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Entry version 192 (31 Jul 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Ribonucleoside-diphosphate reductase 1 subunit alpha

Gene

nrdA

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

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.

Miscellaneous

E.coli produces two separate class I enzymes. This one is the functional enzyme during growth.
Two distinct regulatory sites have been defined: one controls substrate specificity and the other regulates the overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2.

<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 <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

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the alpha subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site. In vitro, its activity is increased by dithiothreitol (DTT) or thioredoxins (non-specific). Inhibited by hydroxyurea, leads to dNTP depletion, replication fork arrest and genomic instability (PubMed:20005847).1 Publication2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei9Allosteric activator1
Binding sitei55Allosteric activator1
Binding sitei91Allosteric activator1
Binding sitei209Substrate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei225Important for hydrogen atom transfer1
Sitei232Allosteric effector binding1
Binding sitei253Substrate; via amide nitrogenBy similarity1
Sitei262Allosteric effector binding1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei437Proton acceptor1
Active sitei439Cysteine radical intermediate1
Active sitei441Proton acceptor1
Sitei462Important for hydrogen atom transfer1
Sitei730Important for electron transfer1
Sitei731Important for electron transfer1
Sitei754Interacts with thioredoxin/glutaredoxin1
Sitei759Interacts with thioredoxin/glutaredoxin1

<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 functionAllosteric enzyme, Oxidoreductase
Biological processDNA replication
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:NRDA-MONOMER
ECOL316407:JW2228-MONOMER
MetaCyc:NRDA-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.17.4.1 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00452

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00326

<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:
Ribonucleoside-diphosphate reductase 1 subunit alpha (EC:1.17.4.1)
Alternative name(s):
Protein B1
Ribonucleoside-diphosphate reductase 1 R1 subunit
Ribonucleotide reductase 1
<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:nrdA
Synonyms:dnaF
Ordered Locus Names:b2234, JW2228
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10660 nrdA

<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

<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_and_biotech_section">'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>Mutagenesisi441E → A or Q: Loss of activity. 1 Publication1
Mutagenesisi441E → D: Decrease in activity. 1 Publication1
Mutagenesisi730Y → F: Loss of activity. 1 Publication1
Mutagenesisi731Y → F: Loss of 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000305961 – 761Ribonucleoside-diphosphate reductase 1 subunit alphaAdd BLAST761

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 bondi225 ↔ 462Redox-active2 Publications
<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 residuei283N6-acetyllysine1 Publication1

<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

Binding of the substrate occurs primarily when the active-site cysteines are reduced.

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P00452

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P00452

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

More...
PaxDbi
P00452

PRoteomics IDEntifications database

More...
PRIDEi
P00452

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00452

<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 5-fold by hydroxyurea (at protein level).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

Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between 'Tyr-122' of R2 and R1.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262130, 184 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1075 Ribonucleoside-diphosphate reductase complex

Database of interacting proteins

More...
DIPi
DIP-584N

Protein interaction database and analysis system

More...
IntActi
P00452, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2234

<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

1761
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

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SMRi
P00452

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00452

<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>Domaini5 – 95ATP-conePROSITE-ProRule annotationAdd BLAST91

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>Regioni15 – 21Allosteric activator binding7
Regioni224 – 225Substrate bindingBy similarity2
Regioni437 – 441Substrate bindingBy similarity5
Regioni621 – 625Substrate binding5

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105BZH Bacteria
COG0209 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000278076

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00452

KEGG Orthology (KO)

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KOi
K00525

Database for complete collections of gene phylogenies

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PhylomeDBi
P00452

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1

The PANTHER Classification System

More...
PANTHERi
PTHR11573 PTHR11573, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 2 hits
PF00317 Ribonuc_red_lgN, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01183 RIBORDTASEM1

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48168 SSF48168, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02506 NrdE_NrdA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Alpha (identifier: P00452-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY
60 70 80 90 100
DGIKTSDIHE TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP
110 120 130 140 150
ALYDHVVKMV EMGKYDNHLL EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ
160 170 180 190 200
LEGKYLVQNR VTGEIYESAQ FLYILVAACL FSNYPRETRL QYVKRFYDAV
210 220 230 240 250
STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT SSAIVKYVSQ
260 270 280 290 300
RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
310 320 330 340 350
AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG
360 370 380 390 400
EDITLFSPSD VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS
410 420 430 440 450
LMMQERASTG RIYIQNVDHC NTHSPFDPAI APVRQSNLCL EIALPTKPLN
460 470 480 490 500
DVNDENGEIA LCTLSAFNLG AINNLDELEE LAILAVRALD ALLDYQDYPI
510 520 530 540 550
PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT HKTFEAIQYY
560 570 580 590 600
LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE
610 620 630 640 650
ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG
660 670 680 690 700
ILRQVVPDYE HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD
710 720 730 740 750
PSRFPSGKVP MQQLLKDLLT AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ
760
DDGCESGACK I
Length:761
Mass (Da):85,775
Last modified:November 1, 1997 - 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:i7E034F154567C3FC
GO
Isoform Alpha' (identifier: P00452-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
     26-26: L → M

Show »
Length:736
Mass (Da):82,860
Checksum:i498ADEDC2154C084
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA24223 differs from that shown.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti1 – 2Missing in 15% of the chains. 2
Natural varianti1Missing in 30% of the chains. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0188711 – 25Missing in isoform Alpha'. CuratedAdd BLAST25
Alternative sequenceiVSP_01887226L → M in isoform Alpha'. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
K02672 Genomic DNA Translation: AAA24223.1 Sequence problems.
X06999 Genomic DNA Translation: CAA30056.2
U00096 Genomic DNA Translation: AAC75294.1
AP009048 Genomic DNA Translation: BAA16053.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H64993 RDEC1R

NCBI Reference Sequences

More...
RefSeqi
NP_416737.1, NC_000913.3
WP_001075164.1, NZ_STEB01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75294; AAC75294; b2234
BAA16053; BAA16053; BAA16053

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946612

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2228
eco:b2234

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1

Keywords - Coding sequence diversityi

Alternative initiation

<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
K02672 Genomic DNA Translation: AAA24223.1 Sequence problems.
X06999 Genomic DNA Translation: CAA30056.2
U00096 Genomic DNA Translation: AAC75294.1
AP009048 Genomic DNA Translation: BAA16053.1
PIRiH64993 RDEC1R
RefSeqiNP_416737.1, NC_000913.3
WP_001075164.1, NZ_STEB01000002.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QFNNMR-B737-761[»]
1R1RX-ray2.90A/B/C1-761[»]
1RLRX-ray2.50A1-761[»]
2R1RX-ray3.00A/B/C1-761[»]
2X0XX-ray2.30A/B/C1-761[»]
2XAKX-ray2.80A/B/C1-761[»]
2XAPX-ray2.10A/B/C1-761[»]
2XAVX-ray2.80A/B/C1-761[»]
2XAWX-ray3.10A/B/C1-761[»]
2XAXX-ray2.75A/B/C1-761[»]
2XAYX-ray2.65A/B/C1-761[»]
2XAZX-ray2.60A/B/C1-761[»]
2XO4X-ray2.50A/B/C1-761[»]
2XO5X-ray2.70A/B/C1-761[»]
3R1RX-ray3.00A/B/C1-761[»]
3UUSX-ray5.65A/B/C/D1-761[»]
4ERMX-ray3.95A/B/C/D1-761[»]
4ERPX-ray4.45A/B/C/D1-761[»]
4R1RX-ray3.20A/B/C1-761[»]
5CNSX-ray2.98A/B/C/D1-761[»]
5CNTX-ray3.25A/B/C/D1-761[»]
5CNUX-ray3.40A/B/C/D1-761[»]
5CNVX-ray3.20A/B/C/D1-761[»]
5R1RX-ray3.10A/B/C1-761[»]
6R1RX-ray3.10A/B/C1-761[»]
7R1RX-ray3.10A/B/C1-761[»]
SMRiP00452
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262130, 184 interactors
ComplexPortaliCPX-1075 Ribonucleoside-diphosphate reductase complex
DIPiDIP-584N
IntActiP00452, 10 interactors
STRINGi511145.b2234

PTM databases

iPTMnetiP00452

Proteomic databases

EPDiP00452
jPOSTiP00452
PaxDbiP00452
PRIDEiP00452

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75294; AAC75294; b2234
BAA16053; BAA16053; BAA16053
GeneIDi946612
KEGGiecj:JW2228
eco:b2234
PATRICifig|1411691.4.peg.1

Organism-specific databases

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

More...
EchoBASEi
EB0654
EcoGeneiEG10660 nrdA

Phylogenomic databases

eggNOGiENOG4105BZH Bacteria
COG0209 LUCA
HOGENOMiHOG000278076
InParanoidiP00452
KOiK00525
PhylomeDBiP00452

Enzyme and pathway databases

UniPathwayiUPA00326
BioCyciEcoCyc:NRDA-MONOMER
ECOL316407:JW2228-MONOMER
MetaCyc:NRDA-MONOMER
BRENDAi1.17.4.1 2026
SABIO-RKiP00452

Miscellaneous databases

EvolutionaryTraceiP00452

Protein Ontology

More...
PROi
PR:P00452

Family and domain databases

InterProiView protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1
PANTHERiPTHR11573 PTHR11573, 1 hit
PfamiView protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 2 hits
PF00317 Ribonuc_red_lgN, 1 hit
PRINTSiPR01183 RIBORDTASEM1
SUPFAMiSSF48168 SSF48168, 1 hit
TIGRFAMsiTIGR02506 NrdE_NrdA, 1 hit
PROSITEiView protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiRIR1_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: P00452
Secondary accession number(s): P78088, P78177
<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 21, 1986
Last sequence update: November 1, 1997
Last modified: July 31, 2019
This is version 192 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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