ID A0A6G6IZA0_9PSED Unreviewed; 182 AA. AC A0A6G6IZA0; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 25-MAY-2022, entry version 4. DE RecName: Full=NADH-quinone oxidoreductase subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01351}; DE AltName: Full=NADH dehydrogenase I subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; DE AltName: Full=NDH-1 subunit I {ECO:0000256|HAMAP-Rule:MF_01351}; GN Name=nuoI {ECO:0000256|HAMAP-Rule:MF_01351, GN ECO:0000313|EMBL:QIE88130.1}; GN ORFNames=G5B91_18370 {ECO:0000313|EMBL:QIE88130.1}; OS Pseudomonas nitroreducens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=46680 {ECO:0000313|EMBL:QIE88130.1, ECO:0000313|Proteomes:UP000501063}; RN [1] {ECO:0000313|EMBL:QIE88130.1, ECO:0000313|Proteomes:UP000501063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HBP1 {ECO:0000313|EMBL:QIE88130.1, RC ECO:0000313|Proteomes:UP000501063}; RA Sentchilo V., Carraro N., Bertelli C., van der Meer J.R.; RT "Integrative conjugative elements (ICEs) and plasmids drive adaptation of RT Pseudomonas nitroreducens strain HBP1 to wastewater environment."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01351}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01351}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01351}; CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H, CC J, K, L, M, N constitute the membrane sector of the complex. CC {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01351}. CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family. CC {ECO:0000256|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; CP049140; QIE88130.1; -; Genomic_DNA. DR RefSeq; WP_024765123.1; NZ_JUEH01000012.1. DR GeneID; 61670898; -. DR Proteomes; UP000501063; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. 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 PANTHER; PTHR10849; PTHR10849; 1. DR Pfam; PF12838; Fer4_7; 1. DR TIGRFAMs; TIGR01971; NuoI; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01351}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01351}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01351}; Membrane {ECO:0000256|HAMAP-Rule:MF_01351}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01351}; NAD {ECO:0000256|HAMAP-Rule:MF_01351}; KW Oxidoreductase {ECO:0000313|EMBL:QIE88130.1}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01351}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}. FT DOMAIN 52..82 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 92..121 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT METAL 62 FT /note="Iron-sulfur (4Fe-4S) 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 65 FT /note="Iron-sulfur (4Fe-4S) 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 68 FT /note="Iron-sulfur (4Fe-4S) 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 72 FT /note="Iron-sulfur (4Fe-4S) 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 101 FT /note="Iron-sulfur (4Fe-4S) 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 104 FT /note="Iron-sulfur (4Fe-4S) 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 107 FT /note="Iron-sulfur (4Fe-4S) 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT METAL 111 FT /note="Iron-sulfur (4Fe-4S) 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" SQ SEQUENCE 182 AA; 20645 MW; 7A300018F3285ECE CRC64; MIKYIFEVVH GTYTQLRSLV MIFGHAFRKR DTLQYPEEAV YLPPRYRGRI VLTRDPDGEE RCVACNLCAV ACPVGCISLQ KAETDDGRWY PEFFRINFSR CIFCGLCEEA CPTTAIQLTP DFEMGEFKRQ DLVYEKEDLL ISGPGKNPDY NFYRVAGMAI AGKPKGAAQN EAEPINVKSL LP //