Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q94511

- NDUS1_DROME

UniProt

Q94511 - NDUS1_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene

ND75

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

Binds 1 2Fe-2S cluster per subunit.By similarity
Binds 2 4Fe-4S clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi85 – 851Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi88 – 881Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi102 – 1021Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi134 – 1341Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi138 – 1381Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi147 – 1471Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi190 – 1901Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi193 – 1931Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi196 – 1961Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi240 – 2401Iron-sulfur 3 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. electron carrier activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. NADH dehydrogenase (ubiquinone) activity Source: RefGenome

GO - Biological processi

  1. ATP synthesis coupled electron transport Source: InterPro
  2. cellular respiration Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Names & Taxonomyi

Protein namesi
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 namesi
Name:ND75
ORF Names:CG2286
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0017566. ND75.

Subcellular locationi

Mitochondrion inner membrane By similarity
Note: Matrix and cytoplasmic side of the mitochondrial inner membrane.By similarity

GO - Cellular componenti

  1. mitochondrial respiratory chain complex I Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 731704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000019971Add
BLAST

Proteomic databases

PaxDbiQ94511.
PRIDEiQ94511.

Expressioni

Gene expression databases

BgeeiQ94511.
ExpressionAtlasiQ94511. differential.

Interactioni

Subunit structurei

Complex I is composed of about 45 different subunits.By similarity

Protein-protein interaction databases

BioGridi58223. 24 interactions.
DIPiDIP-17348N.
IntActiQ94511. 1 interaction.
MINTiMINT-868919.

Structurei

3D structure databases

ProteinModelPortaliQ94511.
SMRiQ94511. Positions 42-725.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 118792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini259 – 315574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1034.
GeneTreeiENSGT00390000018768.
HOGENOMiHOG000264012.
InParanoidiQ94511.
KOiK03934.
OMAiFQGNDVA.
OrthoDBiEOG783MTP.
PhylomeDBiQ94511.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q94511-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIRAPLVKAL GALGSPTHQM ASRAVRTSAM VAQTPAKAPE KIEVFVDDIP
60 70 80 90 100
VQVVPGTTVL QAAAQIGVEI PRFCYHERLA VAGNCRMCLV EVEKSPKPVA
110 120 130 140 150
ACAMPVMKGW RIKTNSDLTR KAREGVMEFL LMNHPLDCPI CDQGGECDLQ
160 170 180 190 200
DQAMAFGSDR SRFTDINYTG KRAVEDKDIG PLVKTIMTRC IHCTRCVRFA
210 220 230 240 250
SEIAGVDDLG TTGRGNDMQI GTYVEKLFLT ELSGNVIDLC PVGALTNKPY
260 270 280 290 300
SFVARPWEIR KVSSIDVLDA VGSNIVVSTR TNEVLRILPR ENEDVNEEWL
310 320 330 340 350
ADKSRFACDG LKRQRLVAPM VRMPNGELQA VEWEGALIAV AKAIKAAGGQ
360 370 380 390 400
IAGISGQLAD LEAQVALKDL LNRLGSEVVA TEQGFIAGGT DNRANYLLNS
410 420 430 440 450
TIAGLEEADA VLLVGTNPRY EAPLVNTRLR KAYVHNELQI ASIGPKIDLS
460 470 480 490 500
YDHENLGADA ALVKDVCSGA HAFSKVLEGA KKPAIIIGAD LLERADGAAI
510 520 530 540 550
HATVAEYCKK LKKPNWNPFN VLQTNAAQVG ALDVGYKAGA QTAVKAQPKV
560 570 580 590 600
LFLLNADAGK VTREQLPKDC FVVYIGSHGD NGASIADAVL PGAAYTEKQG
610 620 630 640 650
IYVNTEGRPQ QTLPGVSPPG MAREDWKILR ALSEVVGKPL PYDNLDELRN
660 670 680 690 700
RLEDVAPHLT RLGQLEPAGD AGAAGTISKS IGGGAIDIKL KELRDYFMTD
710 720 730
AISRASPTMA KCISAVNKQQ RENEAKQSVA I
Length:731
Mass (Da):78,630
Last modified:February 21, 2001 - v3
Checksum:iB3CA26B56AFACBFD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651Q → L in CAA70284. (PubMed:10071211)Curated
Sequence conflicti94 – 941K → N in CAA70284. (PubMed:10071211)Curated
Sequence conflicti111 – 1111R → P in CAA70284. (PubMed:10071211)Curated
Sequence conflicti120 – 1201R → P in CAA70284. (PubMed:10071211)Curated
Sequence conflicti470 – 4701A → S in CAA70284. (PubMed:10071211)Curated
Sequence conflicti611 – 6111Q → H in CAA70284. (PubMed:10071211)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF46356.1.
Y09063 mRNA. Translation: CAA70284.1.
RefSeqiNP_511083.1. NM_078528.3.
NP_727255.1. NM_167152.2.
UniGeneiDm.6840.

Genome annotation databases

EnsemblMetazoaiFBtr0071180; FBpp0071128; FBgn0017566.
FBtr0071181; FBpp0071129; FBgn0017566.
GeneIDi31762.
KEGGidme:Dmel_CG2286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF46356.1 .
Y09063 mRNA. Translation: CAA70284.1 .
RefSeqi NP_511083.1. NM_078528.3.
NP_727255.1. NM_167152.2.
UniGenei Dm.6840.

3D structure databases

ProteinModelPortali Q94511.
SMRi Q94511. Positions 42-725.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58223. 24 interactions.
DIPi DIP-17348N.
IntActi Q94511. 1 interaction.
MINTi MINT-868919.

Proteomic databases

PaxDbi Q94511.
PRIDEi Q94511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071180 ; FBpp0071128 ; FBgn0017566 .
FBtr0071181 ; FBpp0071129 ; FBgn0017566 .
GeneIDi 31762.
KEGGi dme:Dmel_CG2286.

Organism-specific databases

CTDi 31762.
FlyBasei FBgn0017566. ND75.

Phylogenomic databases

eggNOGi COG1034.
GeneTreei ENSGT00390000018768.
HOGENOMi HOG000264012.
InParanoidi Q94511.
KOi K03934.
OMAi FQGNDVA.
OrthoDBi EOG783MTP.
PhylomeDBi Q94511.

Miscellaneous databases

GenomeRNAii 31762.
NextBioi 775179.
PROi Q94511.

Gene expression databases

Bgeei Q94511.
ExpressionAtlasi Q94511. differential.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SUPFAMi SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR01973. NuoG. 1 hit.
PROSITEi PS51085. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. 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.

Entry informationi

Entry nameiNDUS1_DROME
AccessioniPrimary (citable) accession number: Q94511
Secondary accession number(s): Q9W3H1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 21, 2001
Last modified: October 29, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3