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UniProtKB/Swiss-Prot entry P22142


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NDUS2_NEUCR
Primary accession number P22142
Secondary accession number Q7RVM8
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on December 4, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name NADH-ubiquinone oxidoreductase 49 kDa subunit, mitochondrial [Precursor]
Synonyms EC 1.6.5.3
EC 1.6.99.3
Complex I-49kD
CI-49kD
Gene name
Name: nuo-49
ORFNames: NCU02534
From
Neurospora crassa [TaxID: 5141] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-62.
STRAIN=74-ORS-6a / FGSC 4200;
DOI=10.1007/BF00321116; PubMed=2147127 [NCBI, ExPASy, EBI, Israel, Japan]
Preis D., van der Pas J.C., Nehls U., Roehlen D.-A., Sackmann U., Jahnke U., Weiss H.;
"The 49 K subunit of NADH: ubiquinone reductase (complex I) from Neurospora crassa mitochondria: primary structure of the gene and the protein.";
Curr. Genet. 18:59-64(1990).
[2]
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.
  • CATALYTIC ACTIVITY: NADH + ubiquinone = NAD+ + ubiquinol.
  • CATALYTIC ACTIVITY: NADH + acceptor = NAD+ + reduced acceptor.
  • COFACTOR: Binds 1 4Fe-4S cluster.
  • SUBUNIT: Complex I is composed of about 40 different subunits.
  • SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
  • SIMILARITY: Belongs to the complex I 49 kDa subunit family.
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
X54508; CAA38368.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AABX02000006; EAA36429.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S13801; S13801.
RefSeq XP_965665.2; -.
3D structure databases
ModBase P22142.
Ontologies
GO
GO:0005746; Cellular component: mitochondrial respiratory chain (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:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0008137; Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900; Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
IPR010219; NADH_DH_1_dsu.
IPR001135; NADH_UbQ_OxRdtase_49kDa.
Graphical view of domain structure.
Pfam PF00346; Complex1_49kDa; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01962; NuoD; 1.
PROSITE PS00535; COMPLEX1_49K; 1.
ProtoNet P22142.
Genome annotation databases
GeneID 3881799; -.
KEGG ncr:NCU02534; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    42  42     Mitochondrion. 
CHAIN   43   478  436     NADH-ubiquinone oxidoreductase 49 kDa subunit, mitochondrial. PRO_0000019984
METAL   341   341        Iron-sulfur (4Fe-4S) (Potential). 
METAL   347   347        Iron-sulfur (4Fe-4S) (Potential). 
METAL   362   362        Iron-sulfur (4Fe-4S) (Potential). 
CONFLICT   417   417        A -> G (in Ref. 1; CAA38368). 
Sequence information
Length: 478 AA [This is the length of the unprocessed precursor] Molecular weight: 54019 Da [This is the MW of the unprocessed precursor] CRC64: 159C35BE3DF9D916 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATTLFRLAG RNAKRHCMRQ STTIAHNLNS TRAFSASALR RYAEPSYEGQ GTRLVPTGDD 

        70         80         90        100        110        120 
FAPNNDLYGL EALKADGAPR VPPQDHILAR KVRHYTVNFG PQHPAAHGVL RLILELKGEE 

       130        140        150        160        170        180 
IVRADPHVGL LHRGTEKLCE YRTYLQALPY FDRLDYVSMM TNEQCFALAV EKLLNVEIPE 

       190        200        210        220        230        240 
RAKWIRTMFA EITRILNHLM SVLSHAMDVG ALTPFLWGFE EREKLMEFYE RVSGARLHAA 

       250        260        270        280        290        300 
YVRPGGVHQD IPLGLLDDIY MWATQFGDRI DETEEMLTDN RIWIDRLRGI GVVSAADALN 

       310        320        330        340        350        360 
LSFTGVMLRG SGVPWDIRKS QPYDAYDQVE FDVPVGINGD CYDRYLCRME EFRQSLRIIH 

       370        380        390        400        410        420 
QCLNKMPAGP VRVEDYKISP PPRSAMKENM EALIHHFLLY TKGYAVPPGD TYSAIEAPKG 

       430        440        450        460        470 
EMGVYVVSDG SERPYRVHIR APGFAHLGGF DHLSRGHMLA DAVAVIGTMD LVFGEVDR 

P22142 in FASTA format

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View entry in raw text format (no links)
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