Reviewed, UniProtKB/Swiss-Prot P24917 (NDUV1_NEUCR)

Names and origin

Protein names

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 names

Name:	nuo-51
ORF Names:	B10H18.210, NCU04044

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 = NAD+ + ubiquinol. 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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Inferred from electronic annotation. Source: InterPro NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion
	Chain	28 – 493	466	NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial		PRO_0000019980
Regions
	Nucleotide binding	96 – 105	10	NAD By similarity
	Nucleotide binding	212 – 259	48	FMN By similarity
Sites
	Metal binding	391	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	394	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	397	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	437	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	260 – 261	2	VA → AV in CAA39676. Ref.1
	Sequence conflict	442	1	A → R in CAA39676. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24917-1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 351B01F00602B06E	FASTA	493	54,241
	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

References

	« Hide 'large scale' referencesShow '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: 1832016] [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: 12655011] [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: 12712197] [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
EMBLGenBankDDBJ	X56227 mRNA. Translation: CAA39676.1. BX897678 Genomic DNA. Translation: CAE85605.1. AABX02000012 Genomic DNA. Translation: EAA28423.1.
PIR	S17663.
RefSeq	XP_957659.1.
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	3.D.1.6.2. proton-translocating NADH dehydrogenase (NDH) family.
Genome annotation databases
GeneID	3873830.
KEGG	ncr:NCU04044.
NMPDR	fig|5141.1.peg.1296.
Enzyme and pathway databases
BRENDA	1.6.5.3. 266. 1.6.99.3. 266.
Family and domain databases
InterPro	IPR001949. 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]
Pfam	PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view]
TIGRFAMs	TIGR01959. nuoF_fam. 1 hit.
PROSITE	PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUV1_NEUCR

Accession

Primary (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:	June 16, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)