ID A0A2U1XAP8_9PROT Unreviewed; 687 AA. AC A0A2U1XAP8; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 05-DEC-2018, entry version 5. DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525}; DE EC=1.6.5.11 {ECO:0000256|RuleBase:RU003525}; GN ORFNames=TSH20_06610 {ECO:0000313|EMBL:PWC70575.1}; OS Azospirillum sp. TSH20. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; 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 -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:132124, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.6.5.11; Evidence={ECO:0000256|RuleBase:RU003525}; CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000256|RuleBase:RU004523}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000245203; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. 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 4Fe-4S {ECO:0000256|RuleBase:RU003525}; KW Complete proteome {ECO:0000313|Proteomes:UP000245203}; KW Iron {ECO:0000256|SAAS:SAAS00509295}; KW Iron-sulfur {ECO:0000256|SAAS:SAAS00077451}; KW Metal-binding {ECO:0000256|RuleBase:RU003525, KW ECO:0000256|SAAS:SAAS00509306}; NAD {ECO:0000256|RuleBase:RU003525}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003525, KW ECO:0000256|SAAS:SAAS00509324, ECO:0000313|EMBL:PWC70575.1}. FT DOMAIN 2 78 2Fe-2S ferredoxin-type. FT {ECO:0000259|PROSITE:PS51085}. FT DOMAIN 78 117 4Fe-4S His(Cys)3-ligated-type. FT {ECO:0000259|PROSITE:PS51839}. FT DOMAIN 215 271 4Fe-4S Mo/W bis-MGD-type. FT {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 //