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UniProtKB - P9WIV9 (NUOG_MYCTU)

Entry version 37 (16 Oct 2019)
Sequence version 1 (16 Apr 2014)
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Protein

NADH-quinone oxidoreductase subunit G

Gene

nuoG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi49Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi60Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi63Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi77Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi111Iron-sulfur 2 (4Fe-4S); via tele nitrogenPROSITE-ProRule annotation1
Metal bindingi115Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi118Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi124Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi164Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi167Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi170Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi214Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi240Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi243Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi247Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi275Iron-sulfur 4 (4Fe-4S)Sequence analysis1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processVirulence
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MTBH37RV:G185E-7416-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:nuoG
Ordered Locus Names:Rv3151
ORF Names:MTCY03A2.07c
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...TubercuListi		Rv3151

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Complete GO annotation on QuickGO ...

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001185592 – 806NADH-quinone oxidoreductase subunit GAdd BLAST805

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1

Keywords - PTMi

Acetylation, Quinone

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P9WIV9

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P9WIV9

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The type I NADH dehydrogenase consists of 14 different subunits.

Curated

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		83332.Rv3151

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P9WIV9

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini15 – 932Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST79
Domaini95 – 1344Fe-4S His(Cys)3-ligated-typePROSITE-ProRule annotationAdd BLAST40
Domaini233 – 2894Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST57

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108IEH Bacteria
COG1034 LUCA

KEGG Orthology (KO)

More...KOi		K00336

Identification of Orthologs from Complete Genome Data

More...OMAi		PSICHGC

Database for complete collections of gene phylogenies

More...PhylomeDBi		P9WIV9

Family and domain databases

Conserved Domains Database

More...CDDi		cd00207 fer2, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
PF10588 NADH-G_4Fe-4S_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00926 Molybdop_Fe4S4, 1 hit
SM00929 NADH-G_4Fe-4S_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50692 SSF50692, 1 hit
SSF54292 SSF54292, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01973 NuoG, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P9WIV9-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:806
Mass (Da):85,424
Last modified:April 16, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i519A1EA833181064
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP45962.1

Protein sequence database of the Protein Information Resource

More...PIRi		H70647

NCBI Reference Sequences

More...RefSeqi		NP_217667.1, NC_000962.3
WP_003916519.1, NZ_NVQJ01000019.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CCP45962; CCP45962; Rv3151

Database of genes from NCBI RefSeq genomes

More...GeneIDi		887540

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mtu:Rv3151
mtv:RVBD_3151

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP45962.1
PIRiH70647
RefSeqiNP_217667.1, NC_000962.3
WP_003916519.1, NZ_NVQJ01000019.1

3D structure databases

SMRiP9WIV9
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3151

PTM databases

iPTMnetiP9WIV9

Proteomic databases

PaxDbiP9WIV9

Genome annotation databases

EnsemblBacteriaiCCP45962; CCP45962; Rv3151
GeneIDi887540
KEGGimtu:Rv3151
mtv:RVBD_3151

Organism-specific databases

TubercuListiRv3151

Phylogenomic databases

eggNOGiENOG4108IEH Bacteria
COG1034 LUCA
KOiK00336
OMAiPSICHGC
PhylomeDBiP9WIV9

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-7416-MONOMER

Family and domain databases

CDDicd00207 fer2, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00384 Molybdopterin, 1 hit
PF01568 Molydop_binding, 1 hit
PF10588 NADH-G_4Fe-4S_3, 1 hit
SMARTiView protein in SMART
SM00926 Molybdop_Fe4S4, 1 hit
SM00929 NADH-G_4Fe-4S_3, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
SSF54292 SSF54292, 1 hit
TIGRFAMsiTIGR01973 NuoG, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNUOG_MYCTU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P9WIV9
Secondary accession number(s): L0TBP2, P95175
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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