Reviewed, UniProtKB/Swiss-Prot Q94511 (NDUS1_DROME)

Names and origin

Protein names

Recommended name:
    NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    Complex I-75kD
      Short name=CI-75kD

Gene names

Name:	ND75
ORF Names:	CG2286

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	731 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 By similarity. 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 By similarity.
Catalytic activity	NADH + ubiquinone = NAD(+) + ubiquinol. NADH + acceptor = NAD(+) + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	Complex I is composed of about 45 different subunits By similarity.
Subcellular location	Mitochondrion inner membraneBy similarity. Note= Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 731	704	NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial		PRO_0000019971
Regions
	Domain	40 – 118	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	74	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	85	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	88	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	102	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	134	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	138	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	141	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	147	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	190	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	193	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	196	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	240	1	Iron-sulfur 3 (4Fe-4S) By similarity
Experimental info
	Sequence conflict	65	1	Q → L in CAA70284. Ref.3
	Sequence conflict	94	1	K → N in CAA70284. Ref.3
	Sequence conflict	111	1	R → P in CAA70284. Ref.3
	Sequence conflict	120	1	R → P in CAA70284. Ref.3
	Sequence conflict	470	1	A → S in CAA70284. Ref.3
	Sequence conflict	611	1	Q → H in CAA70284. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q94511-1 [UniParc]. Last modified February 21, 2001. Version 3. Checksum: B3CA26B56AFACBFD	FASTA	731	78,630
	10 20 30 40 50 60 MIRAPLVKAL GALGSPTHQM ASRAVRTSAM VAQTPAKAPE KIEVFVDDIP VQVVPGTTVL 70 80 90 100 110 120 QAAAQIGVEI PRFCYHERLA VAGNCRMCLV EVEKSPKPVA ACAMPVMKGW RIKTNSDLTR 130 140 150 160 170 180 KAREGVMEFL LMNHPLDCPI CDQGGECDLQ DQAMAFGSDR SRFTDINYTG KRAVEDKDIG 190 200 210 220 230 240 PLVKTIMTRC IHCTRCVRFA SEIAGVDDLG TTGRGNDMQI GTYVEKLFLT ELSGNVIDLC 250 260 270 280 290 300 PVGALTNKPY SFVARPWEIR KVSSIDVLDA VGSNIVVSTR TNEVLRILPR ENEDVNEEWL 310 320 330 340 350 360 ADKSRFACDG LKRQRLVAPM VRMPNGELQA VEWEGALIAV AKAIKAAGGQ IAGISGQLAD 370 380 390 400 410 420 LEAQVALKDL LNRLGSEVVA TEQGFIAGGT DNRANYLLNS TIAGLEEADA VLLVGTNPRY 430 440 450 460 470 480 EAPLVNTRLR KAYVHNELQI ASIGPKIDLS YDHENLGADA ALVKDVCSGA HAFSKVLEGA 490 500 510 520 530 540 KKPAIIIGAD LLERADGAAI HATVAEYCKK LKKPNWNPFN VLQTNAAQVG ALDVGYKAGA 550 560 570 580 590 600 QTAVKAQPKV LFLLNADAGK VTREQLPKDC FVVYIGSHGD NGASIADAVL PGAAYTEKQG 610 620 630 640 650 660 IYVNTEGRPQ QTLPGVSPPG MAREDWKILR ALSEVVGKPL PYDNLDELRN RLEDVAPHLT 670 680 690 700 710 720 RLGQLEPAGD AGAAGTISKS IGGGAIDIKL KELRDYFMTD AISRASPTMA KCISAVNKQQ 730 RENEAKQSVA I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"Identification of nuclear genes encoding mitochondrial proteins: isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database." Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R., Barsanti P. Mol. Gen. Genet. 261:64-70(1999) [PubMed: 10071211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-653. Tissue: Ovary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014298 Genomic DNA. Translation: AAF46356.1. Y09063 mRNA. Translation: CAA70284.1.
RefSeq	NP_511083.1. NP_727255.1.
UniGene	Dm.6840
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:17348N.
IntAct	Q94511.
Genome annotation databases
Ensembl	CG2286. Drosophila melanogaster. [Contig view]
GeneID	31762.
KEGG	dme:Dmel_CG2286.
Organism-specific databases
FlyBase	FBgn0017566. ND75.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001065-MON. DMEL-XXX-02:DMEL-XXX-02-001066-MON.
Gene expression databases
ArrayExpress	Q94511.
GermOnline	CG2286. Drosophila melanogaster.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_DHase_75KDa_su_CS. IPR010228. NADH_quinone_OxRdtase_G. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	775179.

Entry information

Entry name

NDUS1_DROME

Accession

Primary (citable) accession number: Q94511
Secondary accession number(s): Q9W3H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 21, 2001
Last modified:	November 25, 2008
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project