ID A0A2U1XAP8_9PROT Unreviewed; 687 AA. AC A0A2U1XAP8; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 03-AUG-2022, entry version 18. DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525}; DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525}; GN ORFNames=TSH20_06610 {ECO:0000313|EMBL:PWC70575.1}; OS Azospirillum sp. TSH20. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Azospirillaceae; Azospirillum; unclassified Azospirillum. OX NCBI_TaxID=652754 {ECO:0000313|EMBL:PWC70575.1, ECO:0000313|Proteomes:UP000245203}; RN [1] {ECO:0000313|EMBL:PWC70575.1, ECO:0000313|Proteomes:UP000245203} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSH20 {ECO:0000313|EMBL:PWC70575.1, RC ECO:0000313|Proteomes:UP000245203}; RA Jang J., Ishii S.; RT "Comparative genome analysis of Azospirillum sp. strains."; RL Submitted (JUL-2015) 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. Couples the redox CC reaction to proton translocation (for every two electrons transferred, CC four hydrogen ions are translocated across the cytoplasmic membrane), CC and thus conserves the redox energy in a proton gradient. CC {ECO:0000256|RuleBase:RU003525}. 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|ARBA:ARBA00000100, CC ECO:0000256|RuleBase:RU003525}; CC -!- COFACTOR: CC Name=2Fe-2S cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000256|RuleBase:RU003525}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. CC {ECO:0000256|RuleBase:RU003525}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966, CC ECO:0000256|RuleBase:RU003525}; CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU003525}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01004}. 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:PWC70575.1}. 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; LGQU01000022; PWC70575.1; -; Genomic_DNA. DR EnsemblBacteria; PWC70575; PWC70575; TSH20_06610. DR Proteomes; UP000245203; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR CDD; cd00207; fer2; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR015405; NuoG_C. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR Pfam; PF09326; NADH_dhqG_C; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR01973; NuoG; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51839; 4FE4S_HC3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 3: Inferred from homology; KW 2Fe-2S {ECO:0000256|RuleBase:RU003525}; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003525}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003525}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003525}; KW Metal-binding {ECO:0000256|RuleBase:RU003525}; KW NAD {ECO:0000256|RuleBase:RU003525}; KW Oxidoreductase {ECO:0000313|EMBL:PWC70575.1}; KW Quinone {ECO:0000256|RuleBase:RU003525}; KW Translocase {ECO:0000256|RuleBase:RU003525}. FT DOMAIN 2..78 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51085" FT DOMAIN 78..117 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000259|PROSITE:PS51839" FT DOMAIN 215..271 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000259|PROSITE:PS51669" SQ SEQUENCE 687 AA; 74584 MW; 3FF624EC44B0F300 CRC64; MPKLTIDGIE IEVEPGTSIL QACEQLGIEI PRFCYHERLS VPANCRMCLV EMERAPKPVA SCAMPCGDGM VVRTNSETVL KARKGVMEFL LINHPLDCPI CDQGGECDLQ DQAMAYGFDR GRYGENKRAV KDKYMGPVIK TIMTRCIHCT RCIRFINEVA GVPDVGAVYR GEHMEITTFV EKAIGSELSG NLADVCPVGA LTHKPYAFTA RPWELRKTET IDVLDAVGSN IRVDARGAEV MRVLPRVNDD INEEWLNDKS RYSYDGLKRQ RLDRPYIRQN GKLVPASWAE AFTAISARLK GLPGNRVAAI SGDLVDVEAQ FALKELLSRL GSTNLDCRQD GARFDTSVRA GYLFNSGIAG IEKADVILLV GTNPRWEGTL VNARIRKRYL AGGVTIASIG EQRDLTYPYS VIGSGPDTLQ QLVDGSHPFA ETLRAAKNPM IIVGMGAFQR ADGLAVQAAA RLVGEAYGMF RDDWNGFNVL HTAAARVGGI EAGFLPGEGG RDTHGILDGA SKGEIDFVYL LGADEIDMAK LGNAFVVYQG HHGDAGAHRA DVILPGAAYT EKNAVYVNTE GRPQLARLAV FPPGEAREDW KIVRALSEVL GTTLPFDTHG QLRQRLMAAN PIFGAVGEMT PANWAPFGAQ GPVDAAPFVT PITNFYMTDP ISRASVTMAN CTEALVGPAQ ERTGTHG //