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UniProtKB - P28903 (NRDD_ECOLI)

Entry version 163 (02 Dec 2020)
Sequence version 2 (29 Aug 2003)
Previous versions | rss
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Protein

Anaerobic ribonucleoside-triphosphate reductase

Gene

nrdD

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

Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.5 Publications

Miscellaneous

The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl radical bridge between methionine and cysteine residues. Oxidation of formate by the thiosulfuranyl radical results in the release of CO2 and regeneration of the thiyl radical.1 Publication

Caution

Was originally thought to contain an iron sulfur cluster (PubMed:8381402). It was shown later that only NrdG contains an iron sulfur center (PubMed:8621608).1 Publication1 Publication

<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 <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

Activated under anaerobic conditions by NrdG, a tightly associated activase (PubMed:1460049, PubMed:7852304, PubMed:9305874). Activation involves the formation of a glycyl radical at Gly-681 (PubMed:7852304, PubMed:8636106, PubMed:9305874). Exposure of the activated reductase to oxygen leads to C-terminal truncation and inactivation of the protein, by cleavage at the N-terminal side of Gly-681 (PubMed:8421692, PubMed:7826394). The presence of zinc protects the protein from proteolysis and prevents the formation of disulfide bridges within it (PubMed:19381696).7 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=0.35 mM for CTP1 Publication

    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 bindingi644Zinc2 Publications1
    Metal bindingi647Zinc2 Publications1
    Metal bindingi662Zinc2 Publications1
    Metal bindingi665Zinc2 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

    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
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER
    MetaCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P28903

    <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:
    Anaerobic ribonucleoside-triphosphate reductaseCurated (EC:1.1.98.65 Publications)
    Alternative name(s):
    Class III ribonucleoside-triphosphate reductaseCurated
    <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:nrdD1 Publication
    Ordered Locus Names:b4238, JW4197
    <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

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi644C → A: Loss of activity. 1 Publication1
    Mutagenesisi647C → A: Almost loss of activity. 1 Publication1
    Mutagenesisi662C → A: Loss of activity. 1 Publication1
    Mutagenesisi665C → A: Loss of activity. 1 Publication1
    Mutagenesisi680C → S: Still retains some radical and some enzyme activity. 1 Publication1
    Mutagenesisi681G → A: Lacks both radical and enzyme activity. 1 Publication1
    Mutagenesisi682Y → F: Still retains some radical and some enzyme activity. 1 Publication1

    <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_00001666831 – 712Anaerobic ribonucleoside-triphosphate reductaseAdd BLAST712

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei681Glycine radicalPROSITE-ProRule annotation2 Publications1

    Keywords - PTMi

    Organic radical

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P28903

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

    More...    PaxDbi    		P28903

    PRoteomics IDEntifications database

    More...    PRIDEi    		P28903

    <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

    Induced 2-fold by hydroxyurea.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%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 (PubMed:1460049, PubMed:8621608).

    Forms a tetramer composed of two NrdD and two NrdG subunits (PubMed:8621608, PubMed:9305874).

    3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4259318, 27 interactors
    853044, 4 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...    ComplexPortali    		CPX-3821, nrdDG class III anaerobic ribonucleotide reductase activation complex
    CPX-3822, nrdD class III anaerobic ribonucleotide reductase complex

    Database of interacting proteins

    More...    DIPi    		DIP-10358N

    Protein interaction database and analysis system

    More...    IntActi    		P28903, 9 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b4238

    <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    		P28903

    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>Domaini3 – 92ATP-conePROSITE-ProRule annotationAdd BLAST90
    Domaini583 – 708Glycine radicalPROSITE-ProRule annotationAdd BLAST126

    <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 anaerobic ribonucleoside-triphosphate reductase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG1328, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_002707_2_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P28903

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P28903

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01675, RNR_III, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR005144, ATP-cone_dom
    IPR019777, Form_AcTrfase_GR_CS
    IPR001150, Gly_radical
    IPR012833, NrdD

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF03477, ATP-cone, 1 hit
    PF13597, NRDD, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR02487, NrdD, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51161, ATP_CONE, 1 hit
    PS00850, GLY_RADICAL_1, 1 hit
    PS51149, GLY_RADICAL_2, 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.

    P28903-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTPHVMKRDG CKVPFKSERI KEAILRAAKA AEVDDADYCA TVAAVVSEQM 
            60         70         80         90        100
    QGRNQVDINE IQTAVENQLM SGPYKQLARA YIEYRHDRDI EREKRGRLNQ 
           110        120        130        140        150
    EIRGLVEQTN ASLLNENANK DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV 
           160        170        180        190        200
    VQAHERGDIH YHDLDYSPFF PMFNCMLIDL KGMLTQGFKM GNAEIEPPKS 
           210        220        230        240        250
    ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTASY NKHRKTAEEW 
           260        270        280        290        300
    NIPDAEGYAN SRTIKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS 
           310        320        330        340        350
    WESRLIQESI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KKGDPNYDIK 
           360        370        380        390        400
    QLALECASKR MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH 
           410        420        430        440        450
    DGRNNLGVIS LNLPRIALEA KGDEATFWKL LDERLVLARK ALMTRIARLE 
           460        470        480        490        500
    GVKARVAPIL YMEGACGVRL NADDDVSEIF KNGRASISLG YIGIHETINA 
           510        520        530        540        550
    LFGGEHVYDN EQLRAKGIAI VERLRQAVDQ WKEETGYGFS LYSTPSENLC 
           560        570        580        590        600
    DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL 
           610        620        630        640        650
    ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT 
           660        670        680        690        700
    GEFECTSKGF TCPKCGNHDA SRVSVTRRVC GYLGSPDARP FNAGKQEEVK 
           710 
    RRVKHLGNGQ IG
    Length:712
    Mass (Da):80,023
    Last modified:August 29, 2003 - 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:i943589D653EB0C38
    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 conflicti257G → R in AAA24226 (PubMed:8421692).Curated1
    Sequence conflicti420A → P in AAA24226 (PubMed:8421692).Curated1

    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
    		L06097 Genomic DNA Translation: AAA24226.1
    U14003 Genomic DNA Translation: AAA97135.1
    U00096 Genomic DNA Translation: AAC77195.1
    AP009048 Genomic DNA Translation: BAE78237.1
    U06195 Genomic DNA Translation: AAC43383.1
    Z46865 Genomic DNA Translation: CAA86938.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A47331

    NCBI Reference Sequences

    More...    RefSeqi    		NP_418659.1, NC_000913.3
    WP_000187778.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC77195; AAC77195; b4238
    BAE78237; BAE78237; BAE78237

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		948755

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW4197
    eco:b4238

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2464

    <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
    		L06097 Genomic DNA Translation: AAA24226.1
    U14003 Genomic DNA Translation: AAA97135.1
    U00096 Genomic DNA Translation: AAC77195.1
    AP009048 Genomic DNA Translation: BAE78237.1
    U06195 Genomic DNA Translation: AAC43383.1
    Z46865 Genomic DNA Translation: CAA86938.1
    PIRiA47331
    RefSeqiNP_418659.1, NC_000913.3
    WP_000187778.1, NZ_LN832404.1

    3D structure databases

    SMRiP28903
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi4259318, 27 interactors
    853044, 4 interactors
    ComplexPortaliCPX-3821, nrdDG class III anaerobic ribonucleotide reductase activation complex
    CPX-3822, nrdD class III anaerobic ribonucleotide reductase complex
    DIPiDIP-10358N
    IntActiP28903, 9 interactors
    STRINGi511145.b4238

    Proteomic databases

    jPOSTiP28903
    PaxDbiP28903
    PRIDEiP28903

    Genome annotation databases

    EnsemblBacteriaiAAC77195; AAC77195; b4238
    BAE78237; BAE78237; BAE78237
    GeneIDi948755
    KEGGiecj:JW4197
    eco:b4238
    PATRICifig|1411691.4.peg.2464

    Organism-specific databases

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

    More...    EchoBASEi    		EB1388

    Phylogenomic databases

    eggNOGiCOG1328, Bacteria
    HOGENOMiCLU_002707_2_0_6
    InParanoidiP28903
    PhylomeDBiP28903

    Enzyme and pathway databases

    BioCyciEcoCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER
    MetaCyc:RIBONUCLEOSIDE-TRIP-REDUCT-MONOMER
    SABIO-RKiP28903

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P28903

    Family and domain databases

    CDDicd01675, RNR_III, 1 hit
    InterProiView protein in InterPro
    IPR005144, ATP-cone_dom
    IPR019777, Form_AcTrfase_GR_CS
    IPR001150, Gly_radical
    IPR012833, NrdD
    PfamiView protein in Pfam
    PF03477, ATP-cone, 1 hit
    PF13597, NRDD, 1 hit
    TIGRFAMsiTIGR02487, NrdD, 1 hit
    PROSITEiView protein in PROSITE
    PS51161, ATP_CONE, 1 hit
    PS00850, GLY_RADICAL_1, 1 hit
    PS51149, GLY_RADICAL_2, 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 nameiNRDD_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: P28903
    Secondary accession number(s): Q2M669
    <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: December 1, 1992
    Last sequence update: August 29, 2003
    Last modified: December 2, 2020
    This is version 163 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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