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P24917 (NDUV1_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:nuo-51
ORF Names:B10H18.210, NCU04044
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 length493 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.

Catalytic activity

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

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 FMN Potential.

Binds 1 4Fe-4S cluster Potential.

Subunit structure

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

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

Sequence similarities

Belongs to the complex I 51 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion
Chain28 – 493466NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial
PRO_0000019980

Regions

Nucleotide binding96 – 10510NAD By similarity
Nucleotide binding212 – 25948FMN By similarity

Sites

Metal binding3911Iron-sulfur (4Fe-4S) Potential
Metal binding3941Iron-sulfur (4Fe-4S) Potential
Metal binding3971Iron-sulfur (4Fe-4S) Potential
Metal binding4371Iron-sulfur (4Fe-4S) Potential

Experimental info

Sequence conflict260 – 2612VA → AV in CAA39676. Ref.1
Sequence conflict4421A → R in CAA39676. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24917 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 351B01F00602B06E

FASTA49354,241
        10         20         30         40         50         60 
MLSRTAAPTK ASARTLSRAA AEQCRTFATV QDGSANPVRH YGGLKDQDRI FQNLYGRYPP 

        70         80         90        100        110        120 
DLKHAKKMGD WHKTKEILLK GHDWIIGEVK ASGLRGRGGA GFPSGLKWSF MNFKDWDKDD 

       130        140        150        160        170        180 
KPRYLVVNAD EGEPGTCKDR EIMRKDPHKL VEGCLVAGRA MNATAAYIYI RGEFIQEAAI 

       190        200        210        220        230        240 
LQNAINEAYA DGLIGKNACG SGYDFDVYLH RGAGAYVCGE ETSLIESLEG KPGKPRLKPP 

       250        260        270        280        290        300 
FPAAVGLFGC PSTVANVETV AVAPTICRRG GNWFAGFGRE RNQGTKLFCI SGHVNNPCTV 

       310        320        330        340        350        360 
EEEMSIPMRE LIDKHCGGVR GGWDNLLAVI PGGSSTPILP KHICDTQLMD FDALKDSQSG 

       370        380        390        400        410        420 
LGTAALIVMD KSTDVVRAIS RLSHFYRHES CGQCTPCREG SKWTEQIMKR FEKGQGRERE 

       430        440        450        460        470        480 
IDMLQELTKQ VEGHTICALG EAFAWPIQGL IRHFRPELEA RIRKFAQENG GEALAGGWQR 

       490 
NARQQGKLVS PGM 

« 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].
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
X56227 mRNA. Translation: CAA39676.1.
BX897678 Genomic DNA. Translation: CAE85605.1.
CM002241 Genomic DNA. Translation: EAA28423.1.
PIRS17663.
RefSeqXP_957659.1. XM_952566.1.

3D structure databases

ProteinModelPortalP24917.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5141.NCU04044.1.

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

EnsemblFungiEFNCRT00000003696; EFNCRP00000003696; EFNCRG00000003692.
GeneID3873830.
KEGGncr:NCU04044.

Phylogenomic databases

eggNOGCOG1894.
HOGENOMHOG000251534.
KOK03942.
OMAKWSFMNP.
OrthoDBEOG7M3J8B.

Family and domain databases

InterProIPR001949. NADH-UbQ_OxRdtase_51kDa_CS.
IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. NADH_UbQ_OxRdtase_51kDa_su.
IPR019554. Soluble_ligand-bd.
[Graphical view]
PfamPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
SMARTSM00928. NADH_4Fe-4S. 1 hit.
[Graphical view]
TIGRFAMsTIGR01959. nuoF_fam. 1 hit.
PROSITEPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDUV1_NEUCR
AccessionPrimary (citable) accession number: P24917
Secondary accession number(s): Q7RV82
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 115 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