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UniProtKB - P05020 (PYRC_ECOLI)

Entry version 176 (13 Nov 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Dihydroorotase

Gene

pyrC

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 reversible cyclization of carbamoyl aspartate to dihydroorotate.UniRule annotation2 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

Zn2+UniRule annotation5 PublicationsNote: Binds 2 Zn2+ ions per subunit (PubMed:6142052, PubMed:11401542, PubMed:15826651). In vitro, can also use Co2+ or Cd2+ (PubMed:1671037, PubMed:15610022).5 Publications

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

kcat is 127 sec(-1) with dihydroorotate as substrate and 195 sec(-1) with N-carbamoyl-DL-aspartate as substrate (PubMed:6142052). kcat is 100 sec(-1) with dihydroorotate as substrate and 160 sec(-1) with carbamoyl aspartate as substrate in the presence of Zn2+. kcat is 15 sec(-1) with dihydroorotate as substrate and 25 sec(-1) with carbamoyl aspartate as substrate in the presence of Co2+. kcat is 1.9 sec(-1) with dihydroorotate as substrate and 8.2 sec(-1) with carbamoyl aspartate as substrate in the presence of Cd2+ (PubMed:15610022).2 Publications
  1. KM=0.0756 mM for dihydroorotate1 Publication
  2. KM=0.080 mM for dihydroorotate (in the presence of Zn2+)1 Publication
  3. KM=0.70 mM for dihydroorotate (in the presence of Co2+)1 Publication
  4. KM=0.23 mM for dihydroorotate (in the presence of Cd2+)1 Publication
  5. KM=1.07 mM for N-carbamoyl-DL-aspartate1 Publication
  6. KM=1.70 mM for carbamoyl aspartate (in the presence of Zn2+)1 Publication
  7. KM=15 mM for carbamoyl aspartate (in the presence of Co2+)1 Publication
  8. KM=4.0 mM for carbamoyl aspartate (in the presence of Cd2+)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: UMP biosynthesis via de novo pathway

    This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotationCurated
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA)
    2. Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase catalytic subunit (pyrB), Aspartate carbamoyltransferase (pyrB)
    3. Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC)
    This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi17Zinc 1; via tele nitrogenUniRule annotationCombined sources2 Publications1
    Metal bindingi19Zinc 1; via tele nitrogenUniRule annotationCombined sources2 Publications1
    <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 sitei45SubstrateUniRule annotationCombined sources2 Publications1
    Metal bindingi103Zinc 1; via carbamate groupUniRule annotationCombined sources2 Publications1
    Metal bindingi103Zinc 2; via carbamate groupUniRule annotationCombined sources2 Publications1
    Metal bindingi140Zinc 2; via pros nitrogenUniRule annotationCombined sources2 Publications1
    Binding sitei140SubstrateUniRule annotationCombined sources1 Publication1
    Metal bindingi178Zinc 2; via tele nitrogenUniRule annotationCombined sources2 Publications1
    Binding sitei223Substrate; via amide nitrogen and carbonyl oxygenUniRule annotationCombined sources2 Publications1
    <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 sitei251UniRule annotation1 Publication1
    Metal bindingi251Zinc 1UniRule annotationCombined sources2 Publications1
    Binding sitei255SubstrateUniRule annotationCombined sources2 Publications1
    Binding sitei267Substrate; via carbonyl oxygenUniRule annotationCombined sources2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • dihydroorotase activity Source: EcoCyc
    • zinc ion binding Source: EcoCyc
    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    Biological processPyrimidine biosynthesis
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:DIHYDROOROT-MONOMER
    ECOL316407:JW1049-MONOMER
    MetaCyc:DIHYDROOROT-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.5.2.3 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P05020

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

    More...    UniPathwayi    		UPA00070;UER00117

    <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:
    DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation2 Publications)
    Short name:
    DHOaseUniRule 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:pyrC1 PublicationUniRule annotation
    Ordered Locus Names:b1062, JW1049
    <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

    <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

    Complete GO annotation on QuickGO ...

    <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>Mutagenesisi21R → K: 9-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication1
    Mutagenesisi21R → M or Q: Lack of activity. 1 Publication1
    Mutagenesisi45N → A: Lack of activity. 1 Publication1
    Mutagenesisi251D → A, H or N: Lack of activity. 1 Publication1
    Mutagenesisi251D → E: 24-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication1
    Mutagenesisi251D → S: 3500-fold decrease in catalytic efficiency with carbamoyl aspartate as substrate. 1 Publication1
    Mutagenesisi255H → N: Lack of activity. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB02129 Dihydroorotic Acid
    DB03801 Lysine Nz-Carboxylic Acid
    DB04252 N-Carbamoyl-L-Aspartate
    DB02262 Orotic Acid

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <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_00001472052 – 348DihydroorotaseAdd BLAST347

    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 residuei103N6-carboxylysineUniRule annotationCombined sources2 Publications1

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P05020

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

    More...    PaxDbi    		P05020

    PRoteomics IDEntifications database

    More...    PRIDEi    		P05020

    <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 by pyrimidine limitation.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

    Homodimer.

    UniRule annotation3 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4261761, 32 interactors
    850154, 4 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-10624N

    Protein interaction database and analysis system

    More...    IntActi    		P05020, 6 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1062

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P05020

    <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

    1348
    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    		P05020

    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    		P05020

    <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>Regioni19 – 21Substrate bindingUniRule annotationCombined sources2 Publications3

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    There is an asymmetry between active sites in the dimer, with dihydroorotate bound to the active site of subunit A and N-carbamoyl-L-aspartate bound to the active site of subunit B.1 Publication

    <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 metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105EKE Bacteria
    COG0418 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000256259

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P05020

    KEGG Orthology (KO)

    More...    KOi    		K01465

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P05020

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01294 DHOase, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00219 PyrC_classII, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR006680 Amidohydro-rel
    IPR004721 DHOdimr
    IPR002195 Dihydroorotase_CS
    IPR032466 Metal_Hydrolase

    The PANTHER Classification System

    More...    PANTHERi    		PTHR43137 PTHR43137, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01979 Amidohydro_1, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001237 DHOdimr, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51556 SSF51556, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00856 pyrC_dimer, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00482 DIHYDROOROTASE_1, 1 hit
    PS00483 DIHYDROOROTASE_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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P05020-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV 
            60         70         80         90        100
    TTVEAAVAYR QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT 
           110        120        130        140        150
    AAKLYPANAT TNSSHGVTSI DAIMPVLERM EKIGMPLLVH GEVTHADIDI 
           160        170        180        190        200
    FDREARFIES VMEPLRQRLT ALKVVFEHIT TKDAADYVRD GNERLAATIT 
           210        220        230        240        250
    PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA SGFNRVFLGT 
           260        270        280        290        300
    DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 
           310        320        330        340 
    PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
    Length:348
    Mass (Da):38,827
    Last modified:January 23, 2007 - 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:i179B35324204A111
    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
    		X04469 Genomic DNA Translation: CAA28157.1
    M16752 Genomic DNA Translation: AAA24482.1
    U00096 Genomic DNA Translation: AAC74146.1
    AP009048 Genomic DNA Translation: BAA35870.1
    D31709 Genomic DNA Translation: BAA06514.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A25008 DEECOO

    NCBI Reference Sequences

    More...    RefSeqi    		NP_415580.1, NC_000913.3
    WP_000126534.1, NZ_SSZK01000053.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74146; AAC74146; b1062
    BAA35870; BAA35870; BAA35870

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		945787

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1049
    eco:b1062

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.1206

    <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
    		X04469 Genomic DNA Translation: CAA28157.1
    M16752 Genomic DNA Translation: AAA24482.1
    U00096 Genomic DNA Translation: AAC74146.1
    AP009048 Genomic DNA Translation: BAA35870.1
    D31709 Genomic DNA Translation: BAA06514.1
    PIRiA25008 DEECOO
    RefSeqiNP_415580.1, NC_000913.3
    WP_000126534.1, NZ_SSZK01000053.1

    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
    1J79X-ray1.70A/B2-348[»]
    1XGEX-ray1.90A/B2-348[»]
    2E25X-ray2.70A2-348[»]
    2EG6X-ray1.70A/B2-348[»]
    2EG7X-ray2.00A/B2-348[»]
    2EG8X-ray2.20A/B2-348[»]
    2Z24X-ray1.90A/B2-348[»]
    2Z25X-ray1.87A/B2-348[»]
    2Z26X-ray1.29A/B2-348[»]
    2Z27X-ray1.87A/B2-348[»]
    2Z28X-ray1.87A/B2-348[»]
    2Z29X-ray1.90A/B2-348[»]
    2Z2AX-ray1.87A/B2-348[»]
    2Z2BX-ray1.85A2-348[»]
    6HG1X-ray2.12A107-119[»]
    SMRiP05020
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4261761, 32 interactors
    850154, 4 interactors
    DIPiDIP-10624N
    IntActiP05020, 6 interactors
    STRINGi511145.b1062

    Chemistry databases

    BindingDBiP05020
    DrugBankiDB02129 Dihydroorotic Acid
    DB03801 Lysine Nz-Carboxylic Acid
    DB04252 N-Carbamoyl-L-Aspartate
    DB02262 Orotic Acid

    Proteomic databases

    jPOSTiP05020
    PaxDbiP05020
    PRIDEiP05020

    Genome annotation databases

    EnsemblBacteriaiAAC74146; AAC74146; b1062
    BAA35870; BAA35870; BAA35870
    GeneIDi945787
    KEGGiecj:JW1049
    eco:b1062
    PATRICifig|1411691.4.peg.1206

    Organism-specific databases

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

    More...    EchoBASEi    		EB0799

    Phylogenomic databases

    eggNOGiENOG4105EKE Bacteria
    COG0418 LUCA
    HOGENOMiHOG000256259
    InParanoidiP05020
    KOiK01465
    PhylomeDBiP05020

    Enzyme and pathway databases

    UniPathwayiUPA00070;UER00117
    BioCyciEcoCyc:DIHYDROOROT-MONOMER
    ECOL316407:JW1049-MONOMER
    MetaCyc:DIHYDROOROT-MONOMER
    BRENDAi3.5.2.3 2026
    SABIO-RKiP05020

    Miscellaneous databases

    EvolutionaryTraceiP05020

    Protein Ontology

    More...    PROi    		PR:P05020

    Family and domain databases

    CDDicd01294 DHOase, 1 hit
    HAMAPiMF_00219 PyrC_classII, 1 hit
    InterProiView protein in InterPro
    IPR006680 Amidohydro-rel
    IPR004721 DHOdimr
    IPR002195 Dihydroorotase_CS
    IPR032466 Metal_Hydrolase
    PANTHERiPTHR43137 PTHR43137, 1 hit
    PfamiView protein in Pfam
    PF01979 Amidohydro_1, 1 hit
    PIRSFiPIRSF001237 DHOdimr, 1 hit
    SUPFAMiSSF51556 SSF51556, 1 hit
    TIGRFAMsiTIGR00856 pyrC_dimer, 1 hit
    PROSITEiView protein in PROSITE
    PS00482 DIHYDROOROTASE_1, 1 hit
    PS00483 DIHYDROOROTASE_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 nameiPYRC_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: P05020
    <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: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: November 13, 2019
    This is version 176 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. SIMILARITY comments
      Index of protein domains and families
    2. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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