Skip Header

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

UniProtKB - P00861 (DCDA_ECOLI)

Entry version 162 (31 Jul 2019)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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_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

pyridoxal 5'-phosphate2 Publications

<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

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_section">'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
    Proteins known to be involved in this subpathway in this organism are:
    1. Diaminopimelate decarboxylase (lysA)
    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_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 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_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 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
    ECOL316407:JW2806-MONOMER
    MetaCyc:DIAMINOPIMDECARB-MONOMER

    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_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:
    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_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:lysAUniRule annotation
    Ordered Locus Names:b2838, JW2806
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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    		EG10549 lysA

    <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.<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_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

    WithEntry#Exp.IntActNotes
    cpxRP0AE884EBI-553837,EBI-550918

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261891, 8 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

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

    More...    SMRi    		P00861

    Database of comparative protein structure models

    More...    ModBasei    		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    		ENOG4105CU5 Bacteria
    COG0019 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000045070

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P00861

    KEGG Orthology (KO)

    More...    KOi    		K01586

    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_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.

    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[»]
    SMRiP00861
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi4261891, 8 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

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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
    EcoGeneiEG10549 lysA

    Phylogenomic databases

    eggNOGiENOG4105CU5 Bacteria
    COG0019 LUCA
    HOGENOMiHOG000045070
    InParanoidiP00861
    KOiK01586
    PhylomeDBiP00861

    Enzyme and pathway databases

    UniPathwayiUPA00034;UER00027
    BioCyciEcoCyc:DIAMINOPIMDECARB-MONOMER
    ECOL316407:JW2806-MONOMER
    MetaCyc:DIAMINOPIMDECARB-MONOMER

    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

    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 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_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: July 21, 1986
    Last modified: July 31, 2019
    This is version 162 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, Complete proteome, 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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

    Do not show this banner again