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UniProtKB - P00393 (NDH_ECOLI)

Entry version 175 (25 May 2022)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Type II NADH:quinone oxidoreductase

Gene

ndh

Organism
Escherichia coli (strain K12)
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

Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones (PubMed:6784762, PubMed:7009604, PubMed:7020757, PubMed:6362717, PubMed:3122832, PubMed:2679883, PubMed:10664466).

Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient (PubMed:3122832, PubMed:2679883).

7 Publications

It may also contribute to copper homeostasis and bacterial oxidative protection (PubMed:7487066, PubMed:10510271, PubMed:16759635, PubMed:21390523).

Shows cupric reductase activity, and catalyzes the reduction of Cu2+ to Cu+ with NADH as electron donor (PubMed:10510271).

Exhibits Cu2+ reductase activity in the presence of either FAD or quinone, but is unable to reduce Fe3+ (PubMed:10510271).

Contains thiolate-bound copper (PubMed:12176061).

5 Publications

Miscellaneous

Activity in vitro is generally measured with ubiquinone-1 as the electron acceptor. The physiological electron acceptor is probably ubiquinone-8.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

FAD5 PublicationsNote: Binds 1 FAD per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Requires Mg2+ for activity in vitro (PubMed:2679883). Inhibited by 3-n-dodecylmercapto-2-hydroxy-1,4-naphthoquinone (PubMed:7009604). The quinone-dependent Cu2+ reduction is partially inhibited by superoxide dismutase (PubMed:10510271).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=50 µM for NADH (for NADH:quinone oxidoreductase activity)1 Publication
  2. KM=6.1 µM for NADH (for cupric reductase activity, in the presence of FAD)1 Publication
  3. KM=6.9 µM for NADH (for cupric reductase activity, in the presence of duroquinone)1 Publication
  4. KM=34 µM for NADH (for NADH:quinone oxidoreductase activity)1 Publication
  5. KM=5.9 µM for ubiquinone-11 Publication
  6. KM=2.3 µM for ubiquinone-21 Publication
  7. KM=40 µM for ubiquinone-3 (for NADH:quinone oxidoreductase activity)1 Publication
  8. KM=32 µM for duroquinone (for cupric reductase activity)1 Publication
  9. KM=18.7 µM for decylbenzoquinone1 Publication
  10. KM=1.8 µM for idebenone1 Publication
  11. KM=20 µM for dichlorophenolindophenol1 Publication
  12. KM=12 µM for decylbenzoquinone (for NADH:quinone oxidoreductase activity)1 Publication
  13. KM=0.022 nM for Cu2+ (in the presence of FAD)1 Publication
  14. KM=0.032 nM for Cu2+ (in the presence of duroquinone)1 Publication
  15. KM=102 µM for FAD (for cupric reductase activity)1 Publication
  1. Vmax=106 mmol/min/mg enzyme with NADH as substrate1 Publication
  2. Vmax=106 mmol/min/mg enzyme with ubiquinone-1 as substrate1 Publication
  3. Vmax=190 mmol/min/mg enzyme with ubiquinone-2 as substrate1 Publication
  4. Vmax=191 mmol/min/mg enzyme with decylbenzoquinone as substrate1 Publication
  5. Vmax=107 mmol/min/mg enzyme with idebenone as substrate1 Publication
  6. Vmax=19.5 mmol/min/mg enzyme with dichlorophenolindophenol as substrate1 Publication
  7. Vmax=8.8 µmol/min/mg enzyme (for cupric reductase activity, in the presence of FAD)1 Publication
  8. Vmax=21.1 µmol/min/mg enzyme (for cupric reductase activity, in the presence of duroquinone)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei42FAD1 Publication1
Binding sitei84FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei124FAD; via amide nitrogen1 Publication1
Binding sitei275NAD; via amide nitrogen1 Publication1
Binding sitei315FAD1 Publication1
Binding sitei331FAD; via amide nitrogen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi12 – 16FAD1 Publication5
Nucleotide bindingi176 – 181NAD1 Publication6

<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 functionOxidoreductase
Biological processElectron transport, Transport
LigandFAD, Flavoprotein, NAD, Ubiquinone

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:NADH-DHII-MONOMER

Protein family/group databases

PeroxiBase, a peroxidase database

More...PeroxiBasei		5949, EcoNadDH_K12

<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%5Fand%5Ftaxonomy%5Fsection">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:
Type II NADH:quinone oxidoreductaseCurated (EC:1.6.5.96 Publications)
Alternative name(s):
Cupric reductase1 Publication (EC:1.16.1.-1 Publication)
NADH dehydrogenase-21 Publication
Short name:
NADH dh II1 Publication
Short name:
NDH-21 Publication
NADH-quinone reductase1 Publication
Short name:
NQR1 Publication
NADH:ubiquinone oxidoreductase1 Publication
Respiratory NADH dehydrogenase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ndh1 Publication
Ordered Locus Names:b1109, JW1095
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000000625 Componenti: Chromosome

<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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

Disruption mutant retains membrane-bound NADH dehydrogenase activity and shows no obvious growth defects. Mutations at two sites, one in ndh and one in nuo locus, remove the NADH oxidase activity from E.coli membranes (PubMed:8387992). The ndh deficient strain is more sensitive than the wild-type to Cu(II)/tert-butyl hydroperoxide (t-BOOH). Furthermore, several ndh deficient mutants grew less well than the corresponding parental strains in media containing either high or low copper concentrations (PubMed:16759635). The Cu(II)-reduction rate of the cell decreases by about 10% in the absence of NDH-2 and by about 85% in a strain lacking both NDH-2 and quinones (PubMed:21390523).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%5Fprocessing%5Fsection">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 methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000798902 – 434Type II NADH:quinone oxidoreductaseAdd BLAST433

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00393

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

More...PaxDbi		P00393

PRoteomics IDEntifications database

More...PRIDEi		P00393

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is subject to a complex network of regulatory controls at the transcriptional level (PubMed:8809757, PubMed:9168602). Under anaerobic conditions, is repressed by the global transcriptional regulator FNR, which binds at two sites in the ndh promoter region (PubMed:9168602). Transcription can be activated or repressed by the DNA-binding protein Fis (Nbp): at high concentrations, during early-exponential phase, Fis represses ndh transcription by binding to at least three sites in the ndb promoter, whereas at low concentrations Fis activates ndh expression by binding solely to the far upstream high-affinity site (PubMed:8809757). Also regulated by the integration host factor (IHF) and the histone-like protein HU (PubMed:9308170).3 Publications

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:7020757).

Forms a supercomplex with the NADH:quinone oxidoreductase NDH-1 in the aerobic respiratory chain (PubMed:21040753).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260082, 82 interactors

Database of interacting proteins

More...DIPi		DIP-10325N

Protein interaction database and analysis system

More...IntActi		P00393, 9 interactors

STRING: functional protein association networks

More...STRINGi		511145.b1109

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P00393

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

More...SMRi		P00393

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

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains four structural/functional domains: the FAD-binding domain, the NAD(H)-binding domain, the copper-binding domain and the domain of anchorage to the membrane at the C-terminus.1 Publication

<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 NADH dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1252, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021377_7_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00393

Identification of Orthologs from Complete Genome Data

More...OMAi		DHCIFLD

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00393

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR045024, NDH-2

The PANTHER Classification System

More...PANTHERi		PTHR43706, PTHR43706, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07992, Pyr_redox_2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P00393-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTPLKKIVI VGGGAGGLEM ATQLGHKLGR KKKAKITLVD RNHSHLWKPL 
        60         70         80         90        100
LHEVATGSLD EGVDALSYLA HARNHGFQFQ LGSVIDIDRE AKTITIAELR 
       110        120        130        140        150
DEKGELLVPE RKIAYDTLVM ALGSTSNDFN TPGVKENCIF LDNPHQARRF 
       160        170        180        190        200
HQEMLNLFLK YSANLGANGK VNIAIVGGGA TGVELSAELH NAVKQLHSYG 
       210        220        230        240        250
YKGLTNEALN VTLVEAGERI LPALPPRISA AAHNELTKLG VRVLTQTMVT 
       260        270        280        290        300
SADEGGLHTK DGEYIEADLM VWAAGIKAPD FLKDIGGLET NRINQLVVEP 
       310        320        330        340        350
TLQTTRDPDI YAIGDCASCP RPEGGFVPPR AQAAHQMATC AMNNILAQMN 
       360        370        380        390        400
GKPLKNYQYK DHGSLVSLSN FSTVGSLMGN LTRGSMMIEG RIARFVYISL 
       410        420        430 
YRMHQIALHG YFKTGLMMLV GSINRVIRPR LKLH
Length:434
Mass (Da):47,359
Last modified:January 23, 2007 - v2
<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:i3C3F4FA0E31E10E1
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
V00306 Genomic DNA Translation: CAA23586.1
U00096 Genomic DNA Translation: AAC74193.1
AP009048 Genomic DNA Translation: BAA35924.1

Protein sequence database of the Protein Information Resource

More...PIRi		A00461, DEECR

NCBI Reference Sequences

More...RefSeqi		NP_415627.1, NC_000913.3
WP_000211045.1, NZ_STEB01000016.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC74193; AAC74193; b1109
BAA35924; BAA35924; BAA35924

Database of genes from NCBI RefSeq genomes

More...GeneIDi		66670625
946792

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW1095
eco:b1109

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1158

<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
V00306 Genomic DNA Translation: CAA23586.1
U00096 Genomic DNA Translation: AAC74193.1
AP009048 Genomic DNA Translation: BAA35924.1
PIRiA00461, DEECR
RefSeqiNP_415627.1, NC_000913.3
WP_000211045.1, NZ_STEB01000016.1

3D structure databases

AlphaFoldDBiP00393
SMRiP00393
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4260082, 82 interactors
DIPiDIP-10325N
IntActiP00393, 9 interactors
STRINGi511145.b1109

Protein family/group databases

PeroxiBasei5949, EcoNadDH_K12

Proteomic databases

jPOSTiP00393
PaxDbiP00393
PRIDEiP00393

Genome annotation databases

EnsemblBacteriaiAAC74193; AAC74193; b1109
BAA35924; BAA35924; BAA35924
GeneIDi66670625
946792
KEGGiecj:JW1095
eco:b1109
PATRICifig|1411691.4.peg.1158

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0643

Phylogenomic databases

eggNOGiCOG1252, Bacteria
HOGENOMiCLU_021377_7_0_6
InParanoidiP00393
OMAiDHCIFLD
PhylomeDBiP00393

Enzyme and pathway databases

BioCyciEcoCyc:NADH-DHII-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P00393

Family and domain databases

InterProiView protein in InterPro
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR045024, NDH-2
PANTHERiPTHR43706, PTHR43706, 1 hit
PfamiView protein in Pfam
PF07992, Pyr_redox_2, 1 hit
SUPFAMiSSF51905, SSF51905, 1 hit

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 nameiNDH_ECOLI
<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: P00393
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 175 of the entry and version 2 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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