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UniProtKB - P27828 (WECB_ECOLI)

Entry version 152 (11 Dec 2019)
Sequence version 2 (01 Jul 1993)
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Protein

UDP-N-acetylglucosamine 2-epimerase

Gene

wecB

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 epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption.5 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 <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

Allosterically activated by its substrate, UDP-GlcNAc.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

kcat is 7.1 sec(-1).1 Publication
  1. KM=0.6 mM for UDP-GlcNAc1 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: enterobacterial common antigen biosynthesis

    This protein is involved in the pathway enterobacterial common antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.

    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 sitei10SubstrateUniRule annotation2 Publications1
    Binding sitei15SubstrateUniRule annotation1 Publication1
    Binding sitei95SubstrateUniRule annotation1 Publication1
    Binding sitei117SubstrateUniRule annotation1 Publication1
    Binding sitei213SubstrateUniRule annotation2 Publications1
    Binding sitei271Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation2 Publications1
    Binding sitei276SubstrateUniRule annotation2 Publications1
    Binding sitei296SubstrateUniRule annotation2 Publications1
    Binding sitei313SubstrateUniRule annotation1 Publication1

    <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

    • identical protein binding Source: EcoCyc
    • UDP-N-acetylglucosamine 2-epimerase activity 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 functionAllosteric enzyme, Isomerase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:UDPGLCNACEPIM-MONOMER
    ECOL316407:JW5600-MONOMER
    MetaCyc:UDPGLCNACEPIM-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		3.2.1.183 1960
    5.1.3.14 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P27828

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

    More...    UniPathwayi    		UPA00566

    <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:
    UDP-N-acetylglucosamine 2-epimeraseUniRule annotationCurated (EC:5.1.3.14UniRule annotation2 Publications)
    Alternative name(s):
    Bacteriophage N4 adsorption protein C1 Publication
    UDP-GlcNAc-2-epimeraseUniRule annotationCurated
    <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:wecBUniRule annotation
    Synonyms:nfrC1 Publication, rffE1 Publication, yifF
    Ordered Locus Names:b3786, JW5600
    <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 ...

    Keywords - Cellular componenti

    Cytoplasm

    <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>Mutagenesisi15K → A: More than 100-fold increase in KM for UDP-GlcNAc. 1 Publication1
    Mutagenesisi95D → N: Strong decrease in activity. 1 Publication1
    Mutagenesisi117E → Q: Strong decrease in activity. 1 Publication1
    Mutagenesisi131E → Q: Strong decrease in activity. 1 Publication1
    Mutagenesisi213H → N: 30-fold increase in KM for UDP-GlcNAc and 50-fold decrease in kcat. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB03435 Uridine-5'-Diphosphate
    DB02196 Uridine-Diphosphate-N-Acetylgalactosamine

    <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_00002085271 – 376UDP-N-acetylglucosamine 2-epimeraseAdd BLAST376

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P27828

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

    More...    PaxDbi    		P27828

    PRoteomics IDEntifications database

    More...    PRIDEi    		P27828

    <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 annotation1 Publication

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4263321, 147 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b3786

    <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

    1376
    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    		P27828

    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    		P27828

    <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>Regioni290 – 292Substrate bindingUniRule annotation2 Publications3

    <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 UDP-N-acetylglucosamine 2-epimerase family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105EAG Bacteria
    COG0381 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000076048

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P27828

    KEGG Orthology (KO)

    More...    KOi    		K01791

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P27828

    Family and domain databases

    HAMAP database of protein families

    More...    HAMAPi    		MF_02028 WecB_RffE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003331 UDP_GlcNAc_Epimerase_2_dom
    IPR032892 WecB
    IPR029767 WecB-like

    The PANTHER Classification System

    More...    PANTHERi    		PTHR43174 PTHR43174, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02350 Epimerase_2, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00236 wecB, 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.

    P27828-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKVLTVFGTR PEAIKMAPLV HALAKDPFFE AKVCVTAQHR EMLDQVLKLF 
            60         70         80         90        100
    SIVPDYDLNI MQPGQGLTEI TCRILEGLKP ILAEFKPDVV LVHGDTTTTL 
           110        120        130        140        150
    ATSLAAFYQR IPVGHVEAGL RTGDLYSPWP EEANRTLTGH LAMYHFSPTE 
           160        170        180        190        200
    TSRQNLLREN VADSRIFITG NTVIDALLWV RDQVMSSDKL RSELAANYPF 
           210        220        230        240        250
    IDPDKKMILV TGHRRESFGR GFEEICHALA DIATTHQDIQ IVYPVHLNPN 
           260        270        280        290        300
    VREPVNRILG HVKNVILIDP QEYLPFVWLM NHAWLILTDS GGIQEEAPSL 
           310        320        330        340        350
    GKPVLVMRDT TERPEAVTAG TVRLVGTDKQ RIVEEVTRLL KDENEYQAMS 
           360        370 
    RAHNPYGDGQ ACSRILEALK NNRISL
    Length:376
    Mass (Da):42,245
    Last modified:July 1, 1993 - 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:i7B02EE6C2630DD77
    GO

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

    The sequence AAA67586 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti191Missing in AAA67586 (PubMed:1379743).Curated1

    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
    		L18799 Unassigned DNA Translation: AAC36847.1
    M87049 Genomic DNA Translation: AAA67586.1 Different initiation.
    U00096 Genomic DNA Translation: AAT48211.1
    AP009048 Genomic DNA Translation: BAE77512.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		E65182

    NCBI Reference Sequences

    More...    RefSeqi    		WP_001340422.1, NZ_SSZK01000025.1
    YP_026253.1, NC_000913.3

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAT48211; AAT48211; b3786
    BAE77512; BAE77512; BAE77512

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		944789

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW5600
    eco:b3786

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|511145.12.peg.3902

    <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
    		L18799 Unassigned DNA Translation: AAC36847.1
    M87049 Genomic DNA Translation: AAA67586.1 Different initiation.
    U00096 Genomic DNA Translation: AAT48211.1
    AP009048 Genomic DNA Translation: BAE77512.1
    PIRiE65182
    RefSeqiWP_001340422.1, NZ_SSZK01000025.1
    YP_026253.1, NC_000913.3

    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
    1F6DX-ray2.50A/B/C/D1-376[»]
    1VGVX-ray2.31A/B/C/D2-376[»]
    SMRiP27828
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4263321, 147 interactors
    STRINGi511145.b3786

    Chemistry databases

    DrugBankiDB03435 Uridine-5'-Diphosphate
    DB02196 Uridine-Diphosphate-N-Acetylgalactosamine

    Proteomic databases

    jPOSTiP27828
    PaxDbiP27828
    PRIDEiP27828

    Genome annotation databases

    EnsemblBacteriaiAAT48211; AAT48211; b3786
    BAE77512; BAE77512; BAE77512
    GeneIDi944789
    KEGGiecj:JW5600
    eco:b3786
    PATRICifig|511145.12.peg.3902

    Organism-specific databases

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

    More...    EchoBASEi    		EB1420

    Phylogenomic databases

    eggNOGiENOG4105EAG Bacteria
    COG0381 LUCA
    HOGENOMiHOG000076048
    InParanoidiP27828
    KOiK01791
    PhylomeDBiP27828

    Enzyme and pathway databases

    UniPathwayiUPA00566
    BioCyciEcoCyc:UDPGLCNACEPIM-MONOMER
    ECOL316407:JW5600-MONOMER
    MetaCyc:UDPGLCNACEPIM-MONOMER
    BRENDAi3.2.1.183 1960
    5.1.3.14 2026
    SABIO-RKiP27828

    Miscellaneous databases

    EvolutionaryTraceiP27828

    Protein Ontology

    More...    PROi    		PR:P27828

    Family and domain databases

    HAMAPiMF_02028 WecB_RffE, 1 hit
    InterProiView protein in InterPro
    IPR003331 UDP_GlcNAc_Epimerase_2_dom
    IPR032892 WecB
    IPR029767 WecB-like
    PANTHERiPTHR43174 PTHR43174, 1 hit
    PfamiView protein in Pfam
    PF02350 Epimerase_2, 1 hit
    TIGRFAMsiTIGR00236 wecB, 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 nameiWECB_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: P27828
    Secondary accession number(s): P76753, Q2M894
    <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 1, 1992
    Last sequence update: July 1, 1993
    Last modified: December 11, 2019
    This is version 152 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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