ID   NDUS2_NEUCR             Reviewed;         478 AA.
AC   P22142; Q7RVM8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   04-NOV-2008, entry version 77.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=Complex I-49kD;
DE            Short=CI-49kD;
DE   Flags: Precursor;
GN   Name=nuo-49; ORFNames=NCU02534;
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=5141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-62.
RC   STRAIN=74-ORS-6a / FGSC 4200;
RX   MEDLINE=91059421; PubMed=2147127; DOI=10.1007/BF00321116;
RA   Preis D., van der Pas J.C., Nehls U., Roehlen D.-A., Sackmann U.,
RA   Jahnke U., Weiss H.;
RT   "The 49 K subunit of NADH: ubiquinone reductase (complex I) from
RT   Neurospora crassa mitochondria: primary structure of the gene and the
RT   protein.";
RL   Curr. Genet. 18:59-64(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone.
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster.
CC   -!- SUBUNIT: Complex I is composed of about 40 different subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X54508; CAA38368.1; -; Genomic_DNA.
DR   EMBL; AABX02000006; EAA36429.2; -; Genomic_DNA.
DR   PIR; S13801; S13801.
DR   RefSeq; XP_965665.2; -.
DR   GeneID; 3881799; -.
DR   KEGG; ncr:NCU02534; -.
DR   GO; GO:0005746; C:mitochondrial respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR010219; NADH_DH_1_dsu.
DR   InterPro; IPR001135; NADH_UbQ_OxRdtase_49kDa.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Direct protein sequencing;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW   Respiratory chain; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1     42       Mitochondrion.
FT   CHAIN        43    478       NADH-ubiquinone oxidoreductase 49 kDa
FT                                subunit, mitochondrial.
FT                                /FTId=PRO_0000019984.
FT   METAL       341    341       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       347    347       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       362    362       Iron-sulfur (4Fe-4S) (Potential).
FT   CONFLICT    417    417       A -> G (in Ref. 1; CAA38368).
SQ   SEQUENCE   478 AA;  54019 MW;  159C35BE3DF9D916 CRC64;
     MATTLFRLAG RNAKRHCMRQ STTIAHNLNS TRAFSASALR RYAEPSYEGQ GTRLVPTGDD
     FAPNNDLYGL EALKADGAPR VPPQDHILAR KVRHYTVNFG PQHPAAHGVL RLILELKGEE
     IVRADPHVGL LHRGTEKLCE YRTYLQALPY FDRLDYVSMM TNEQCFALAV EKLLNVEIPE
     RAKWIRTMFA EITRILNHLM SVLSHAMDVG ALTPFLWGFE EREKLMEFYE RVSGARLHAA
     YVRPGGVHQD IPLGLLDDIY MWATQFGDRI DETEEMLTDN RIWIDRLRGI GVVSAADALN
     LSFTGVMLRG SGVPWDIRKS QPYDAYDQVE FDVPVGINGD CYDRYLCRME EFRQSLRIIH
     QCLNKMPAGP VRVEDYKISP PPRSAMKENM EALIHHFLLY TKGYAVPPGD TYSAIEAPKG
     EMGVYVVSDG SERPYRVHIR APGFAHLGGF DHLSRGHMLA DAVAVIGTMD LVFGEVDR
//