ID   NDUS1_DROME             Reviewed;         731 AA.
AC   Q94511; Q9W3H1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 3.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial;
DE            EC=7.1.1.2;
DE   AltName: Full=Complex I-75kD;
DE            Short=CI-75kD;
DE   Flags: Precursor;
GN   Name=ND-75 {ECO:0000312|FlyBase:FBgn0017566}; Synonyms=ND75;
GN   ORFNames=CG2286 {ECO:0000312|FlyBase:FBgn0017566};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-653.
RC   TISSUE=Ovary;
RX   PubMed=10071211; DOI=10.1007/s004380050942;
RA   Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA   Barsanti P.;
RT   "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT   of a collection of D. melanogaster cDNAs homologous to sequences in the
RT   Human Gene Index database.";
RL   Mol. Gen. Genet. 261:64-70(1999).
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 (By
CC       similarity). This is the largest subunit of complex I and it is a
CC       component of the iron-sulfur (IP) fragment of the enzyme. It may form
CC       part of the active site crevice where NADH is oxidized (By similarity).
CC       {ECO:0000250}.
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 45 different subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC       Note=Matrix and cytoplasmic side of the mitochondrial inner membrane.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE014298; AAF46356.1; -; Genomic_DNA.
DR   EMBL; Y09063; CAA70284.1; -; mRNA.
DR   RefSeq; NP_511083.1; NM_078528.3.
DR   RefSeq; NP_727255.1; NM_167152.2.
DR   PDB; 8B9Z; EM; 3.28 A; G=1-731.
DR   PDB; 8BA0; EM; 3.68 A; G=1-731.
DR   PDB; 8ESW; EM; 3.30 A; S1=1-731.
DR   PDB; 8ESZ; EM; 3.40 A; S1=1-731.
DR   PDBsum; 8B9Z; -.
DR   PDBsum; 8BA0; -.
DR   PDBsum; 8ESW; -.
DR   PDBsum; 8ESZ; -.
DR   AlphaFoldDB; Q94511; -.
DR   EMDB; EMD-15936; -.
DR   EMDB; EMD-15937; -.
DR   EMDB; EMD-28581; -.
DR   EMDB; EMD-28582; -.
DR   SMR; Q94511; -.
DR   BioGRID; 58223; 30.
DR   DIP; DIP-17348N; -.
DR   IntAct; Q94511; 1.
DR   MINT; Q94511; -.
DR   STRING; 7227.FBpp0071128; -.
DR   PaxDb; 7227-FBpp0071128; -.
DR   EnsemblMetazoa; FBtr0071180; FBpp0071128; FBgn0017566.
DR   EnsemblMetazoa; FBtr0071181; FBpp0071129; FBgn0017566.
DR   GeneID; 31762; -.
DR   KEGG; dme:Dmel_CG2286; -.
DR   AGR; FB:FBgn0017566; -.
DR   CTD; 31762; -.
DR   FlyBase; FBgn0017566; ND-75.
DR   VEuPathDB; VectorBase:FBgn0017566; -.
DR   eggNOG; KOG2282; Eukaryota.
DR   GeneTree; ENSGT00940000153514; -.
DR   HOGENOM; CLU_000422_11_6_1; -.
DR   InParanoid; Q94511; -.
DR   OMA; QDQAMAY; -.
DR   OrthoDB; 19999at2759; -.
DR   PhylomeDB; Q94511; -.
DR   Reactome; R-DME-611105; Respiratory electron transport.
DR   Reactome; R-DME-6799198; Complex I biogenesis.
DR   BioGRID-ORCS; 31762; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31762; -.
DR   PRO; PR:Q94511; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0017566; Expressed in second segment of antenna (Drosophila) and 36 other cell types or tissues.
DR   ExpressionAtlas; Q94511; baseline and differential.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:FlyBase.
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:0045333; P:cellular respiration; ISS:FlyBase.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IC:FlyBase.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:FlyBase.
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.
DR   Genevisible; Q94511; DM.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; 4Fe-4S; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW   Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW   Translocase; Transport; Ubiquinone.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..731
FT                   /note="NADH-ubiquinone oxidoreductase 75 kDa subunit,
FT                   mitochondrial"
FT                   /id="PRO_0000019971"
FT   DOMAIN          40..118
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          118..157
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   DOMAIN          259..315
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         74
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         138
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         147
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT   BINDING         190
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        65
FT                   /note="Q -> L (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="K -> N (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="R -> P (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="R -> P (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="A -> S (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611
FT                   /note="Q -> H (in Ref. 3; CAA70284)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   731 AA;  78630 MW;  B3CA26B56AFACBFD CRC64;
     MIRAPLVKAL GALGSPTHQM ASRAVRTSAM VAQTPAKAPE KIEVFVDDIP VQVVPGTTVL
     QAAAQIGVEI PRFCYHERLA VAGNCRMCLV EVEKSPKPVA ACAMPVMKGW RIKTNSDLTR
     KAREGVMEFL LMNHPLDCPI CDQGGECDLQ DQAMAFGSDR SRFTDINYTG KRAVEDKDIG
     PLVKTIMTRC IHCTRCVRFA SEIAGVDDLG TTGRGNDMQI GTYVEKLFLT ELSGNVIDLC
     PVGALTNKPY SFVARPWEIR KVSSIDVLDA VGSNIVVSTR TNEVLRILPR ENEDVNEEWL
     ADKSRFACDG LKRQRLVAPM VRMPNGELQA VEWEGALIAV AKAIKAAGGQ IAGISGQLAD
     LEAQVALKDL LNRLGSEVVA TEQGFIAGGT DNRANYLLNS TIAGLEEADA VLLVGTNPRY
     EAPLVNTRLR KAYVHNELQI ASIGPKIDLS YDHENLGADA ALVKDVCSGA HAFSKVLEGA
     KKPAIIIGAD LLERADGAAI HATVAEYCKK LKKPNWNPFN VLQTNAAQVG ALDVGYKAGA
     QTAVKAQPKV LFLLNADAGK VTREQLPKDC FVVYIGSHGD NGASIADAVL PGAAYTEKQG
     IYVNTEGRPQ QTLPGVSPPG MAREDWKILR ALSEVVGKPL PYDNLDELRN RLEDVAPHLT
     RLGQLEPAGD AGAAGTISKS IGGGAIDIKL KELRDYFMTD AISRASPTMA KCISAVNKQQ
     RENEAKQSVA I
//