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UniProtKB - P50384 (TRPD_SACS2)

Entry version 143 (02 Dec 2020)
Sequence version 1 (01 Oct 1996)
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Protein

Anthranilate phosphoribosyltransferase

Gene

trpD

Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
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 transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).UniRule annotation2 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

Mg2+Note: Binds 2 magnesium ions per monomer.

<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=50 µM for magnesium (at 60 degrees Celsius and at pH 7.5)2 Publications
  2. KM=40 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
  3. KM=160 µM for phosphoribosylpyrophosphate (at 60 degrees Celsius and at pH 7.5)2 Publications
  4. KM=20 nM for anthranilate (at 25 degrees Celsius and at pH 7.5)2 Publications
  5. KM=26 nM for anthranilate (at 40 degrees Celsius and at pH 7.5)2 Publications
  6. KM=32 nM for anthranilate (at 50 degrees Celsius and at pH 7.5)2 Publications
  7. KM=35 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
  8. KM=500 nM for anthranilate (at 87 degrees Celsius and at pH 7.52 Publications

    <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-tryptophan biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
    2. Anthranilate phosphoribosyltransferase (trpD)
    3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
    4. Indole-3-glycerol phosphate synthase (trpC)
    5. Tryptophan synthase beta chain 2 (trpB2), Tryptophan synthase beta chain 1 (trpB1), Tryptophan synthase alpha chain (trpA)
    This subpathway is part of the pathway L-tryptophan biosynthesis, 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-tryptophan from chorismate, the pathway L-tryptophan biosynthesis 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 sitei79Anthranilate 1; via carbonyl oxygen1
    Binding sitei87PhosphoribosylpyrophosphateUniRule annotation2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi91Magnesium 11
    Binding sitei109Anthranilate 11
    Binding sitei118Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation2 Publications1
    Binding sitei164Anthranilate 21
    Metal bindingi223Magnesium 21
    Metal bindingi224Magnesium 11
    Metal bindingi224Magnesium 21

    <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

    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 functionGlycosyltransferase, Transferase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		SSOL273057:G1FZF-929-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		2.4.2.18, 6163

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P50384

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

    More...    UniPathwayi    		UPA00035;UER00041

    <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:
    Anthranilate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.18UniRule 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:trpDUniRule annotation
    Ordered Locus Names:SSO0890
    <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>OrganismiSaccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
    <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 identifieri273057 [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 lineageiArchaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Saccharolobus ›
    <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
    • UP000001974 <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

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi106K → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency dedreases only 10-fold. 1 Publication1
    Mutagenesisi107H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-178. 1 Publication1
    Mutagenesisi154H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 1 Publication1
    Mutagenesisi164R → A: Strong decrease of the affinity for anthranilate, although only a moderate 7-fold decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi178P → A: 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-107. 1
    Mutagenesisi223D → N: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication1
    Mutagenesisi224E → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication1

    <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_00001545231 – 345Anthranilate phosphoribosyltransferaseAdd BLAST345

    <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 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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    UniRule annotation4 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		273057.SSO0890

    <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

    1345
    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    		P50384

    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    		P50384

    <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>Regioni77 – 79Phosphoribosylpyrophosphate binding3
    Regioni82 – 83Phosphoribosylpyrophosphate binding2
    Regioni89 – 92Phosphoribosylpyrophosphate binding4
    Regioni106 – 114Phosphoribosylpyrophosphate binding9

    <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 anthranilate phosphoribosyltransferase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		arCOG02012, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_034315_2_1_2

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P50384

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		LYHQSFK

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.20.970.10, 1 hit
    3.40.1030.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00211, TrpD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR005940, Anthranilate_Pribosyl_Tfrase
    IPR000312, Glycosyl_Trfase_fam3
    IPR017459, Glycosyl_Trfase_fam3_N_dom
    IPR036320, Glycosyl_Trfase_fam3_N_dom)sf
    IPR035902, Nuc_phospho_transferase

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02885, Glycos_trans_3N, 1 hit
    PF00591, Glycos_transf_3, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF47648, SSF47648, 1 hit
    SSF52418, SSF52418, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01245, trpD, 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.

    P50384-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNINEILKKL INKSDLEINE AEELAKAIIR GEVPEILVSA ILVALRMKGE 
            60         70         80         90        100
    SKNEIVGFAR AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL 
           110        120        130        140        150
    VNPVAKHGNR AVSGKSGSAD VLEALGYNII VPPERAKELV NKTNFVFLFA 
           160        170        180        190        200
    QYYHPAMKNV ANVRKTLGIR TIFNILGPLT NPANAKYQLM GVFSKDHLDL 
           210        220        230        240        250
    LSKSAYELDF NKIILVYGEP GIDEVSPIGN TFMKIVSKRG IEEVKLNVTD 
           260        270        280        290        300
    FGISPIPIEK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD 
           310        320        330        340 
    RVGDFREGYE YADHLIEKSL DKLNEIISMN GDVTKLKTIV VKSSG
    Length:345
    Mass (Da):37,574
    Last modified:October 1, 1996 - 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:iD51927F4B7AAFA90
    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
    		Z50014 Genomic DNA Translation: CAA90309.1
    AE006641 Genomic DNA Translation: AAK41173.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		F90239

    NCBI Reference Sequences

    More...    RefSeqi    		WP_009992305.1, NC_002754.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAK41173; AAK41173; SSO0890

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		44129821

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		sso:SSO0890

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|273057.12.peg.894

    <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
    		Z50014 Genomic DNA Translation: CAA90309.1
    AE006641 Genomic DNA Translation: AAK41173.1
    PIRiF90239
    RefSeqiWP_009992305.1, NC_002754.1

    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
    1GXBX-ray2.70A/B/C/D1-345[»]
    1O17X-ray2.05A/B/C/D1-345[»]
    1ZXYX-ray2.56A/B/C/D1-345[»]
    1ZYKX-ray2.40A/B/C/D1-345[»]
    2GVQX-ray2.43A/B/C/D1-345[»]
    3GBRX-ray2.25A/B1-345[»]
    SMRiP50384
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO0890

    Genome annotation databases

    EnsemblBacteriaiAAK41173; AAK41173; SSO0890
    GeneIDi44129821
    KEGGisso:SSO0890
    PATRICifig|273057.12.peg.894

    Phylogenomic databases

    eggNOGiarCOG02012, Archaea
    HOGENOMiCLU_034315_2_1_2
    InParanoidiP50384
    OMAiLYHQSFK

    Enzyme and pathway databases

    UniPathwayiUPA00035;UER00041
    BioCyciSSOL273057:G1FZF-929-MONOMER
    BRENDAi2.4.2.18, 6163
    SABIO-RKiP50384

    Miscellaneous databases

    EvolutionaryTraceiP50384

    Family and domain databases

    Gene3Di1.20.970.10, 1 hit
    3.40.1030.10, 1 hit
    HAMAPiMF_00211, TrpD, 1 hit
    InterProiView protein in InterPro
    IPR005940, Anthranilate_Pribosyl_Tfrase
    IPR000312, Glycosyl_Trfase_fam3
    IPR017459, Glycosyl_Trfase_fam3_N_dom
    IPR036320, Glycosyl_Trfase_fam3_N_dom)sf
    IPR035902, Nuc_phospho_transferase
    PfamiView protein in Pfam
    PF02885, Glycos_trans_3N, 1 hit
    PF00591, Glycos_transf_3, 1 hit
    SUPFAMiSSF47648, SSF47648, 1 hit
    SSF52418, SSF52418, 1 hit
    TIGRFAMsiTIGR01245, trpD, 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 nameiTRPD_SACS2
    <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: P50384
    <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: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: December 2, 2020
    This is version 143 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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