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Entry version 43 (11 Dec 2019)
Sequence version 1 (05 Sep 2012)
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Protein

Respiratory nitrate reductase subunit beta

Gene

narH

Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
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

The respiratory membrane-bound nitrate reductase enzyme complex plays a role in generation of metabolic energy by using nitrate as a terminal electron acceptor during anaerobic conditions. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers.1 Publication

<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:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Inhibited by cyanide, azide and antimycin A. Enzyme stability is not dependent on salt concentration.1 Publication

<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

Characterized with purified enzyme corresponding to a dimer of NarG and NarH.
  1. KM=0.82 mM for nitrate1 Publication
  2. KM=0.25 mM for methyl viologen1 Publication

    pH dependencei

    Optimum pH is 8.2. At 40 degrees Celsius (temperature of natural environment) the optimum pH is 7.9.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.1 Publication

    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 bindingi29Iron-sulfur 1 (4Fe-4S)By similarity1
    Metal bindingi32Iron-sulfur 1 (4Fe-4S)By similarity1
    Metal bindingi35Iron-sulfur 1 (4Fe-4S)By similarity1
    Metal bindingi39Iron-sulfur 2 (4Fe-4S)By similarity1
    Metal bindingi148Iron-sulfur 3 (4Fe-4S)By similarity1
    Metal bindingi151Iron-sulfur 3 (4Fe-4S)By similarity1
    Metal bindingi156Iron-sulfur 3 (4Fe-4S)By similarity1
    Metal bindingi160Iron-sulfur 4 (3Fe-4S)By similarity1
    Metal bindingi181Iron-sulfur 4 (3Fe-4S)By similarity1
    Metal bindingi187Iron-sulfur 4 (3Fe-4S)By similarity1
    Metal bindingi191Iron-sulfur 3 (4Fe-4S)By similarity1
    Metal bindingi208Iron-sulfur 2 (4Fe-4S)By similarity1
    Metal bindingi211Iron-sulfur 2 (4Fe-4S)By similarity1
    Metal bindingi229Iron-sulfur 2 (4Fe-4S)By similarity1
    Metal bindingi233Iron-sulfur 1 (4Fe-4S)By similarity1

    <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

    GO - Biological processi

    <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, Nitrate assimilation, Transport
    Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    HMED523841:G1HBL-3242-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:
    Respiratory nitrate reductase subunit beta (EC:1.7.5.11 Publication)
    Alternative name(s):
    Nitrate reductase beta chain
    <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:narH
    Ordered Locus Names:HFX_5103
    ORF Names:C439_00695
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pHM3000 Publication
    <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>OrganismiHaloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
    <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 identifieri523841 [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 lineageiArchaeaEuryarchaeotaStenosarchaea groupHalobacteriaHaloferacalesHaloferacaceaeHaloferax
    <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
    • UP000011603 <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: Unassembled WGS sequence
    • UP000006469 Componenti: Plasmid pHM300

    <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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    <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 ‘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_00004288871 – 352Respiratory nitrate reductase subunit betaAdd BLAST352

    <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

    By nitrate.1 Publication

    <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

    Probable multiprotein complex; a catalytic heterodimer of an alpha and beta chain is proposed to associate with additional subunits involved in membrane attachment and electron transfer.

    2 Publications

    <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
    I3R9M8

    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>Domaini20 – 484Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST29
    Domaini139 – 1704Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
    Domaini172 – 2014Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K00371

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NHCTHPS

    Database of Orthologous Groups

    More...
    OrthoDBi
    105930at2157

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd10555 EBDH_beta, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017896 4Fe4S_Fe-S-bd
    IPR017839 DMSO_Rdtase_II_Fe-S_su

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13247 Fer4_11, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03478 DMSO_red_II_bet, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51379 4FE4S_FER_2, 3 hits

    <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.

    I3R9M8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSTDSDAETV DLADGVDHQV AMVMDLNKCI GCQTCTVACK SLWTEGGGRD
    60 70 80 90 100
    YMYWNNVETK PGKGYPRNWE ESGGGWKSSE HKERKPGQIP DKEDYGDAWE
    110 120 130 140 150
    FNHEEIMYNG SDRPLRPDSD PEWGPNWDED QGTGEYPNSY YFYLPRICNH
    160 170 180 190 200
    CTHPSCVEAC PRKAIYKREE DGIVLIDQER CRGYRYCVEG CPYKKVYYNA
    210 220 230 240 250
    TQKTSEKCIF CYPRIEGEGP DGKTFAPACA EDCPPQLRLV GFLDDEQGPI
    260 270 280 290 300
    HKLVEEYEVA LPLHPEYQTQ PNVYYIPPFA PPQHSEDGES VDVDRIPRNY
    310 320 330 340 350
    LEELFGERVH DALDTIERER EKVNRGGGSE LLDMLTDTNP ARKFRLEVFD

    DD
    Length:352
    Mass (Da):40,390
    Last modified:September 5, 2012 - 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:iC0A34119DE660316
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti132G → C in CAF21907 (PubMed:15342113).Curated1
    Sequence conflicti158 – 160EAC → GSL in CAF21907 (PubMed:15342113).Curated3
    Sequence conflicti314 – 315DT → RH in CAF21907 (PubMed:15342113).Curated2
    Sequence conflicti323 – 324VN → SH in CAF21907 (PubMed:15342113).Curated2

    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
    AJ621881 Genomic DNA Translation: CAF21907.1
    CP001870 Genomic DNA Translation: AFK20938.1
    AOLO01000001 Genomic DNA Translation: EMA05272.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_004056335.1, NZ_CP039141.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AFK20938; AFK20938; HFX_5103
    EMA05272; EMA05272; C439_00695

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    40158239

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hme:HFX_5103

    <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
    AJ621881 Genomic DNA Translation: CAF21907.1
    CP001870 Genomic DNA Translation: AFK20938.1
    AOLO01000001 Genomic DNA Translation: EMA05272.1
    RefSeqiWP_004056335.1, NZ_CP039141.1

    3D structure databases

    SMRiI3R9M8
    ModBaseiSearch...

    Genome annotation databases

    EnsemblBacteriaiAFK20938; AFK20938; HFX_5103
    EMA05272; EMA05272; C439_00695
    GeneIDi40158239
    KEGGihme:HFX_5103

    Phylogenomic databases

    KOiK00371
    OMAiNHCTHPS
    OrthoDBi105930at2157

    Enzyme and pathway databases

    BioCyciHMED523841:G1HBL-3242-MONOMER

    Family and domain databases

    CDDicd10555 EBDH_beta, 1 hit
    InterProiView protein in InterPro
    IPR017896 4Fe4S_Fe-S-bd
    IPR017839 DMSO_Rdtase_II_Fe-S_su
    PfamiView protein in Pfam
    PF13247 Fer4_11, 1 hit
    TIGRFAMsiTIGR03478 DMSO_red_II_bet, 1 hit
    PROSITEiView protein in PROSITE
    PS51379 4FE4S_FER_2, 3 hits

    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 nameiNARH_HALMT
    <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: I3R9M8
    Secondary accession number(s): Q703H5
    <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: May 14, 2014
    Last sequence update: September 5, 2012
    Last modified: December 11, 2019
    This is version 43 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

    Plasmid
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