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P24918

- NDUS1_NEUCR

UniProt

P24918 - NDUS1_NEUCR

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Protein

NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial

Gene

nuo78

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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. 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 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 bindingi68 – 681Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi79 – 791Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi82 – 821Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi96 – 961Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi132 – 1321Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi135 – 1351Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi141 – 1411Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi185 – 1851Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi188 – 1881Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi232 – 2321Iron-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: UniProtKB-EC

GO - Biological processi

  1. ATP synthesis coupled electron transport Source: InterPro
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

Protein family/group databases

TCDBi3.D.1.6.2. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:nuo78
ORF Names:B17C10.90, NCU01765
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 6, Linkage Group II

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
  2. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
BLAST
Chaini34 – 744711NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrialPRO_0000019974Add
BLAST

Interactioni

Subunit structurei

Complex I is composed of about 40 different subunits.

Protein-protein interaction databases

STRINGi5141.NCU01765.1.

Structurei

3D structure databases

ProteinModelPortaliP24918.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 112792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini251 – 307574Fe-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.
HOGENOMiHOG000031442.
InParanoidiP24918.
KOiK03934.
OrthoDBiEOG7KWSS1.

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.
PF00111. Fer2. 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.

P24918-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRSTLSRSA WRTGRHQAAR NASRAFSATA QRPAEVELTI DGKKVSIEAG
60 70 80 90 100
SALIQACEKA GVTIPRYCYH EKLMIAGNCR MCLVEVEKVP KPVASCAWPV
110 120 130 140 150
QPGMVVKTNS PLTHKAREGV MEFLLANHPL DCPICDQGGE CDLQDQSMRY
160 170 180 190 200
GGDRGRFHEV GGKRAVEDKN MGPLIKTSMN RCIQCTRCVR FANDIAGAPE
210 220 230 240 250
LGSTGRGNDL QIGTYLEKNL DSELSGNVID LCPVGALTSK PYAFRARPWE
260 270 280 290 300
LKKTESIDVL DGLGSNIRVD TRGLEVMRIL PRLNDEVNEE WINDKTRFAC
310 320 330 340 350
DGLKTQRLTI PLVRREGKFE PASWDQALTE IAHAYQTLNP QGNEFKAIAG
360 370 380 390 400
QLTEVESLVA MKDLANRLGS ENLALDMPSG HKPLAHGVDV RSNYIFNSSI
410 420 430 440 450
VGIESADVIL LVGTNPRHEA AVLNARIRKQ WLRSDLEIGV VGQTWDSTFE
460 470 480 490 500
FEHLGTDHAA LQKALEGDFG KKLQSAKNPM IIVGSGVTDH GDANAFYETV
510 520 530 540 550
GKFVDSNASN FLTEEWNGYN VLQRAASRVG AFEVGFTVPS AEIAQTKPKF
560 570 580 590 600
VWLLGADEFN EADIPKDAFI VYQGHHGDRG AQIADIVLPG AAYTEKAGTY
610 620 630 640 650
VNTEGRVQMT RAATGLPGAA RTDWKILRAV SEYLGVRLPY DDVAQLRDRM
660 670 680 690 700
VEISPALSSY DIIEPPSLQQ LSKVQLVEQN QGATATNEPL KKVIENFYFT
710 720 730 740
DAISRSSPTM ARCSAAKKTG DPRTNFMAPG MEEDRPMGQI AYGA
Length:744
Mass (Da):81,602
Last modified:June 1, 2001 - v2
Checksum:iD842DDCE80510929
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251L → P in CAA40828. (PubMed:1832016)Curated
Sequence conflicti152 – 1521G → R in CAA40828. (PubMed:1832016)Curated
Sequence conflicti164 – 1641R → Q in CAA40828. (PubMed:1832016)Curated
Sequence conflicti340 – 3401P → A in CAA40828. (PubMed:1832016)Curated
Sequence conflicti379 – 38810SGHKPLAHGV → FGPQTSCSWC in CAA40828. (PubMed:1832016)Curated
Sequence conflicti493 – 4931A → R in CAA40828. (PubMed:1832016)Curated
Sequence conflicti527 – 5348SRVGAFEV → PESAPSRL in CAA40828. (PubMed:1832016)Curated
Sequence conflicti666 – 6672PS → SL in CAA40828. (PubMed:1832016)Curated
Sequence conflicti722 – 7221P → S in CAA40828. (PubMed:1832016)Curated
Sequence conflicti727 – 7293MAP → IGS in CAA40828. (PubMed:1832016)Curated
Sequence conflicti740 – 7401I → Y in CAA40828. (PubMed:1832016)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57602 mRNA. Translation: CAA40828.1.
AL355926 Genomic DNA. Translation: CAB91229.1.
CM002237 Genomic DNA. Translation: EAA27952.3.
PIRiS17664.
T49428.
RefSeqiXP_957188.2. XM_952095.2.

Genome annotation databases

EnsemblFungiiEFNCRT00000001842; EFNCRP00000001842; EFNCRG00000001840.
GeneIDi3873340.
KEGGincr:NCU01765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X57602 mRNA. Translation: CAA40828.1 .
AL355926 Genomic DNA. Translation: CAB91229.1 .
CM002237 Genomic DNA. Translation: EAA27952.3 .
PIRi S17664.
T49428.
RefSeqi XP_957188.2. XM_952095.2.

3D structure databases

ProteinModelPortali P24918.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU01765.1.

Protein family/group databases

TCDBi 3.D.1.6.2. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000001842 ; EFNCRP00000001842 ; EFNCRG00000001840 .
GeneIDi 3873340.
KEGGi ncr:NCU01765.

Phylogenomic databases

eggNOGi COG1034.
HOGENOMi HOG000031442.
InParanoidi P24918.
KOi K03934.
OrthoDBi EOG7KWSS1.

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.
PF00111. Fer2. 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. "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.
    , 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.

Entry informationi

Entry nameiNDUS1_NEUCR
AccessioniPrimary (citable) accession number: P24918
Secondary accession number(s): Q7RV66, Q9P6E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3