ID NUOI_THET2 Reviewed; 182 AA. AC Q72GD6; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 120. DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; DE AltName: Full=NDH-1 subunit I {ECO:0000255|HAMAP-Rule:MF_01351}; GN Name=nuoI {ECO:0000255|HAMAP-Rule:MF_01351}; GN OrderedLocusNames=TT_C1912; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC ubiquinone. Couples the redox reaction to proton translocation (for CC every two electrons transferred, four hydrogen ions are translocated CC across the cytoplasmic membrane), and thus conserves the redox energy CC in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 CC H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01351}; CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000255|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01351}. CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC {ECO:0000255|HAMAP-Rule:MF_01351}. 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; AE017221; AAS82254.1; -; Genomic_DNA. DR RefSeq; WP_011174264.1; NC_005835.1. DR AlphaFoldDB; Q72GD6; -. DR SMR; Q72GD6; -. DR GeneID; 3167944; -. DR KEGG; tth:TT_C1912; -. DR eggNOG; COG1143; Bacteria. DR HOGENOM; CLU_067218_4_3_0; -. DR OrthoDB; 9803192at2; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) (non-electrogenic) activity; IEA:UniProtKB-UniRule. DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter. DR Gene3D; 3.30.70.3270; -; 1. DR HAMAP; MF_01351; NDH1_NuoI; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI. DR NCBIfam; TIGR01971; NuoI; 1. DR NCBIfam; NF004537; PRK05888.1-3; 1. DR PANTHER; PTHR10849:SF20; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR Pfam; PF12838; Fer4_7; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane; KW Metal-binding; NAD; Quinone; Reference proteome; Repeat; Translocase. FT CHAIN 1..182 FT /note="NADH-quinone oxidoreductase subunit I" FT /id="PRO_0000245755" FT DOMAIN 43..73 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT DOMAIN 89..118 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 53 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 56 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 59 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 63 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 98 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 101 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 104 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" FT BINDING 108 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351" SQ SEQUENCE 182 AA; 20080 MW; 054A9F7942C64C66 CRC64; MTLKALAQSL GITLKYLFSK PVTVPYPDAP VALKPRFHGR HVLTRHPNGL EKCIGCSLCA AACPAYAIYV EPAENDPENP VSAGERYAKV YEINMLRCIF CGLCEEACPT GAIVLGYDFE MADYEYSDLV YGKEDMLVDV VGTKPQRREA KRTGKPVKVG YVVPYVRPEL EGFKAPTEGG KR //