Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P27783 (NIA_BETPN)

Entry version 111 (07 Apr 2021)
Sequence version 1 (01 Aug 1992)
Previous versions | rss
Add a publicationFeedback
Protein

Nitrate reductase [NAD(P)H]

Gene

NIA1

Organism
Betula pendula (European white birch) (Betula verrucosa)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

<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

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%5Fsection">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 bindingi180MolybdenumBy similarity1
Metal bindingi563Iron (heme axial ligand)PROSITE-ProRule annotation1
Metal bindingi586Iron (heme axial ligand)PROSITE-ProRule annotation1
<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 sitei716FAD; via carbonyl oxygenBy similarity1
Binding sitei723FAD; via pi-pi stackingBy similarity1
Binding sitei781FADBy similarity1

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 bindingi694 – 697FADBy similarity4
Nucleotide bindingi711 – 715FADBy similarity5
Nucleotide bindingi728 – 730FADBy similarity3

<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 processNitrate assimilation
LigandFAD, Flavoprotein, Heme, Iron, Metal-binding, Molybdenum, NAD, NADP

<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:
Nitrate reductase [NAD(P)H] (EC:1.7.1.2)
Short name:
NR
<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:NIA1
<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>OrganismiBetula pendula (European white birch) (Betula verrucosa)
<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 identifieri3505 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › fabids › Fagales › Betulaceae › Betula

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001660751 – 898Nitrate reductase [NAD(P)H]Add BLAST898

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi419InterchainSequence analysis

Keywords - PTMi

Disulfide bond

<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.

<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

Homodimer.

<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		P27783

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%5Fand%5Fdomains%5Fsection">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>Domaini528 – 603Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini642 – 754FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113

<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 nitrate reductase family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.10.120.10, 1 hit
3.40.50.80, 1 hit
3.90.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001834, CBR-like
IPR008333, Cbr1-like_FAD-bd_dom
IPR001199, Cyt_B5-like_heme/steroid-bd
IPR036400, Cyt_B5-like_heme/steroid_sf
IPR018506, Cyt_B5_heme-BS
IPR017927, FAD-bd_FR_type
IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR039261, FNR_nucleotide-bd
IPR014756, Ig_E-set
IPR005066, MoCF_OxRdtse_dimer
IPR008335, Mopterin_OxRdtase_euk
IPR012137, Nitr_rd_NADH
IPR001433, OxRdtase_FAD/NAD-bd
IPR000572, OxRdtase_Mopterin-bd_dom
IPR036374, OxRdtase_Mopterin-bd_sf
IPR022407, OxRdtase_Mopterin_BS
IPR017938, Riboflavin_synthase-like_b-brl

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00173, Cyt-b5, 1 hit
PF00970, FAD_binding_6, 1 hit
PF03404, Mo-co_dimer, 1 hit
PF00175, NAD_binding_1, 1 hit
PF00174, Oxidored_molyb, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000233, Nitr_rd_NADH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00406, CYTB5RDTASE
PR00363, CYTOCHROMEB5
PR00407, EUMOPTERIN
PR00371, FPNCR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01117, Cyt-b5, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52343, SSF52343, 1 hit
SSF55856, SSF55856, 1 hit
SSF56524, SSF56524, 1 hit
SSF63380, SSF63380, 1 hit
SSF81296, SSF81296, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00191, CYTOCHROME_B5_1, 1 hit
PS50255, CYTOCHROME_B5_2, 1 hit
PS51384, FAD_FR, 1 hit
PS00559, MOLYBDOPTERIN_EUK, 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.

P27783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAASVENRRF THHEPAVNGL VRTFKPVPNS HRSDSPDLGR QIPSSPKKQV 
        60         70         80         90        100
ATGEDSSSED ENENDYKELI QKGNGELEPS ILDPRDEATA DNWVERNATM 
       110        120        130        140        150
VRLTGKHPFN SEAPLTRLMH HGFITPAPLH YVRNHGPVPK ARWEDWSVEV 
       160        170        180        190        200
CGLVKRPARF TMDRLVTEFR SREFPVTLVC AGNRRKEQNM VKKTIGFNWG 
       210        220        230        240        250
AAGVSTSVWR GVPLRDVLKR CGIFSRGRGA FNVCFEGAED LPGGGGSKYG 
       260        270        280        290        300
TSVKYEMAMD PARDIILGYM QNGERLSPDH GFPVRMIIPG FIGGRMVKWL 
       310        320        330        340        350
KRIIVTTKES DNYYHYNDNR VLPSHVDADV AKAEAWWYKP EHIINELNIN 
       360        370        380        390        400
SVITTPCHEE ILPINSWTTQ RPYTLRGYAY SGGGRKVTRV EITMNGGEKW 
       410        420        430        440        450
RVCALDHPEK PNKYGKYWCW CFWSLEVEVL DLLGAKEIAV RAWDEAHNTQ 
       460        470        480        490        500
PEKLIWNVMG MMNNCWFRVK TNVCKAHMGE IGIAFEHPTV PGNESGGWMA 
       510        520        530        540        550
REKNLETSSD ANQSLKKSVS SPFMNTSSKM FSMSEVKKHN SAESAWIIVH 
       560        570        580        590        600
GHIYDCTHFL KDHPGGADSI LINAGTDCTE EFDAIHSDKA KKMLEDYRIG 
       610        620        630        640        650
ELITTGYVSD SPNSTVHGAS NTSHLAPIKE IAPLRNVALI PGAKIPTKLV 
       660        670        680        690        700
YKKSLSHDVR LFRLALPSDD QVLGLPVGKH VFLCATIDDK LCMRAYTPTS 
       710        720        730        740        750
TIDEVGYLDL VVKIYFKNSN PRFPNGGLMS QHLDSLPIGS VLHVKGPLGH 
       760        770        780        790        800
VEYTGRGNFL VHGEPKFAKR LAMVAGGTGI TPIYQVIQAI LKDPEDETEM 
       810        820        830        840        850
FVVYANRTED DILLREELDD WAKKHEKLKV WYVVKESKRE GWEYSVGYIR 
       860        870        880        890 
ESILREHIPE GSDDVLALAC GAPSMIEEAV RLNLEKMNYD TKNSLIIF
Length:898
Mass (Da):101,002
Last modified:August 1, 1992 - 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:iC6B2B2B12FBCDC58
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
X54097 mRNA Translation: CAA38031.1

Protein sequence database of the Protein Information Resource

More...PIRi		S15959, RDBJNH

<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
X54097 mRNA Translation: CAA38031.1
PIRiS15959, RDBJNH

3D structure databases

SMRiP27783
ModBaseiSearch...

Family and domain databases

Gene3Di3.10.120.10, 1 hit
3.40.50.80, 1 hit
3.90.420.10, 1 hit
InterProiView protein in InterPro
IPR001834, CBR-like
IPR008333, Cbr1-like_FAD-bd_dom
IPR001199, Cyt_B5-like_heme/steroid-bd
IPR036400, Cyt_B5-like_heme/steroid_sf
IPR018506, Cyt_B5_heme-BS
IPR017927, FAD-bd_FR_type
IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase
IPR039261, FNR_nucleotide-bd
IPR014756, Ig_E-set
IPR005066, MoCF_OxRdtse_dimer
IPR008335, Mopterin_OxRdtase_euk
IPR012137, Nitr_rd_NADH
IPR001433, OxRdtase_FAD/NAD-bd
IPR000572, OxRdtase_Mopterin-bd_dom
IPR036374, OxRdtase_Mopterin-bd_sf
IPR022407, OxRdtase_Mopterin_BS
IPR017938, Riboflavin_synthase-like_b-brl
PfamiView protein in Pfam
PF00173, Cyt-b5, 1 hit
PF00970, FAD_binding_6, 1 hit
PF03404, Mo-co_dimer, 1 hit
PF00175, NAD_binding_1, 1 hit
PF00174, Oxidored_molyb, 1 hit
PIRSFiPIRSF000233, Nitr_rd_NADH, 1 hit
PRINTSiPR00406, CYTB5RDTASE
PR00363, CYTOCHROMEB5
PR00407, EUMOPTERIN
PR00371, FPNCR
SMARTiView protein in SMART
SM01117, Cyt-b5, 1 hit
SUPFAMiSSF52343, SSF52343, 1 hit
SSF55856, SSF55856, 1 hit
SSF56524, SSF56524, 1 hit
SSF63380, SSF63380, 1 hit
SSF81296, SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS00191, CYTOCHROME_B5_1, 1 hit
PS50255, CYTOCHROME_B5_2, 1 hit
PS51384, FAD_FR, 1 hit
PS00559, MOLYBDOPTERIN_EUK, 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 nameiNIA_BETPN
<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: P27783
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 7, 2021
This is version 111 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 programPlant 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again