGSTGRGNDL QIGTYLEKNL DSELSGNVID LCPVGALTSK
PYAFRARPWE LKKTESIDVL DGLGSNIRVD TRGLEVMRIL PRLNDEVNEE WINDKTRFAC
DGLKTQRLTI PLVRREGKFE PASWDQALTE IAHAYQTLNP QGNEFKAIAG QLTEVESLVA
MKDLANRLGS ENLALDMPSG HKPLAHGVDV RSNYIFNSSI VGIESADVIL LVGTNPRHEA
AVLNARIRKQ WLRSDLEIGV VGQTWDSTFE FEHLGTDHAA LQKALEGDFG KKLQSAKNPM
IIVGSGVTDH GDANAFYETV GKFVDSNASN FLTEEWNGYN VLQRAASRVG AFEVGFTVPS
AEIAQTKPKF VWLLGADEFN EADIPKDAFI VYQGHHGDRG AQIADIVLPG AAYTEKAGTY
VNTEGRVQMT RAATGLPGAA RTDWKILRAV SEYLGVRLPY DDVAQLRDRM VEISPALSSY
DIIEPPSLQQ LSKVQLVEQN QGATATNEPL KKVIENFYFT DAISRSSPTM ARCSAAKKTG
DPRTNFMAPG MEEDRPMGQI AYGA
//
