ID A0A6G6IZA0_PSENT Unreviewed; 182 AA. AC A0A6G6IZA0; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 13-SEP-2023, entry version 10. 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; Pseudomonadota; 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 AlphaFoldDB; A0A6G6IZA0; -. DR GeneID; 79914204; -. DR KEGG; pnt:G5B91_18370; -. 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 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 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; 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 BINDING 62 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT BINDING 65 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT BINDING 68 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT BINDING 72 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01351" FT BINDING 107 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01351" FT BINDING 111 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="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 //