UniProtKB - P9WIV9 (NUOG_MYCTU)
Protein
NADH-quinone oxidoreductase subunit G
Gene
nuoG
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).By similarity
Plays a critical role in M.tuberculosis ability to inhibit apoptosis of infected macrophages; thus helps the bacterium in its struggle to resist the host immune response (PubMed:17658950). In fact, via a NuoG-dependent mechanism, M.tuberculosis can neutralize NOX2-derived reactive oxygen species (ROS) in order to inhibit TNF-alpha-mediated host cell apoptosis (PubMed:20421951). Also mediates inhibition of neutrophil apoptosis, leading to delayed activation of naive CD4 T cells (PubMed:22264515).3 Publications
Catalytic activityi
Cofactori
Protein has several cofactor binding sites:- [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
- [4Fe-4S] clusterBy similarityNote: Binds 3 [4Fe-4S] clusters per subunit.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 49 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 60 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 63 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 77 | Iron-sulfur 1 (2Fe-2S)By similarity | 1 | |
Metal bindingi | 111 | Iron-sulfur 2 (4Fe-4S); via tele nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 115 | Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation | 1 | |
Metal bindingi | 118 | Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation | 1 | |
Metal bindingi | 124 | Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation | 1 | |
Metal bindingi | 164 | Iron-sulfur 3 (4Fe-4S)By similarity | 1 | |
Metal bindingi | 167 | Iron-sulfur 3 (4Fe-4S)By similarity | 1 | |
Metal bindingi | 170 | Iron-sulfur 3 (4Fe-4S)By similarity | 1 | |
Metal bindingi | 214 | Iron-sulfur 3 (4Fe-4S)By similarity | 1 | |
Metal bindingi | 240 | Iron-sulfur 4 (4Fe-4S)Sequence analysis | 1 | |
Metal bindingi | 243 | Iron-sulfur 4 (4Fe-4S)Sequence analysis | 1 | |
Metal bindingi | 247 | Iron-sulfur 4 (4Fe-4S)Sequence analysis | 1 | |
Metal bindingi | 275 | Iron-sulfur 4 (4Fe-4S)Sequence analysis | 1 |
GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
- 4 iron, 4 sulfur cluster binding Source: GO_Central
- electron transfer activity Source: InterPro
- metal ion binding Source: UniProtKB-KW
- molybdopterin cofactor binding Source: InterPro
- NADH dehydrogenase (ubiquinone) activity Source: InterPro
- quinone binding Source: UniProtKB-KW
GO - Biological processi
- ATP synthesis coupled electron transport Source: InterPro
- negative regulation by symbiont of host apoptotic process Source: MTBBASE
- pathogenesis Source: MTBBASE
Keywordsi
Molecular function | Translocase |
Biological process | Virulence |
Ligand | 2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-7416-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: NADH-quinone oxidoreductase subunit G (EC:7.1.1.-)Alternative name(s): NADH dehydrogenase I subunit G NDH-1 subunit G |
Gene namesi | Name:nuoG Ordered Locus Names:Rv3151 ORF Names:MTCY03A2.07c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv3151 |
Subcellular locationi
GO - Cellular componenti
- cell wall Source: MTBBASE
- plasma membrane Source: MTBBASE
Pathology & Biotechi
Disruption phenotypei
Deletion of nuoG in M.tuberculosis reduces its ability to inhibit apoptosis of infected human or mouse macrophages and significantly decreases its virulence in mice (PubMed:17658950). The apoptogenic phenotype of the mutant strain is significantly reduced in human macrophages treated with caspase-3 and -8 inhibitors, TNF-alpha-neutralizing antibodies, and also after infection of murine TNF(-/-) macrophages. Moreover, incubation of macrophages with inhibitors of reactive oxygen species (ROS) reduces not only the apoptosis induced by the nuoG deletion mutant, but also its capacity to increase macrophage TNF-alpha secretion. The phagosomes infected with the mutant show increased ROS levels compared to M.tuberculosis phagosomes in primary murine and human alveolar macrophages. The increase in nuoG deletion mutant induced ROS and apoptosis is abolished in NOX-2 deficient (gp91(-/-)) macrophages (PubMed:20421951). Compared to wild-type, the nuoG deletion mutant spreads to a larger number of lung phagocytic cells. Consistent with the shorter lifespan of infected neutrophils, infection with the nuoG mutant results in fewer bacteria per infected neutrophil, accelerated bacterial acquisition by dendritic cells, earlier trafficking of these dendritic cells to lymph nodes, and faster CD4 T cell priming. Neutrophil depletion abrogates accelerated CD4 T cell priming by the nuoG mutant, suggesting that inhibiting neutrophil apoptosis delays adaptive immunity in tuberculosis (PubMed:22264515).3 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000118559 | 2 – 806 | NADH-quinone oxidoreductase subunit GAdd BLAST | 805 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylthreonineCombined sources | 1 |
Keywords - PTMi
Acetylation, QuinoneProteomic databases
PaxDbi | P9WIV9 |
PTM databases
iPTMneti | P9WIV9 |
Interactioni
Subunit structurei
The type I NADH dehydrogenase consists of 14 different subunits.
CuratedProtein-protein interaction databases
STRINGi | 83332.Rv3151 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 15 – 93 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST | 79 | |
Domaini | 95 – 134 | 4Fe-4S His(Cys)3-ligated-typePROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 233 – 289 | 4Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST | 57 |
Sequence similaritiesi
Belongs to the complex I 75 kDa subunit family.Curated
Phylogenomic databases
eggNOGi | ENOG4108IEH Bacteria COG1034 LUCA |
KOi | K00336 |
OMAi | PSICHGC |
PhylomeDBi | P9WIV9 |
Family and domain databases
CDDi | cd00207 fer2, 1 hit |
InterProi | View protein in InterPro IPR036010 2Fe-2S_ferredoxin-like_sf IPR001041 2Fe-2S_ferredoxin-type IPR009010 Asp_de-COase-like_dom_sf IPR006657 MoPterin_dinucl-bd_dom IPR006656 Mopterin_OxRdtase IPR006963 Mopterin_OxRdtase_4Fe-4S_dom IPR000283 NADH_UbQ_OxRdtase_75kDa_su_CS IPR010228 NADH_UbQ_OxRdtase_Gsu IPR019574 NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd |
Pfami | View protein in Pfam PF00384 Molybdopterin, 1 hit PF01568 Molydop_binding, 1 hit PF10588 NADH-G_4Fe-4S_3, 1 hit |
SMARTi | View protein in SMART SM00926 Molybdop_Fe4S4, 1 hit SM00929 NADH-G_4Fe-4S_3, 1 hit |
SUPFAMi | SSF50692 SSF50692, 1 hit SSF54292 SSF54292, 1 hit |
TIGRFAMsi | TIGR01973 NuoG, 1 hit |
PROSITEi | View protein in PROSITE PS51085 2FE2S_FER_2, 1 hit PS51839 4FE4S_HC3, 1 hit PS51669 4FE4S_MOW_BIS_MGD, 1 hit PS00641 COMPLEX1_75K_1, 1 hit PS00642 COMPLEX1_75K_2, 1 hit PS00643 COMPLEX1_75K_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WIV9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTQAADTDIR VGQPEMVTLT IDGVEISVPK GTLVIRAAEL MGIQIPRFCD
60 70 80 90 100
HPLLEPVGAC RQCLVEVEGQ RKPLASCTTV ATDDMVVRTQ LTSEIADKAQ
110 120 130 140 150
HGVMELLLIN HPLDCPMCDK GGECPLQNQA MSNGRTDSRF TEAKRTFAKP
160 170 180 190 200
INISAQVLLD RERCILCARC TRFSDQIAGD PFIDMQERGA LQQVGIYADE
210 220 230 240 250
PFESYFSGNT VQICPVGALT GTAYRFRARP FDLVSSPSVC EHCASGCAQR
260 270 280 290 300
TDHRRGKVLR RLAGDDPEVN EEWNCDKGRW AFTYATQPDV ITTPLIRDGG
310 320 330 340 350
DPKGALVPTS WSHAMAVAAQ GLAAARGRTG VLVGGRVTWE DAYAYAKFAR
360 370 380 390 400
ITLGTNDIDF RARPHSAEEA DFLAARIAGR HMAVSYADLE SAPVVLLVGF
410 420 430 440 450
EPEDESPIVF LRLRKAARRH RVPVYTIAPF ATGGLHKMSG RLIKTVPGGE
460 470 480 490 500
PAALDDLATG AVGDLLATPG AVIIVGERLA TVPGGLSAAA RLADTTGARL
510 520 530 540 550
AWVPRRAGER GALEAGALPT LLPGGRPLAD EVARAQVCAA WHIAELPAAA
560 570 580 590 600
GRDADGILAA AADETLAALL VGGIEPADFA DPDAVLAALD ATGFVVSLEL
610 620 630 640 650
RHSTVTERAD VVFPVAPTTQ KAGAFVNWEG RYRTFEPALR GSTLQAGQSD
660 670 680 690 700
HRVLDALADD MGVHLGVPTV EAAREELAAL GIWDGKHAAG PHIAATGPTQ
710 720 730 740 750
PEAGEAILTG WRMLLDEGRL QDGEPYLAGT ARTPVVRLSP DTAAEIGAAD
760 770 780 790 800
GEAVTVSTSR GSITLPCSVT DMPDRVVWLP LNSAGSTVHR QLRVTIGSIV
KIGAGS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45962.1 |
PIRi | H70647 |
RefSeqi | NP_217667.1, NC_000962.3 WP_003916519.1, NZ_NVQJ01000019.1 |
Genome annotation databases
EnsemblBacteriai | CCP45962; CCP45962; Rv3151 |
GeneIDi | 887540 |
KEGGi | mtu:Rv3151 mtv:RVBD_3151 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP45962.1 |
PIRi | H70647 |
RefSeqi | NP_217667.1, NC_000962.3 WP_003916519.1, NZ_NVQJ01000019.1 |
3D structure databases
SMRi | P9WIV9 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3151 |
PTM databases
iPTMneti | P9WIV9 |
Proteomic databases
PaxDbi | P9WIV9 |
Genome annotation databases
EnsemblBacteriai | CCP45962; CCP45962; Rv3151 |
GeneIDi | 887540 |
KEGGi | mtu:Rv3151 mtv:RVBD_3151 |
Organism-specific databases
TubercuListi | Rv3151 |
Phylogenomic databases
eggNOGi | ENOG4108IEH Bacteria COG1034 LUCA |
KOi | K00336 |
OMAi | PSICHGC |
PhylomeDBi | P9WIV9 |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-7416-MONOMER |
Family and domain databases
CDDi | cd00207 fer2, 1 hit |
InterProi | View protein in InterPro IPR036010 2Fe-2S_ferredoxin-like_sf IPR001041 2Fe-2S_ferredoxin-type IPR009010 Asp_de-COase-like_dom_sf IPR006657 MoPterin_dinucl-bd_dom IPR006656 Mopterin_OxRdtase IPR006963 Mopterin_OxRdtase_4Fe-4S_dom IPR000283 NADH_UbQ_OxRdtase_75kDa_su_CS IPR010228 NADH_UbQ_OxRdtase_Gsu IPR019574 NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd |
Pfami | View protein in Pfam PF00384 Molybdopterin, 1 hit PF01568 Molydop_binding, 1 hit PF10588 NADH-G_4Fe-4S_3, 1 hit |
SMARTi | View protein in SMART SM00926 Molybdop_Fe4S4, 1 hit SM00929 NADH-G_4Fe-4S_3, 1 hit |
SUPFAMi | SSF50692 SSF50692, 1 hit SSF54292 SSF54292, 1 hit |
TIGRFAMsi | TIGR01973 NuoG, 1 hit |
PROSITEi | View protein in PROSITE PS51085 2FE2S_FER_2, 1 hit PS51839 4FE4S_HC3, 1 hit PS51669 4FE4S_MOW_BIS_MGD, 1 hit PS00641 COMPLEX1_75K_1, 1 hit PS00642 COMPLEX1_75K_2, 1 hit PS00643 COMPLEX1_75K_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NUOG_MYCTU | |
Accessioni | P9WIV9Primary (citable) accession number: P9WIV9 Secondary accession number(s): L0TBP2, P95175 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 37 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names