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Q94511 (NDUS1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).

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 membrane By 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.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 731704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
PRO_0000019971

Regions

Domain40 – 118792Fe-2S ferredoxin-type
Domain259 – 315574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding741Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding851Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding881Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1021Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1341Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1381Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1471Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1901Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1931Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1961Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2401Iron-sulfur 3 (4Fe-4S) By similarity

Experimental info

Sequence conflict651Q → L in CAA70284. Ref.3
Sequence conflict941K → N in CAA70284. Ref.3
Sequence conflict1111R → P in CAA70284. Ref.3
Sequence conflict1201R → P in CAA70284. Ref.3
Sequence conflict4701A → S in CAA70284. Ref.3
Sequence conflict6111Q → H in CAA70284. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q94511 [UniParc].

Last modified February 21, 2001. Version 3.
Checksum: B3CA26B56AFACBFD

FASTA73178,630
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-653.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF46356.1.
Y09063 mRNA. Translation: CAA70284.1.
RefSeqNP_511083.1. NM_078528.2.
NP_727255.1. NM_167152.2.
UniGeneDm.6840.

3D structure databases

ProteinModelPortalQ94511.
SMRQ94511. Positions 42-725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58223. 24 interactions.
DIPDIP-17348N.
IntActQ94511. 1 interaction.
MINTMINT-868919.

Proteomic databases

PaxDbQ94511.
PRIDEQ94511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0071180; FBpp0071128; FBgn0017566.
FBtr0071181; FBpp0071129; FBgn0017566.
GeneID31762.
KEGGdme:Dmel_CG2286.

Organism-specific databases

CTD31762.
FlyBaseFBgn0017566. ND75.

Phylogenomic databases

eggNOGCOG1034.
GeneTreeENSGT00390000018768.
HOGENOMHOG000264012.
InParanoidQ94511.
KOK03934.
OMAFQGNDVA.
OrthoDBEOG783MTP.
PhylomeDBQ94511.

Gene expression databases

BgeeQ94511.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi31762.
NextBio775179.
PROQ94511.

Entry information

Entry nameNDUS1_DROME
AccessionPrimary (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: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase