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Entry version 138 (18 Sep 2019)
Sequence version 2 (30 May 2000)
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Protein

Periplasmic nitrate reductase

Gene

napA

Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
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

Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.UniRule annotation2 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:

<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

Activated by potassium and sodium ions and inhibited by magnesium and calcium ions.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

  1. KM=12 µM for nitrate (in the presence of NaCl)1 Publication
  2. KM=20 µM for nitrate1 Publication
  3. KM=32 µM for nitrate (in the absence of NaCl)1 Publication

    pH dependencei

    Optimum pH is between 8 and 9.5.2 Publications

    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 bindingi45Iron-sulfur (4Fe-4S)UniRule annotationCombined sources2 Publications1
    Metal bindingi48Iron-sulfur (4Fe-4S)UniRule annotationCombined sources2 Publications1
    Metal bindingi52Iron-sulfur (4Fe-4S)UniRule annotationCombined sources2 Publications1
    Metal bindingi79Iron-sulfur (4Fe-4S)UniRule annotationCombined sources2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei81Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei143Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei168Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei172Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei340Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotationCombined sources2 Publications1
    Binding sitei344Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei450Mo-bis(molybdopterin guanine dinucleotide); via amide nitrogenUniRule annotationCombined sources2 Publications1
    Binding sitei721Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication1
    Binding sitei729Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1
    Binding sitei746Mo-bis(molybdopterin guanine dinucleotide)UniRule annotationCombined sources2 Publications1

    <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, Molybdenum

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    DDES525146:G1GUN-648-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:
    Periplasmic nitrate reductaseUniRule annotation (EC:1.9.6.1UniRule annotation2 Publications)
    <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:napAUniRule annotation
    Synonyms:nap
    Ordered Locus Names:Ddes_0616
    <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>OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
    <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 identifieri525146 [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 lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
    <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
    • UP000002598 <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

    <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

    Periplasm

    <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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 32Tat-type signalUniRule annotation1 PublicationAdd BLAST32
    <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_000001916933 – 755Periplasmic nitrate reductaseAdd BLAST723

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Predicted to be exported by the Tat system (By similarity). The position of the signal peptide cleavage has been experimentally proven (PubMed:9367852).UniRule annotation1 Publication

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P81186

    <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

    Monomer (PubMed:16887508).

    Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB (By similarity).

    UniRule annotation1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    525146.Ddes_0616

    <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

    Secondary structure

    1755
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    P81186

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P81186

    <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>Domaini38 – 934Fe-4S Mo/W bis-MGD-typeUniRule annotationAdd BLAST56

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni208 – 212Mo-bis(molybdopterin guanine dinucleotide) bindingCombined sources2 Publications5
    Regioni236 – 238Mo-bis(molybdopterin guanine dinucleotide) bindingCombined sources2 Publications3
    Regioni255 – 257Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotationCombined sources2 Publications3
    Regioni475 – 477Mo-bis(molybdopterin guanine dinucleotide) bindingCombined sources2 Publications3
    Regioni647 – 656Mo-bis(molybdopterin guanine dinucleotide) bindingUniRule annotationCombined sources2 Publications10
    Regioni648 – 653Substrate bindingCombined sources1 Publication6

    <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 prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.UniRule annotationCurated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4107QIW Bacteria
    COG0243 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000031441

    KEGG Orthology (KO)

    More...
    KOi
    K02567

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VCVKGAT

    Database of Orthologous Groups

    More...
    OrthoDBi
    323168at2

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02791 MopB_CT_Nitrate-R-NapA-like, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01630 Nitrate_reduct_NapA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR009010 Asp_de-COase-like_dom_sf
    IPR041957 CT_Nitrate-R-NapA-like
    IPR006657 MoPterin_dinucl-bd_dom
    IPR006656 Mopterin_OxRdtase
    IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
    IPR010051 Periplasm_NO3_reductase_lsu
    IPR006311 TAT_signal

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04879 Molybdop_Fe4S4, 1 hit
    PF00384 Molybdopterin, 1 hit
    PF01568 Molydop_binding, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00926 Molybdop_Fe4S4, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50692 SSF50692, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51669 4FE4S_MOW_BIS_MGD, 1 hit
    PS51318 TAT, 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.

    P81186-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSTSRRDFLK YFAMSAAVAA ASGAGFGSLA LAADNRPEKW VKGVCRYCGT
    60 70 80 90 100
    GCGVLVGVKD GKAVAIQGDP NNHNAGLLCL KGSLLIPVLN SKERVTQPLV
    110 120 130 140 150
    RRHKGGKLEP VSWDEALDLM ASRFRSSIDM YGPNSVAWYG SGQCLTEESY
    160 170 180 190 200
    VANKIFKGGF GTNNVDGNPR LCMASAVGGY VTSFGKDEPM GTYADIDQAT
    210 220 230 240 250
    CFFIIGSNTS EAHPVLFRRI ARRKQVEPGV KIIVADPRRT NTSRIADMHV
    260 270 280 290 300
    AFRPGTDLAF MHSMAWVIIN EELDNPRFWQ RYVNFMDAEG KPSDFEGYKA
    310 320 330 340 350
    FLENYRPEKV AEICRVPVEQ IYGAARAFAE SAATMSLWCM GINQRVQGVF
    360 370 380 390 400
    ANNLIHNLHL ITGQICRPGA TSFSLTGQPN ACGGVRDGGA LSHLLPAGRA
    410 420 430 440 450
    IPNAKHRAEM EKLWGLPEGR IAPEPGYHTV ALFEALGRGD VKCMIICETN
    460 470 480 490 500
    PAHTLPNLNK VHKAMSHPES FIVCIEAFPD AVTLEYADLV LPPAFWCERD
    510 520 530 540 550
    GVYGCGERRY SLTEKAVDPP GQCRPTVNTL VEFARRAGVD PQLVNFRNAE
    560 570 580 590 600
    DVWNEWRMVS KGTTYDFWGM TRERLRKESG LIWPCPSEDH PGTSLRYVRG
    610 620 630 640 650
    QDPCVPADHP DRFFFYGKPD GRAVIWMRPA KGAAEEPDAE YPLYLTSMRV
    660 670 680 690 700
    IDHWHTATMT GKVPELQKAN PIAFVEINEE DAARTGIKHG DSVIVETRRD
    710 720 730 740 750
    AMELPARVSD VCRPGLIAVP FFDPKKLVNK LFLDATDPVS REPEYKICAA

    RVRKA
    Length:755
    Mass (Da):83,497
    Last modified:May 30, 2000 - 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:iD54BDB9D1FE21DC2
    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
    Y18045 Genomic DNA Translation: CAA77019.1
    AJ920046 Genomic DNA Translation: CAI72603.1
    CP001358 Genomic DNA Translation: ACL48525.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    PC4422

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_012624252.1, NC_011883.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ACL48525; ACL48525; Ddes_0616

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    dds:Ddes_0616

    <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
    Y18045 Genomic DNA Translation: CAA77019.1
    AJ920046 Genomic DNA Translation: CAI72603.1
    CP001358 Genomic DNA Translation: ACL48525.1
    PIRiPC4422
    RefSeqiWP_012624252.1, NC_011883.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2JIMX-ray2.45A33-755[»]
    2JIOX-ray2.20A33-755[»]
    2JIPX-ray2.30A33-755[»]
    2JIQX-ray2.44A33-755[»]
    2JIRX-ray2.35A33-755[»]
    2NAPX-ray1.90A33-755[»]
    2V3VX-ray1.99A33-755[»]
    2V45X-ray2.40A33-755[»]
    SMRiP81186
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi525146.Ddes_0616

    Proteomic databases

    PRIDEiP81186

    Genome annotation databases

    EnsemblBacteriaiACL48525; ACL48525; Ddes_0616
    KEGGidds:Ddes_0616

    Phylogenomic databases

    eggNOGiENOG4107QIW Bacteria
    COG0243 LUCA
    HOGENOMiHOG000031441
    KOiK02567
    OMAiVCVKGAT
    OrthoDBi323168at2

    Enzyme and pathway databases

    BioCyciDDES525146:G1GUN-648-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP81186

    Family and domain databases

    CDDicd02791 MopB_CT_Nitrate-R-NapA-like, 1 hit
    HAMAPiMF_01630 Nitrate_reduct_NapA, 1 hit
    InterProiView protein in InterPro
    IPR009010 Asp_de-COase-like_dom_sf
    IPR041957 CT_Nitrate-R-NapA-like
    IPR006657 MoPterin_dinucl-bd_dom
    IPR006656 Mopterin_OxRdtase
    IPR006963 Mopterin_OxRdtase_4Fe-4S_dom
    IPR010051 Periplasm_NO3_reductase_lsu
    IPR006311 TAT_signal
    PfamiView protein in Pfam
    PF04879 Molybdop_Fe4S4, 1 hit
    PF00384 Molybdopterin, 1 hit
    PF01568 Molydop_binding, 1 hit
    SMARTiView protein in SMART
    SM00926 Molybdop_Fe4S4, 1 hit
    SUPFAMiSSF50692 SSF50692, 1 hit
    PROSITEiView protein in PROSITE
    PS51669 4FE4S_MOW_BIS_MGD, 1 hit
    PS51318 TAT, 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 nameiNAPA_DESDA
    <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: P81186
    Secondary accession number(s): B8IYC9, Q599G8
    <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: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: September 18, 2019
    This is version 138 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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