ID NUOC_NEIMB Reviewed; 197 AA. AC Q9K1C1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=NADH-quinone oxidoreductase subunit C; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I subunit C; DE AltName: Full=NDH-1 subunit C; GN Name=nuoC; OrderedLocusNames=NMB0243; OS Neisseria meningitidis serogroup B. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58 / Serogroup B; RX MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., RA Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be ubiquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient (By similarity). CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits CC nuoB, C, D, E, F, and G constitute the peripheral sector of the CC complex (By similarity). CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein; Cytoplasmic side (By similarity). CC -!- SIMILARITY: Belongs to the complex I 30 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; AE002098; AAF40697.1; -; Genomic_DNA. DR PIR; A81222; A81222. DR RefSeq; NP_273299.1; -. DR GeneID; 902354; -. DR GenomeReviews; AE002098_GR; NMB0243. DR KEGG; nme:NMB0243; -. DR NMPDR; fig|122586.1.peg.233; -. DR TIGR; NMB0243; -. DR HOGENOM; Q9K1C1; -. DR OMA; Q9K1C1; VFAPDDD. DR BioCyc; NMEN122586:NMB_0243-MON; -. DR BRENDA; 1.6.99.5; 293828. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:HAMAP. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR HAMAP; MF_01357; -; 1. DR InterPro; IPR010218; NADH_DH_csu. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR Pfam; PF00329; Complex1_30kDa; 1. DR ProDom; PD001581; Complex1_30K; 1. DR TIGRFAMs; TIGR01961; NuoC_fam; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 3: Inferred from homology; KW Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD; KW Oxidoreductase; Quinone; Transport; Ubiquinone. FT CHAIN 1 197 NADH-quinone oxidoreductase subunit C. FT /FTId=PRO_0000118673. SQ SEQUENCE 197 AA; 23007 MW; 983591220B39E2DC CRC64; MASIQDLYET VSRVLGNQAG KVISALGEIT VECLPEHYIS VMTALRDHEE LHFELLVDLC GVDYSTYKNE AWQGKRFAVV SQLLSVKNNQ RIRVRVWVSD DDFPVVESVV DIYNSADWYE REAFDMYGIM FNNHPDLRRI LTDYGFVGHP FRKDFPISGY VEMRYDEEQK RVIYQPVTIE PREITPRIVR EENYGGQ //