NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P24918 (NDUS1_NEUCR)

Last modified June 16, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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 names

Name:	nuo-78
ORF Names:	B17C10.90, NCU01765

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	744 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 = NAD⁺ + ubiquinol. 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.
Sequence caution	The sequence EAA27952.2 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro 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	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 33

Mitochondrion Ref.1

Chain

34 – 744

711

NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial

PRO_0000019974

Regions

Domain

34 – 112

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

128

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

132

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

135

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

141

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

182

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

185

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

188

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

232

Iron-sulfur 3 (4Fe-4S) By similarity

Experimental info

Sequence conflict

125

L → P in CAA40828. Ref.1

Sequence conflict

152

G → R in CAA40828. Ref.1

Sequence conflict

164

R → Q in CAA40828. Ref.1

Sequence conflict

340

P → A in CAA40828. Ref.1

Sequence conflict

379 – 388

SGHKPLAHGV → FGPQTSCSWC in CAA40828. Ref.1

Sequence conflict

493

A → R in CAA40828. Ref.1

Sequence conflict

527 – 534

SRVGAFEV → PESAPSRL in CAA40828. Ref.1

Sequence conflict

666 – 667

PS → SL in CAA40828. Ref.1

Sequence conflict

722

P → S in CAA40828. Ref.1

Sequence conflict

727 – 729

MAP → IGS in CAA40828. Ref.1

Sequence conflict

740

I → Y in CAA40828. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P24918-1 [UniParc].

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

744

81,602

        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

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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], 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: 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. 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.

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Cross-references

Sequence databases
	X57602 mRNA. Translation: CAA40828.1. AL355926 Genomic DNA. Translation: CAB91229.1. AABX02000005 Genomic DNA. Translation: EAA27952.2. Sequence problems.
PIR	S17664. T49428.
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	3.D.1.6.2. proton-translocating NADH dehydrogenase (NDH) family.
Genome annotation databases
NMPDR	fig\|5141.1.peg.6137.
Enzyme and pathway databases
BioCyc	NCRA-XX3-01:NCRA-XX3-01-005475-MON.
BRENDA	1.6.5.3. 266. 1.6.99.3. 266.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

NDUS1_NEUCR

Accession

Primary (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:	June 16, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents