NDUS1_DROME
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 03-AUG-2022, entry version 192.
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 AlphaFoldDB; Q94511; -.
DR SMR; Q94511; -.
DR BioGRID; 58223; 30.
DR DIP; DIP-17348N; -.
DR IntAct; Q94511; 1.
DR MINT; Q94511; -.
DR STRING; 7227.FBpp0071128; -.
DR PaxDb; Q94511; -.
DR EnsemblMetazoa; FBtr0071180; FBpp0071128; FBgn0017566.
DR EnsemblMetazoa; FBtr0071181; FBpp0071129; FBgn0017566.
DR GeneID; 31762; -.
DR KEGG; dme:Dmel_CG2286; -.
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; HKNVGPL; -.
DR OrthoDB; 1095510at2759; -.
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 tissues.
DR ExpressionAtlas; Q94511; baseline and differential.
DR Genevisible; Q94511; DM.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS: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; IBA:GO_Central.
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; ISS:FlyBase.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:FlyBase.
DR CDD; cd00207; fer2; 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; NuoG_C.
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; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 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 2: Evidence at transcript level;
KW 2Fe-2S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane;
KW 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
