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Entry version 174 (02 Jun 2021)
Sequence version 2 (01 Nov 1997)
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Protein

1-deoxy-D-xylulose 5-phosphate reductoisomerase

Gene

dxr

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 NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).

<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

Mg2+, Mn2+, Co2+Note: Divalent cation. Prefers Mg2+, Mn2+ or Co2+.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by fosmidomycin.

<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

Measured in the presence of manganese ions.
  1. KM=250 µM for DXP1 Publication

pH dependencei

Optimum pH is 7.0-8.5.1 Publication

Temperature dependencei

Optimum temperature is 40-60 degrees Celsius.1 Publication

<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: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate. This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

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 sitei125Substrate1 Publication1
<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 bindingi150Divalent metal cation1
Metal bindingi152Divalent metal cation1
Binding sitei152Substrate1 Publication1
Binding sitei186Substrate1 Publication1
Binding sitei209Substrate1 Publication1
Metal bindingi231Divalent metal cation1
Binding sitei231Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi7 – 36NADP2 PublicationsAdd BLAST30

<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 processIsoprene biosynthesis
LigandCobalt, Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:DXPREDISOM-MONOMER
MetaCyc:DXPREDISOM-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.267, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P45568

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

More...
UniPathwayi
UPA00056;UER00092

<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:
1-deoxy-D-xylulose 5-phosphate reductoisomerase (EC:1.1.1.267)
Short name:
DXP reductoisomerase
Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
<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:dxr
Synonyms:ispC, yaeM
Ordered Locus Names:b0173, JW0168
<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

<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>Mutagenesisi14G → D: Loss of solubility and activity. 1 Publication1
Mutagenesisi153H → Q: Increase in KM for substrate. Reduces activity 35-fold. 1 Publication1
Mutagenesisi209H → Q: Increase in KM for substrate. Reduces activity 5000-fold. 1 Publication1
Mutagenesisi231E → K: No effect on KM for substrate. Reduces activity by over 99.9%. 1 Publication1
Mutagenesisi257H → Q: Strong increase in KM for substrate. Loss of activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4091

Drug and drug target database

More...
DrugBanki
DB02496, 1-Deoxy-D-xylulose 5-phosphate
DB03649, [{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate
DB02948, Fosmidomycin

<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_00001636511 – 3981-deoxy-D-xylulose 5-phosphate reductoisomeraseAdd BLAST398

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P45568

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

More...
PaxDbi
P45568

PRoteomics IDEntifications database

More...
PRIDEi
P45568

<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

Homodimer.

5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259751, 202 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1930, DXP reductoisomerase complex

Database of interacting proteins

More...
DIPi
DIP-9484N

Protein interaction database and analysis system

More...
IntActi
P45568, 6 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0173

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P45568

<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

1398
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
P45568

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
P45568

<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

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>Regioni222 – 228Binding to substrate phosphate group7

<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 DXR family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0743, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_035714_4_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P45568

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P45568

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00183, DXP_reductoisom, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003821, DXP_reductoisomerase
IPR013644, DXP_reductoisomerase_C
IPR013512, DXP_reductoisomerase_N
IPR026877, DXPR_C
IPR036169, DXPR_C_sf
IPR036291, NAD(P)-bd_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR30525, PTHR30525, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08436, DXP_redisom_C, 1 hit
PF02670, DXP_reductoisom, 1 hit
PF13288, DXPR_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006205, Dxp_reductismrs, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit
SSF69055, SSF69055, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00243, Dxr, 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.

P45568-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS
60 70 80 90 100
PRYAVMDDEA SAKLLKTMLQ QQGSRTEVLS GQQAACDMAA LEDVDQVMAA
110 120 130 140 150
IVGAAGLLPT LAAIRAGKTI LLANKESLVT CGRLFMDAVK QSKAQLLPVD
160 170 180 190 200
SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS ILLTGSGGPF RETPLRDLAT
210 220 230 240 250
MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN ASASQMEVLI
260 270 280 290 300
HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC
310 320 330 340 350
KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ
360 370 380 390
IRFTDIAALN LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS
Length:398
Mass (Da):43,388
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:i8B532683A4FF1207
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
AB013300 Genomic DNA Translation: BAA32426.1
U70214 Genomic DNA Translation: AAB08602.1
U00096 Genomic DNA Translation: AAC73284.1
AP009048 Genomic DNA Translation: BAA77848.2
D13334 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
E64741

NCBI Reference Sequences

More...
RefSeqi
NP_414715.1, NC_000913.3
WP_000811923.1, NZ_SSZK01000004.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73284; AAC73284; b0173
BAA77848; BAA77848; BAA77848

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61754847
945019

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0168
eco:b0173

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2107

<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
AB013300 Genomic DNA Translation: BAA32426.1
U70214 Genomic DNA Translation: AAB08602.1
U00096 Genomic DNA Translation: AAC73284.1
AP009048 Genomic DNA Translation: BAA77848.2
D13334 Genomic DNA No translation available.
PIRiE64741
RefSeqiNP_414715.1, NC_000913.3
WP_000811923.1, NZ_SSZK01000004.1

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
1JVSX-ray2.20A/B2-398[»]
1K5HX-ray2.50A/B/C1-398[»]
1ONNX-ray2.60A/B1-398[»]
1ONOX-ray2.50A/B1-398[»]
1ONPX-ray2.50A/B1-398[»]
1Q0HX-ray2.20A1-398[»]
1Q0LX-ray2.65A1-398[»]
1Q0QX-ray1.90A/B1-398[»]
1T1RX-ray2.30A/B2-398[»]
1T1SX-ray2.40A/B2-398[»]
2EGHX-ray2.20A/B2-398[»]
3ANLX-ray2.10A/B2-398[»]
3ANMX-ray2.00A/B2-398[»]
3ANNX-ray2.00A/B2-398[»]
3R0IX-ray2.10A/B1-398[»]
SMRiP45568
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259751, 202 interactors
ComplexPortaliCPX-1930, DXP reductoisomerase complex
DIPiDIP-9484N
IntActiP45568, 6 interactors
STRINGi511145.b0173

Chemistry databases

BindingDBiP45568
ChEMBLiCHEMBL4091
DrugBankiDB02496, 1-Deoxy-D-xylulose 5-phosphate
DB03649, [{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate
DB02948, Fosmidomycin

Proteomic databases

jPOSTiP45568
PaxDbiP45568
PRIDEiP45568

Genome annotation databases

EnsemblBacteriaiAAC73284; AAC73284; b0173
BAA77848; BAA77848; BAA77848
GeneIDi61754847
945019
KEGGiecj:JW0168
eco:b0173
PATRICifig|1411691.4.peg.2107

Organism-specific databases

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

More...
EchoBASEi
EB2575

Phylogenomic databases

eggNOGiCOG0743, Bacteria
HOGENOMiCLU_035714_4_0_6
InParanoidiP45568
PhylomeDBiP45568

Enzyme and pathway databases

UniPathwayiUPA00056;UER00092
BioCyciEcoCyc:DXPREDISOM-MONOMER
MetaCyc:DXPREDISOM-MONOMER
BRENDAi1.1.1.267, 2026
SABIO-RKiP45568

Miscellaneous databases

EvolutionaryTraceiP45568

Protein Ontology

More...
PROi
PR:P45568

Family and domain databases

HAMAPiMF_00183, DXP_reductoisom, 1 hit
InterProiView protein in InterPro
IPR003821, DXP_reductoisomerase
IPR013644, DXP_reductoisomerase_C
IPR013512, DXP_reductoisomerase_N
IPR026877, DXPR_C
IPR036169, DXPR_C_sf
IPR036291, NAD(P)-bd_dom_sf
PANTHERiPTHR30525, PTHR30525, 1 hit
PfamiView protein in Pfam
PF08436, DXP_redisom_C, 1 hit
PF02670, DXP_reductoisom, 1 hit
PF13288, DXPR_C, 1 hit
PIRSFiPIRSF006205, Dxp_reductismrs, 1 hit
SUPFAMiSSF51735, SSF51735, 1 hit
SSF69055, SSF69055, 1 hit
TIGRFAMsiTIGR00243, Dxr, 1 hit

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 nameiDXR_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: P45568
Secondary accession number(s): P77209, Q8KMY5
<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: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 2, 2021
This is version 174 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, 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
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