[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 34-64. STRAIN=74-ORS-6a / FGSC 4200; DOI=10.1016/0167-4781(91)90049-R; PubMed=1832016 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; Biochim. Biophys. Acta 1090:133-138(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1093/nar/gkg293; PubMed=12655011 [NCBI, ExPASy, EBI, Israel, Japan] Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.; "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."; Nucleic Acids Res. 31:1944-1954(2003).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987; DOI=10.1038/nature01554; PubMed=12712197 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The genome sequence of the filamentous fungus Neurospora crassa."; Nature 422:859-868(2003).

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.
CATALYTIC ACTIVITY: NADH + acceptor = NAD⁺ + reduced acceptor.
COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
SUBUNIT: Complex I is composed of about 40 different subunits.
SUBCELLULAR LOCATION: Mitochondrion inner membrane.
SIMILARITY: Belongs to the complex I 75 kDa subunit family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SEQUENCE CAUTION:
- Sequence=EAA27952.2; Type=Erroneous gene model prediction;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X57602; CAA40828.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355926; CAB91229.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000005; EAA27952.2; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17664; S17664.
T49428; T49428.

3D structure databases

ModBase

P24918.

Enzyme and pathway databases

BioCyc

NCRA-XX3-01:NCRA-XX3-01-005475-MON; -.

Ontologies

GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0042773;	Biological process: ATP synthesis coupled electron transport (inferred from electronic annotation from InterPro).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR001450; 4Fe4S_Fe_S_bd.
IPR001041; Ferredoxin.
IPR006656; Mopterin_OxRdtase.
IPR000283; NADH_DHase_75KDa_su_CS.
IPR010228; NADH_quinone_OxRdtase_G.
IPR015405; NuoG_C.
Graphical view of domain structure.

Pfam

PF09326; DUF1982; 1.
PF00111; Fer2; 1.
PF00384; Molybdopterin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.

TIGRFAMs

TIGR01973; NuoG; 1.

PROSITE

PS00197; 2FE2S_FER_1; FALSE_NEG.
PS51085; 2FE2S_FER_2; 1.
PS00641; COMPLEX1_75K_1; 1.
PS00642; COMPLEX1_75K_2; 1.
PS00643; COMPLEX1_75K_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P24918.

Genome annotation databases

NMPDR

fig|5141.1.peg.6137; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 4Fe-4S; Complete proteome; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Respiratory chain; Transit peptide; Transport; Ubiquinone.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 33`	`33`	`Mitochondrion.`
`CHAIN`	`34 744`	`711`	`NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial.`	`PRO_0000019974`
`DOMAIN`	`34 112`	`79`	`2Fe-2S ferredoxin-type.`
`METAL`	`68 68`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`79 79`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`82 82`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`96 96`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`128 128`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`132 132`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`135 135`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`141 141`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`182 182`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`185 185`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`188 188`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`METAL`	`232 232`		`Iron-sulfur 3 (4Fe-4S) (By similarity).`
`CONFLICT`	`125 125`		`L -> P (in Ref. 1; CAA40828).`
`CONFLICT`	`152 152`		`G -> R (in Ref. 1; CAA40828).`
`CONFLICT`	`164 164`		`R -> Q (in Ref. 1; CAA40828).`
`CONFLICT`	`340 340`		`P -> A (in Ref. 1; CAA40828).`
`CONFLICT`	`379 388`		`SGHKPLAHGV -> FGPQTSCSWC (in Ref. 1; CAA40828).`
`CONFLICT`	`493 493`		`A -> R (in Ref. 1; CAA40828).`
`CONFLICT`	`527 534`		`SRVGAFEV -> PESAPSRL (in Ref. 1; CAA40828).`
`CONFLICT`	`666 667`		`PS -> SL (in Ref. 1; CAA40828).`
`CONFLICT`	`722 722`		`P -> S (in Ref. 1; CAA40828).`
`CONFLICT`	`727 729`		`MAP -> IGS (in Ref. 1; CAA40828).`
`CONFLICT`	`740 740`		`I -> Y (in Ref. 1; CAA40828).`

Sequence information

Length: 744 AA [This is the length of the unprocessed precursor]

Molecular weight: 81602 Da [This is the MW of the unprocessed precursor]

CRC64: D842DDCE80510929 [This is a checksum on the sequence]

        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

P24918 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools