ID NQO3_PARDE Reviewed; 673 AA. AC P29915; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 25-NOV-2008, entry version 72. DE RecName: Full=NADH-quinone oxidoreductase chain 3; DE EC=1.6.99.5; DE AltName: Full=NADH dehydrogenase I, chain 3; DE AltName: Full=NDH-1, chain 3; GN Name=nqo3; OS Paracoccus denitrificans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Paracoccus. OX NCBI_TaxID=266; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16. RC STRAIN=ATCC 13543 / NRRL B-3784; RX MEDLINE=92296779; PubMed=1605643; DOI=10.1016/0003-9861(92)90542-5; RA Xu X., Matsuno-Yagi A., Yagi T.; RT "Structural features of the 66-kDa subunit of the energy-transducing RT NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans."; RL Arch. Biochem. Biophys. 296:40-48(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 658-673. RX MEDLINE=93136200; PubMed=8422400; DOI=10.1021/bi00054a030; RA Xu X., Matsuno-Yagi A., Yagi T.; RT "DNA sequencing of the seven remaining structural genes of the gene RT cluster encoding the energy-transducing NADH-quinone oxidoreductase of RT Paracoccus denitrificans."; RL Biochemistry 32:968-981(1993). RN [3] RP IDENTIFICATION OF A [2FE--2S] AND A [4FE--4S] CLUSTER. RX PubMed=7629145; DOI=10.1074/jbc.270.31.18264; RA Yano T., Yagi T., Sled' V.D., Ohnishi T.; RT "Expression and characterization of the 66-kilodalton (NQO3) iron- RT sulfur subunit of the proton-translocating NADH-quinone oxidoreductase RT of Paracoccus denitrificans."; RL J. Biol. Chem. 270:18264-18270(1995). RN [4] RP IDENTIFICATION OF A SECOND [4FE--4S] CLUSTER, AND MUTAGENESIS OF RP HIS-106. RX PubMed=12600982; DOI=10.1074/jbc.M212275200; RA Yano T., Sklar J., Nakamaru-Ogiso E., Takahashi Y., Yagi T., RA Ohnishi T.; RT "Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in RT the Nqo3 subunit of the proton-translocating NADH-ubiquinone RT oxidoreductase from Paracoccus denitrificans."; RL J. Biol. Chem. 278:15514-15522(2003). 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. CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol. CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit. The 2Fe-2S cluster CC is known as N1b. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit. The 4Fe-4S cluster CC 1 is known as N5 and 4Fe-4S cluster 2 as N4. CC -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1 CC to nqo14. The complex has a L-shaped structure, with the CC hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in CC the inner membrane and the hydrophilic peripheral arm (subunits CC nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The CC hydrophilic domain contains all the redox centers. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein. CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. 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; M84572; AAA25587.1; -; Genomic_DNA. DR PIR; S23948; A45456. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR001041; Ferredoxin. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR000283; NADH_DHase_75KDa_su_CS. DR InterPro; IPR010228; NADH_quinone_OxRdtase_G. DR InterPro; IPR015405; NuoG_C. DR Pfam; PF09326; DUF1982; 1. DR Pfam; PF00111; Fer2; 1. DR Pfam; PF00384; Molybdopterin; 1. DR TIGRFAMs; TIGR01973; NuoG; 1. DR PROSITE; PS00197; 2FE2S_FER_1; FALSE_NEG. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 1: Evidence at protein level; KW 2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane; KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; KW NAD; Oxidoreductase; Quinone; Ubiquinone. FT INIT_MET 1 1 Removed. FT CHAIN 2 673 NADH-quinone oxidoreductase chain 3. FT /FTId=PRO_0000118540. FT DOMAIN 5 90 2Fe-2S ferredoxin-type. FT METAL 37 37 Iron-sulfur 1 (2Fe-2S) (Potential). FT METAL 48 48 Iron-sulfur 1 (2Fe-2S) (Potential). FT METAL 51 51 Iron-sulfur 1 (2Fe-2S) (Potential). FT METAL 66 66 Iron-sulfur 1 (2Fe-2S) (Potential). FT METAL 106 106 Iron-sulfur 2 (4Fe-4S); via pros nitrogen FT (Probable). FT METAL 110 110 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 113 113 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 119 119 Iron-sulfur 2 (4Fe-4S) (Potential). FT METAL 158 158 Iron-sulfur 3 (4Fe-4S) (Potential). FT METAL 161 161 Iron-sulfur 3 (4Fe-4S) (Potential). FT METAL 164 164 Iron-sulfur 3 (4Fe-4S) (Potential). FT METAL 208 208 Iron-sulfur 3 (4Fe-4S) (Potential). FT MUTAGEN 106 106 H->A: Very little incorporation of iron- FT sulfur centers into protein in E.coli. FT MUTAGEN 106 106 H->C: Alters the EPR signal of the N5 FT cluster; all 3 iron-sulfur clusters are FT less stable in E.coli. SQ SEQUENCE 673 AA; 73159 MW; 5778B4A77940CF1D CRC64; MADLRKIKID DTIIEVDPNM TLIQACEMAG IEVPRFCYHE RLSIAGNCRM CLVEVVGGPP KPAASCAMQV KDLRPGPEGA PSEIRTNSPM VKKAREGVME FLLINHPLDC PICDQGGECD LQDQAMAYGV DFSRYREPKR ATEDLNLGPL VETHMTRCIS CTRCVRFTTE VAGITQMGQT GRGEDSEITS YLNQTLESNM QGNIIDLCPV GALVSKPYAF TARPWELTKT ESIDVMDALG SSIRIDTKGR EVMRILPRNH DGVNEEWISD KTRFVWDGLR RQRLDRPYIR ENGRLRPASW PEALEAAARA MKGKKIAGLI GDLVPAEAAF SLKQLVEGLG GKVECRVDGA RLPAGNRSAY VGTARIEDID DAEMIQLIGT NPRDEAPVLN ARIRKAWSKG AKVGLVGEPV DLTYDYAHVG TDRAALESLS SREISDETKA RPSIVIVGQG AIARRDGEAV LAHAMKLAEN SNSGLLILHT AAGRVGAMDV GAVTEGGLLA AIDGAEVVYN LGADEVDIDQ GPFVIYQGSH GDRGAHRDII LPGACYTEES GLFVNTEGRP QLAMRANFAP GEGKENWAIL RALSAELGAT QPWDSLAGLR RKLVEAVPHL AQIDQVPQNE WQPLGRFDLG QASFRYAIRD FYLTNPIARS SPLMGELSAM AAARKAPAPL AAE //