ID NDUS7_NEUCR Reviewed; 226 AA. AC O47950; Q7RZB4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 71. DE RecName: Full=NADH-ubiquinone oxidoreductase 19.3 kDa subunit, mitochondrial; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=Complex I-19.3kD; DE Short=CI-19.3kD; DE Flags: Precursor; GN ORFNames=G17A4.170, NCU03953; 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 [MRNA]. RX MEDLINE=99233617; PubMed=10216160; DOI=10.1016/S0005-2728(99)00014-6; RA Sousa R., Barquera B., Duarte M., Finel M., Videira A.; RT "Characterisation of the last Fe-S cluster-binding subunit of RT Neurospora crassa complex I."; RL Biochim. Biophys. Acta 1411:142-146(1999). 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=22542210; PubMed=12655011; DOI=10.1093/nar/gkg293; RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., RA Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., RA Schulte U.; RT "What's in the genome of a filamentous fungus? Analysis of the RT Neurospora genome sequence."; RL Nucleic Acids Res. 31:1944-1954(2003). RN [3] 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 (Potential). CC -!- SUBUNIT: Complex I is composed of about 40 different subunits. CC This is a component of the iron-sulfur (IP) fragment of the CC enzyme. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the complex I 20 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; AJ001520; CAA04802.1; -; mRNA. DR EMBL; BX908812; CAF06152.1; -; Genomic_DNA. DR EMBL; AABX02000012; EAA28356.1; -; Genomic_DNA. DR RefSeq; XP_957592.1; -. DR TCDB; 3.D.1.6.2; proton-translocating NADH dehydrogenase (NDH) family. DR GeneID; 3873682; -. DR KEGG; ncr:NCU03953; -. DR NMPDR; fig|5141.1.peg.1205; -. DR BioCyc; NCRA-XX3-01:NCRA-XX3-01-007701-MON; -. DR BRENDA; 1.6.5.3; 266. DR BRENDA; 1.6.99.3; 266. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C: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:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa. DR InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB. DR PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1. DR PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR TIGRFAMs; TIGR01957; nuoB_fam; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 2: Evidence at transcript level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Respiratory chain; KW Transit peptide; Transport; Ubiquinone. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 226 NADH-ubiquinone oxidoreductase 19.3 kDa FT subunit, mitochondrial. FT /FTId=PRO_0000020032. FT METAL 101 101 Iron-sulfur (4Fe-4S) (Potential). FT METAL 102 102 Iron-sulfur (4Fe-4S) (Potential). FT METAL 166 166 Iron-sulfur (4Fe-4S) (Potential). FT METAL 196 196 Iron-sulfur (4Fe-4S) (Potential). SQ SEQUENCE 226 AA; 24972 MW; E48CB09C64AAAFC6 CRC64; MMSSVRTGAS MALRARPTAQ IVPFRAAAVA SISSSSRKDA TGAVAPAGAQ HGIARRERRE VPLPSQEGTK GAVQYALTTL DSIVNWARQS SLWPMTFGLA CCAVEMMHLS TPRYDQDRLG IIFRASPRQS DVMIVAGTLT NKMAPALRQV YDQMPDPRWV ISMGSCANGG GYYHYSYSVV RGCDRIVPVD IYVPGCPPTS EALMYGIFQL QRKMRNTKIT RMWYRK //