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P24918 (NDUS1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 78 kDa subunit, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
Complex I-78kD
Short name=CI-78kD
Gene names
Name:nuo78
ORF Names:B17C10.90, NCU01765
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora

Protein attributes

Sequence length744 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. 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.

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 40 different subunits.

Subcellular location

Mitochondrion inner membrane.

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 – 3333Mitochondrion Ref.1
Chain34 – 744711NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
PRO_0000019974

Regions

Domain34 – 112792Fe-2S ferredoxin-type
Domain251 – 307574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding681Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding791Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding821Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding961Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1281Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1321Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1351Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1851Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1881Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2321Iron-sulfur 3 (4Fe-4S) By similarity

Experimental info

Sequence conflict1251L → P in CAA40828. Ref.1
Sequence conflict1521G → R in CAA40828. Ref.1
Sequence conflict1641R → Q in CAA40828. Ref.1
Sequence conflict3401P → A in CAA40828. Ref.1
Sequence conflict379 – 38810SGHKPLAHGV → FGPQTSCSWC in CAA40828. Ref.1
Sequence conflict4931A → R in CAA40828. Ref.1
Sequence conflict527 – 5348SRVGAFEV → PESAPSRL in CAA40828. Ref.1
Sequence conflict666 – 6672PS → SL in CAA40828. Ref.1
Sequence conflict7221P → S in CAA40828. Ref.1
Sequence conflict727 – 7293MAP → IGS in CAA40828. Ref.1
Sequence conflict7401I → Y in CAA40828. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24918 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: D842DDCE80510929

FASTA74481,602
        10         20         30         40         50         60 
MLRSTLSRSA WRTGRHQAAR NASRAFSATA QRPAEVELTI DGKKVSIEAG SALIQACEKA 

        70         80         90        100        110        120 
GVTIPRYCYH EKLMIAGNCR MCLVEVEKVP KPVASCAWPV QPGMVVKTNS PLTHKAREGV 

       130        140        150        160        170        180 
MEFLLANHPL DCPICDQGGE CDLQDQSMRY GGDRGRFHEV GGKRAVEDKN MGPLIKTSMN 

       190        200        210        220        230        240 
RCIQCTRCVR FANDIAGAPE LGSTGRGNDL QIGTYLEKNL DSELSGNVID LCPVGALTSK 

       250        260        270        280        290        300 
PYAFRARPWE LKKTESIDVL DGLGSNIRVD TRGLEVMRIL PRLNDEVNEE WINDKTRFAC 

       310        320        330        340        350        360 
DGLKTQRLTI PLVRREGKFE PASWDQALTE IAHAYQTLNP QGNEFKAIAG QLTEVESLVA 

       370        380        390        400        410        420 
MKDLANRLGS ENLALDMPSG HKPLAHGVDV RSNYIFNSSI VGIESADVIL LVGTNPRHEA 

       430        440        450        460        470        480 
AVLNARIRKQ WLRSDLEIGV VGQTWDSTFE FEHLGTDHAA LQKALEGDFG KKLQSAKNPM 

       490        500        510        520        530        540 
IIVGSGVTDH GDANAFYETV GKFVDSNASN FLTEEWNGYN VLQRAASRVG AFEVGFTVPS 

       550        560        570        580        590        600 
AEIAQTKPKF VWLLGADEFN EADIPKDAFI VYQGHHGDRG AQIADIVLPG AAYTEKAGTY 

       610        620        630        640        650        660 
VNTEGRVQMT RAATGLPGAA RTDWKILRAV SEYLGVRLPY DDVAQLRDRM VEISPALSSY 

       670        680        690        700        710        720 
DIIEPPSLQQ LSKVQLVEQN QGATATNEPL KKVIENFYFT DAISRSSPTM ARCSAAKKTG 

       730        740 
DPRTNFMAPG MEEDRPMGQI AYGA 

« Hide

References

« Hide 'large scale' references
[1]"Primary structures of two subunits of NADH: ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus."
Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Roehlen D.-A., van der Pas J.C., Sackmann U., Schneider R., Werner S., Weiss H.
Biochim. Biophys. Acta 1090:133-138(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-64.
Strain: 74-ORS-6a / FGSC 4200.
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57602 mRNA. Translation: CAA40828.1.
AL355926 Genomic DNA. Translation: CAB91229.1.
CM002237 Genomic DNA. Translation: EAA27952.3.
PIRS17664.
T49428.
RefSeqXP_957188.2. XM_952095.2.

3D structure databases

ProteinModelPortalP24918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU01765.1.

Protein family/group databases

TCDB3.D.1.6.2. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000001842; EFNCRP00000001842; EFNCRG00000001840.
GeneID3873340.
KEGGncr:NCU01765.

Phylogenomic databases

eggNOGCOG1034.
HOGENOMHOG000031442.
KOK03934.
OrthoDBEOG7KWSS1.

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.
PF00111. Fer2. 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...

Entry information

Entry nameNDUS1_NEUCR
AccessionPrimary (citable) accession number: P24918
Secondary accession number(s): Q7RV66, Q9P6E0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 1, 2001
Last modified: March 19, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families