ID NUOG_RICBR Reviewed; 681 AA. AC Q1RKD2; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=NADH-quinone oxidoreductase subunit G; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I subunit G; DE AltName: Full=NDH-1 subunit G; GN Name=nuoG; OrderedLocusNames=RBE_0101; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=336407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RML369-C; RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in RT gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:733-744(2006). 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 (By CC similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000305}. 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; CP000087; ABE04182.1; -; Genomic_DNA. DR RefSeq; WP_011476797.1; NC_007940.1. DR AlphaFoldDB; Q1RKD2; -. DR SMR; Q1RKD2; -. DR KEGG; rbe:RBE_0101; -. DR eggNOG; COG1034; Bacteria. DR HOGENOM; CLU_000422_11_6_5; -. DR OrthoDB; 9803192at2; -. DR Proteomes; UP000001951; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. 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:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR CDD; cd00207; fer2; 1. DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.200.210; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 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; NDUFS1-like_C. DR NCBIfam; TIGR01973; NuoG; 1. DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR Pfam; PF13510; Fer2_4; 1. 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; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone; KW Reference proteome; Translocase. FT CHAIN 1..681 FT /note="NADH-quinone oxidoreductase subunit G" FT /id="PRO_0000287842" FT DOMAIN 1..78 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 78..117 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT DOMAIN 215..271 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 34 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 45 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 48 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 62 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 94 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 98 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 101 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 107 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 146 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 681 AA; 76012 MW; 6DC4D413820168B1 CRC64; MIKLTIDGQE IEVSEGTTVY QACTKAGKEI PHFCYHERLK IAGNCRMCLV EMEKSPKPIA SCAMPVGNGM VIHTDTPMVK KAREGVMEFL LVNHPLDCPI CDQGGECDLQ DQAFRYGKGT NRFHENKRSI KDKYMGPLIK TAMTRCIQCT RCIRFANDIA GIEEMGAIHR GEHMEVTSYL EQTLDSEISG NMIDICPVGA LNSKPYAFKA RKWELRHTAS IGVHDAEGSN IRIDSRGDEV MRVLPRVNEE INEEWLSDKN RFSYDGLKYQ RLDQPYIRKN GKLVSASWDE ALKAIADKIK SIKPEKITAF AGTLASVEAM FMLKTFLQKI GCNNYNVNQF DYKLDTTQRG NYLFNTTIAG LEKADLCLLI GANPRQIAPV LNSRIGGRVR AGSLKVARIG EGHNQTYKIQ DLGSDLKILE ELALDEHKFA EELKAAKYPI IIVGDGVYGR NDGHAILSLI HKIVDKYNIM RDDWKGFNIL HNHASMVGGF DIGFDTSLGK LEDIELAYLL GADELPFDKL KSAFIVYQGH HGDIGATKAD IILPSAAYTE QSGIYVNLEG RPQIAEKAVS PVGKAKEDIA IIKELADCLK LDTLVSNLQE IRTKLAKEYP IFANIGKIID NKFAKFSSKD KLSKEPITAE TINYYMTDVI SKNSVTMARC VEAKQEMSSR GLSTGSRKKR E //