ID A0AAE3P464_9BACT Unreviewed; 180 AA. AC A0AAE3P464; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 24-JUL-2024, entry version 2. 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 ORFNames=OD816_000908 {ECO:0000313|EMBL:MDF2953663.1}; OS Candidatus Thermodesulfobacterium syntrophicum. OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria; OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; OC Thermodesulfobacterium. OX NCBI_TaxID=3060442 {ECO:0000313|EMBL:MDF2953663.1, ECO:0000313|Proteomes:UP001144110}; RN [1] {ECO:0000313|EMBL:MDF2953663.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MCA70 {ECO:0000313|EMBL:MDF2953663.1}; RA Zehnle H., Laso-Perez R., Lipp J., Teske A., Wegener G.; RT "Candidatus Alkanophaga archaea from heated hydrothermal vent sediment RT oxidize petroleum alkanes."; RL Submitted (NOV-2022) 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 14 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MDF2953663.1}. 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; JAPHEG010000003; MDF2953663.1; -; Genomic_DNA. DR Proteomes; UP001144110; Unassembled WGS sequence. 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; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1. DR PANTHER; PTHR10849:SF35; NADH-QUINONE OXIDOREDUCTASE SUBUNIT I; 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 Quinone {ECO:0000256|HAMAP-Rule:MF_01351}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01351}; KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01351}. FT DOMAIN 49..82 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 93..122 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 102 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 105 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 108 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 112 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 180 AA; 21085 MW; BA1DD0F6897C4D79 CRC64; MKILEKALLI EILKGLALTL RKMLFAKPVT IQYFDKVRPV PAPGFRGRHA LVRDEKTGDT LCIACMRCVR VCPSKCINVE YEVDKETKKR KVVKYEIDAL RCVYCGYCEE VCPVNAVVLT EWYEYVGLKR EDLFFDKEKL LKNWDEFIAT QKRPYLNPFW KPRGIPKKFL PAKKRQFTGV //