ID NDUS2_RECAM Reviewed; 396 AA. AC O21270; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit; DE EC=1.6.5.3; DE EC=1.6.99.3; DE AltName: Full=NADH dehydrogenase subunit 7; GN Name=NAD7; OS Reclinomonas americana. OG Mitochondrion. OC Eukaryota; Jakobida; Histionidae; Reclinomonas. OX NCBI_TaxID=48483; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 50394; RX MEDLINE=97311393; PubMed=9168110; DOI=10.1038/387493a0; RA Lang B.F., Burger G., O'Kelly C.J., Cedergren R., Golding G.B., RA Lemieux C., Sankoff D., Turmel M., Gray M.W.; RT "An ancestral mitochondrial DNA resembling a eubacterial genome in RT miniature."; RL Nature 387:493-497(1997). 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 (By similarity). Component of the iron-sulfur (IP) CC fragment of the enzyme. Component of the iron-sulfur (IP) fragment CC of the enzyme. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- SUBCELLULAR LOCATION: Mitochondrion. 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; AF007261; AAD11897.1; -; Genomic_DNA. DR PIR; S78164; S78164. DR RefSeq; NP_044782.1; -. DR GeneID; 801113; -. DR BRENDA; 1.6.5.3; 307247. DR BRENDA; 1.6.99.3; 307247. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. 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; IPR010219; NADH_DH_1_dsu. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_su-49kDa_CS. DR Pfam; PF00346; Complex1_49kDa; 1. DR TIGRFAMs; TIGR01962; NuoD; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. PE 3: Inferred from homology; KW Electron transport; Mitochondrion; NAD; Oxidoreductase; KW Respiratory chain; Transport; Ubiquinone. FT CHAIN 1 396 NADH-ubiquinone oxidoreductase 49 kDa FT subunit. FT /FTId=PRO_0000118593. SQ SEQUENCE 396 AA; 44993 MW; 252B68E29305F096 CRC64; MQQKALTKKL KNFTMNFGPQ HPAAHGVLRL VLELNGEVVN RADPHIGLLH RGTEKLIEYK NYLQALPYFD RLDYVSMMAQ EHAYSLAVEK LLGCEVPKRA QYIRVLFCEI TRILNHLMAV TTHALDVGAM TPFLWGFEER EKLMEFYERV SGARMHAAYI RPGGVSQDMP MGLSEDIYKF AKQFGSRIDE IEDVLSSNRI WKQRLVDIGT VSAEEALDWG FSGVMLRGSG IAWDLRKTQP YDVYDELEFD IPVGTKGDCY DRYLIRVEEM RQSLKLIMQC LNKMPTGVIK VDDKKISPPS RVDMKDSMEA LIHHFKLYTE GYSVPIGETY TAVEAPKGEF GVYLVSDGSS KPYRCKIKAP GFSHLQGLNF MSKGHMIADV VTIIGTQDIV FGEVDR //