ID NDUS3_NEUCR Reviewed; 283 AA. AC P23710; Q7RV79; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 24-JAN-2024, entry version 141. DE RecName: Full=NADH-ubiquinone oxidoreductase 30.4 kDa subunit, mitochondrial; DE EC=7.1.1.2; DE AltName: Full=CI-31kD; DE AltName: Full=Complex I-30kD; DE Flags: Precursor; GN Name=nuo-31; ORFNames=NCU04074; OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / OS FGSC 987). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=367110; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2145832; DOI=10.1016/0006-291x(90)90807-y; RA Videira A., Tropschug M., Werner S.; RT "Primary structure and expression of a nuclear-coded subunit of complex I RT homologous to proteins specified by the chloroplast genome."; RL Biochem. Biophys. Res. Commun. 171:1168-1174(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 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., Werner-Washburne M., RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., RA Cogoni C., 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., Paulsen I., RA 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 chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC -!- SUBUNIT: Complex I is composed of about 40 different subunits. This is CC a component of the iron-sulfur protein fraction. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM002241; EAA28453.1; -; Genomic_DNA. DR PIR; A35935; A35935. DR RefSeq; XP_957689.1; XM_952596.3. DR AlphaFoldDB; P23710; -. DR SMR; P23710; -. DR STRING; 367110.P23710; -. DR TCDB; 3.D.1.6.2; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR PaxDb; 5141-EFNCRP00000003652; -. DR EnsemblFungi; EAA28453; EAA28453; NCU04074. DR GeneID; 3873779; -. DR KEGG; ncr:NCU04074; -. DR VEuPathDB; FungiDB:NCU04074; -. DR HOGENOM; CLU_042628_0_0_1; -. DR InParanoid; P23710; -. DR OMA; PCRKNRF; -. DR OrthoDB; 875497at2759; -. DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS. DR NCBIfam; TIGR01961; NuoC_fam; 1. DR PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1. DR PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1. DR Pfam; PF00329; Complex1_30kDa; 1. DR SUPFAM; SSF143243; Nqo5-like; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 2: Evidence at transcript level; KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane; KW NAD; Oxidoreductase; Reference proteome; Respiratory chain; KW Transit peptide; Translocase; Transport; Ubiquinone. FT TRANSIT 1..17 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 18..283 FT /note="NADH-ubiquinone oxidoreductase 30.4 kDa subunit, FT mitochondrial" FT /id="PRO_0000020000" FT REGION 258..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..283 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 40 FT /note="G -> R (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 283 AA; 32185 MW; 3A2DCD3489F32C6F CRC64; MASKLCRSRA LASALRSAKP SPAIRCLATT SRNLINMPEG PNPRQFPREP LPGALNAAVV NPADKYQSKA DNLHKYGSWL MGCLPKYIQQ FSVWKDELTI YISPAGVIPV FSFLKYNTAA EYTQVSDITA VDFPTKDQRF EVVYNLLSVR HNSRIRVKTY ADEVSPVPSI TPLYDGANWY EREVYDLFGV FFTGHPDLRR IMTDYGFDGH PLRKDFPMTG YTEIRYDEEK KRIVTEPLEM TQAFRNFEGG SSAWEQVGAG IDRKPESFKL PTPKPETKPE EKK //