Skip Header

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

NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial

Gene

nuo-51

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FMNCuratedNote: Binds 1 FMN.Curated
  • [4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi391 – 3911Iron-sulfur (4Fe-4S)Sequence Analysis
Metal bindingi394 – 3941Iron-sulfur (4Fe-4S)Sequence Analysis
Metal bindingi397 – 3971Iron-sulfur (4Fe-4S)Sequence Analysis
Metal bindingi437 – 4371Iron-sulfur (4Fe-4S)Sequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 10510NADBy similarity
Nucleotide bindingi212 – 25948FMNBy similarityAdd
BLAST

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. FMN binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

4Fe-4S, Flavoprotein, FMN, 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 51 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-51kD
Short name:
CI-51kD
Gene namesi
Name:nuo-51
ORF Names:B10H18.210, NCU04044
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 5, Linkage Group VI

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
  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 – 2727MitochondrionAdd
BLAST
Chaini28 – 493466NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrialPRO_0000019980Add
BLAST

Interactioni

Subunit structurei

Complex I is composed of about 40 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme.

Protein-protein interaction databases

STRINGi5141.NCU04044.1.

Structurei

3D structure databases

ProteinModelPortaliP24917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I 51 kDa subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1894.
HOGENOMiHOG000251534.
InParanoidiP24917.
KOiK03942.
OMAiNEPCTVE.
OrthoDBiEOG7M3J8B.

Family and domain databases

InterProiIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. Nuo51_FMN-bd.
IPR019575. Nuop51_4Fe4S-bd.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamiPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTiSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01959. nuoF_fam. 1 hit.
PROSITEiPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRTAAPTK ASARTLSRAA AEQCRTFATV QDGSANPVRH YGGLKDQDRI
60 70 80 90 100
FQNLYGRYPP DLKHAKKMGD WHKTKEILLK GHDWIIGEVK ASGLRGRGGA
110 120 130 140 150
GFPSGLKWSF MNFKDWDKDD KPRYLVVNAD EGEPGTCKDR EIMRKDPHKL
160 170 180 190 200
VEGCLVAGRA MNATAAYIYI RGEFIQEAAI LQNAINEAYA DGLIGKNACG
210 220 230 240 250
SGYDFDVYLH RGAGAYVCGE ETSLIESLEG KPGKPRLKPP FPAAVGLFGC
260 270 280 290 300
PSTVANVETV AVAPTICRRG GNWFAGFGRE RNQGTKLFCI SGHVNNPCTV
310 320 330 340 350
EEEMSIPMRE LIDKHCGGVR GGWDNLLAVI PGGSSTPILP KHICDTQLMD
360 370 380 390 400
FDALKDSQSG LGTAALIVMD KSTDVVRAIS RLSHFYRHES CGQCTPCREG
410 420 430 440 450
SKWTEQIMKR FEKGQGRERE IDMLQELTKQ VEGHTICALG EAFAWPIQGL
460 470 480 490
IRHFRPELEA RIRKFAQENG GEALAGGWQR NARQQGKLVS PGM
Length:493
Mass (Da):54,241
Last modified:June 7, 2005 - v2
Checksum:i351B01F00602B06E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2612VA → AV in CAA39676 (PubMed:1832016).Curated
Sequence conflicti442 – 4421A → R in CAA39676 (PubMed:1832016).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56227 mRNA. Translation: CAA39676.1.
BX897678 Genomic DNA. Translation: CAE85605.1.
CM002241 Genomic DNA. Translation: EAA28423.1.
PIRiS17663.
RefSeqiXP_957659.1. XM_952566.1.

Genome annotation databases

EnsemblFungiiEFNCRT00000003696; EFNCRP00000003696; EFNCRG00000003692.
GeneIDi3873830.
KEGGincr:NCU04044.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56227 mRNA. Translation: CAA39676.1.
BX897678 Genomic DNA. Translation: CAE85605.1.
CM002241 Genomic DNA. Translation: EAA28423.1.
PIRiS17663.
RefSeqiXP_957659.1. XM_952566.1.

3D structure databases

ProteinModelPortaliP24917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU04044.1.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003696; EFNCRP00000003696; EFNCRG00000003692.
GeneIDi3873830.
KEGGincr:NCU04044.

Phylogenomic databases

eggNOGiCOG1894.
HOGENOMiHOG000251534.
InParanoidiP24917.
KOiK03942.
OMAiNEPCTVE.
OrthoDBiEOG7M3J8B.

Family and domain databases

InterProiIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. Nuo51_FMN-bd.
IPR019575. Nuop51_4Fe4S-bd.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamiPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTiSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01959. nuoF_fam. 1 hit.
PROSITEiPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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].
    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 nameiNDUV1_NEUCR
AccessioniPrimary (citable) accession number: P24917
Secondary accession number(s): Q7RV82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 7, 2005
Last modified: January 7, 2015
This is version 119 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.