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NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-78kD) (CI-78kD)

 NDUS1_NEUCR             Reviewed;         744 AA.
P24918; Q7RV66; Q9P6E0;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
23-MAY-2018, entry version 160.
RecName: Full=NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial;
EC=1.6.5.3;
EC=1.6.99.3;
AltName: Full=Complex I-78kD;
Short=CI-78kD;
Flags: Precursor;
Name=nuo78; ORFNames=B17C10.90, NCU01765;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-64.
STRAIN=74-ORS-6a / FGSC 4200;
PubMed=1832016; DOI=10.1016/0167-4781(91)90049-R;
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.;
"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.";
Biochim. Biophys. Acta 1090:133-138(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- FUNCTION: 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 ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
ubiquinol + 4 H(+)(Out).
-!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250};
-!- SUBUNIT: Complex I is composed of about 40 different subunits.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
-!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X57602; CAA40828.1; -; mRNA.
EMBL; AL355926; CAB91229.1; -; Genomic_DNA.
EMBL; CM002237; EAA27952.3; -; Genomic_DNA.
PIR; S17664; S17664.
PIR; T49428; T49428.
RefSeq; XP_957188.3; XM_952095.3.
ProteinModelPortal; P24918; -.
TCDB; 3.D.1.6.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
EnsemblFungi; EAA27952; EAA27952; NCU01765.
GeneID; 3873340; -.
KEGG; ncr:NCU01765; -.
EuPathDB; FungiDB:NCU01765; -.
HOGENOM; HOG000031442; -.
InParanoid; P24918; -.
KO; K03934; -.
OrthoDB; EOG092C0T2O; -.
Proteomes; UP000001805; Chromosome 6, Linkage Group II.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
CDD; cd00207; fer2; 1.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
InterPro; IPR015405; NuoG_C.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
Pfam; PF09326; NADH_dhqG_C; 1.
SMART; SM00929; NADH-G_4Fe-4S_3; 1.
SUPFAM; SSF54292; SSF54292; 1.
TIGRFAMs; TIGR01973; NuoG; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51839; 4FE4S_HC3; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00641; COMPLEX1_75K_1; 1.
PROSITE; PS00642; COMPLEX1_75K_2; 1.
PROSITE; PS00643; COMPLEX1_75K_3; 1.
1: Evidence at protein level;
2Fe-2S; 4Fe-4S; Complete proteome; Direct protein sequencing;
Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
Reference proteome; Respiratory chain; Transit peptide; Transport;
Ubiquinone.
TRANSIT 1 33 Mitochondrion.
{ECO:0000269|PubMed:1832016}.
CHAIN 34 744 NADH-ubiquinone oxidoreductase 78 kDa
subunit, mitochondrial.
/FTId=PRO_0000019974.
DOMAIN 34 112 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 112 151 4Fe-4S His(Cys)3-ligated-type.
{ECO:0000255|PROSITE-ProRule:PRU01184}.
DOMAIN 251 307 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 68 68 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 79 79 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 82 82 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 96 96 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
METAL 128 128 Iron-sulfur 2 (4Fe-4S); via tele
nitrogen. {ECO:0000255|PROSITE-
ProRule:PRU01184}.
METAL 132 132 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 135 135 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 141 141 Iron-sulfur 2 (4Fe-4S).
{ECO:0000255|PROSITE-ProRule:PRU01184}.
METAL 182 182 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 185 185 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 188 188 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
METAL 232 232 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
CONFLICT 125 125 L -> P (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 152 152 G -> R (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 164 164 R -> Q (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 340 340 P -> A (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 379 388 SGHKPLAHGV -> FGPQTSCSWC (in Ref. 1;
CAA40828). {ECO:0000305}.
CONFLICT 493 493 A -> R (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 527 534 SRVGAFEV -> PESAPSRL (in Ref. 1;
CAA40828). {ECO:0000305}.
CONFLICT 666 667 PS -> SL (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 722 722 P -> S (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 727 729 MAP -> IGS (in Ref. 1; CAA40828).
{ECO:0000305}.
CONFLICT 740 740 I -> Y (in Ref. 1; CAA40828).
{ECO:0000305}.
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


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