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UniProtKB - P00861 (DCDA_ECOLI)

Entry version 176 (25 May 2022)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
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Protein

Diaminopimelate decarboxylase

Gene

lysA

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

Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate.

3 Publications

<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

pyridoxal 5'-phosphate2 Publications

<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

Is activated by 2,3-dimercaptopropan-1-ol.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.7 mM for meso-2,6-diaminoheptanedioate (at pH 6.8 and 37 degrees Celsius)1 Publication
  2. KM=1.07 mM for meso-2,6-diaminoheptanedioate (at pH 8)1 Publication

pH dependencei

Optimum pH is 6.7-6.8.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes L-lysine from DL-2,6-diaminopimelate.1 Publication This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from DL-2,6-diaminopimelate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei191Substrate1 Publication1
Binding sitei227Pyridoxal phosphate; via amide nitrogen1 Publication1
Binding sitei271Substrate1 Publication1
Binding sitei307Substrate1 Publication1
Binding sitei311Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei342Proton donorUniRule annotation1
Binding sitei343Substrate1 Publication1
Binding sitei378Pyridoxal phosphate1 Publication1
Binding sitei378SubstrateUniRule annotation1

<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

  • lysine biosynthetic process via diaminopimelate Source: EcoCyc
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 functionDecarboxylase, Lyase
Biological processAmino-acid biosynthesis, Lysine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:DIAMINOPIMDECARB-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.1.1.20, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00861

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

More...UniPathwayi		UPA00034;UER00027

<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:
Diaminopimelate decarboxylaseUniRule annotation (EC:4.1.1.20UniRule annotation3 Publications)
Short name:
DAP decarboxylaseUniRule annotation
Short name:
DAPDCUniRule annotation
<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:lysAUniRule annotation
Ordered Locus Names:b2838, JW2806
<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 disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...DrugBanki		DB03814, 2-(N-morpholino)ethanesulfonic acid
DB03252, D-Lysine

<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_00001499231 – 420Diaminopimelate decarboxylaseAdd BLAST420

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 residuei54N6-(pyridoxal phosphate)lysine1 Publication1

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P00861

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

More...PaxDbi		P00861

PRoteomics IDEntifications database

More...PRIDEi		P00861

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P00861

<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

Up-regulated by LysR. Repressed in the presence of lysine.2 Publications

<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 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		4261891, 8 interactors
851640, 2 interactors

Database of interacting proteins

More...DIPi		DIP-10132N

Protein interaction database and analysis system

More...IntActi		P00861, 9 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2838

<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

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P00861

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

More...SMRi		P00861

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		P00861

<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>Regioni268 – 271Pyridoxal phosphate bindingUniRule annotation1 Publication4

<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 Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0019, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026444_0_2_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00861

Identification of Orthologs from Complete Genome Data

More...OMAi		HGNAKSP

Database for complete collections of gene phylogenies

More...PhylomeDBi		P00861

Family and domain databases

Conserved Domains Database

More...CDDi		cd06828, PLPDE_III_DapDC, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.37.10, 1 hit
3.20.20.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_02120, LysA, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009006, Ala_racemase/Decarboxylase_C
IPR002986, DAP_deCOOHase_LysA
IPR022643, De-COase2_C
IPR022657, De-COase2_CS
IPR022644, De-COase2_N
IPR022653, De-COase2_pyr-phos_BS
IPR000183, Orn/DAP/Arg_de-COase
IPR029066, PLP-binding_barrel

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02784, Orn_Arg_deC_N, 1 hit
PF00278, Orn_DAP_Arg_deC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01181, DAPDCRBXLASE
PR01179, ODADCRBXLASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50621, SSF50621, 1 hit
SSF51419, SSF51419, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01048, lysA, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00878, ODR_DC_2_1, 1 hit
PS00879, ODR_DC_2_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.

P00861-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPHSLFSTDT DLTAENLLRL PAEFGCPVWV YDAQIIRRQI AALKQFDVVR 
        60         70         80         90        100
FAQKACSNIH ILRLMREQGV KVDSVSLGEI ERALAAGYNP QTHPDDIVFT 
       110        120        130        140        150
ADVIDQATLE RVSELQIPVN AGSVDMLDQL GQVSPGHRVW LRVNPGFGHG 
       160        170        180        190        200
HSQKTNTGGE NSKHGIWYTD LPAALDVIQR HHLQLVGIHM HIGSGVDYAH 
       210        220        230        240        250
LEQVCGAMVR QVIEFGQDLQ AISAGGGLSV PYQQGEEAVD TEHYYGLWNA 
       260        270        280        290        300
AREQIARHLG HPVKLEIEPG RFLVAQSGVL ITQVRSVKQM GSRHFVLVDA 
       310        320        330        340        350
GFNDLMRPAM YGSYHHISAL AADGRSLEHA PTVETVVAGP LCESGDVFTQ 
       360        370        380        390        400
QEGGNVETRA LPEVKAGDYL VLHDTGAYGA SMSSNYNSRP LLPEVLFDNG 
       410        420
QARLIRRRQT IEELLALELL
Length:420
Mass (Da):46,177
Last modified:July 21, 1986 - 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:i0A26ABCFAF8462B5
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
J01614 Genomic DNA Translation: AAA83861.1
U29581 Genomic DNA Translation: AAB40485.1
U00096 Genomic DNA Translation: AAC75877.1
AP009048 Genomic DNA Translation: BAE76907.1

Protein sequence database of the Protein Information Resource

More...PIRi		A01078, DCECD

NCBI Reference Sequences

More...RefSeqi		NP_417315.1, NC_000913.3
WP_001120711.1, NZ_SSUV01000026.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75877; AAC75877; b2838
BAE76907; BAE76907; BAE76907

Database of genes from NCBI RefSeq genomes

More...GeneIDi		947313

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2806
eco:b2838

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3896

<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
J01614 Genomic DNA Translation: AAA83861.1
U29581 Genomic DNA Translation: AAB40485.1
U00096 Genomic DNA Translation: AAC75877.1
AP009048 Genomic DNA Translation: BAE76907.1
PIRiA01078, DCECD
RefSeqiNP_417315.1, NC_000913.3
WP_001120711.1, NZ_SSUV01000026.1

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
1KNWX-ray2.10A1-420[»]
1KO0X-ray2.20A1-420[»]
AlphaFoldDBiP00861
SMRiP00861
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261891, 8 interactors
851640, 2 interactors
DIPiDIP-10132N
IntActiP00861, 9 interactors
STRINGi511145.b2838

Chemistry databases

DrugBankiDB03814, 2-(N-morpholino)ethanesulfonic acid
DB03252, D-Lysine

2D gel databases

SWISS-2DPAGEiP00861

Proteomic databases

jPOSTiP00861
PaxDbiP00861
PRIDEiP00861

Genome annotation databases

EnsemblBacteriaiAAC75877; AAC75877; b2838
BAE76907; BAE76907; BAE76907
GeneIDi947313
KEGGiecj:JW2806
eco:b2838
PATRICifig|1411691.4.peg.3896

Organism-specific databases

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

More...EchoBASEi		EB0544

Phylogenomic databases

eggNOGiCOG0019, Bacteria
HOGENOMiCLU_026444_0_2_6
InParanoidiP00861
OMAiHGNAKSP
PhylomeDBiP00861

Enzyme and pathway databases

UniPathwayiUPA00034;UER00027
BioCyciEcoCyc:DIAMINOPIMDECARB-MONOMER
BRENDAi4.1.1.20, 2026
SABIO-RKiP00861

Miscellaneous databases

EvolutionaryTraceiP00861

Protein Ontology

More...PROi		PR:P00861

Family and domain databases

CDDicd06828, PLPDE_III_DapDC, 1 hit
Gene3Di2.40.37.10, 1 hit
3.20.20.10, 1 hit
HAMAPiMF_02120, LysA, 1 hit
InterProiView protein in InterPro
IPR009006, Ala_racemase/Decarboxylase_C
IPR002986, DAP_deCOOHase_LysA
IPR022643, De-COase2_C
IPR022657, De-COase2_CS
IPR022644, De-COase2_N
IPR022653, De-COase2_pyr-phos_BS
IPR000183, Orn/DAP/Arg_de-COase
IPR029066, PLP-binding_barrel
PfamiView protein in Pfam
PF02784, Orn_Arg_deC_N, 1 hit
PF00278, Orn_DAP_Arg_deC, 1 hit
PRINTSiPR01181, DAPDCRBXLASE
PR01179, ODADCRBXLASE
SUPFAMiSSF50621, SSF50621, 1 hit
SSF51419, SSF51419, 1 hit
TIGRFAMsiTIGR01048, lysA, 1 hit
PROSITEiView protein in PROSITE
PS00878, ODR_DC_2_1, 1 hit
PS00879, ODR_DC_2_2, 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 nameiDCDA_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: P00861
Secondary accession number(s): Q2M9Z9
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 25, 2022
This is version 176 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 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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