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UniProtKB - P9WKE3 (KPRS_MYCTU)

Entry version 38 (02 Dec 2020)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors (PubMed:22745722).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation2 PublicationsNote: Binds 2 Mg2+ ions per subunit (Potential). Can also use Mn2+ (PubMed:21085589, PubMed:21045009).UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by inorganic phosphate, and to a lesser extent by sulfate ions (PubMed:21085589, PubMed:21045009). In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:21085589, PubMed:21045009). Strongly inhibited by ADP and GDP through competitive binding at the activation site and at a specific allosteric site (PubMed:21085589, PubMed:21045009, PubMed:22745722). Competitively inhibited by Ca2+, Cu2+ and Fe2+ (PubMed:21085589, PubMed:21045009).3 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 37 sec(-1) with Rib-5-P as substrate (PubMed:21085589). Kcat is 0.83 sec(-1) with Rib-5-P as substrate (PubMed:22745722). Kcat is 0.66 sec(-1) with ATP as substrate (PubMed:22745722). Kcat is 0.155 sec(-1) with UTP as substrate (PubMed:22745722). Kcat is 0.140 sec(-1) with GTP as substrate (PubMed:22745722). Kcat is 0.065 sec(-1) with CTP as substrate (PubMed:22745722).2 Publications
  1. KM=8.2 µM for Rib-5-P1 Publication
  2. KM=14 µM for Rib-5-P1 Publication
  3. KM=25 µM for ATP1 Publication
  4. KM=26 µM for CTP1 Publication
  5. KM=37 µM for GTP1 Publication
  6. KM=52 µM for UTP1 Publication
  7. KM=70 µM for Rib-5-P (without divalent cation)1 Publication
  1. Vmax=601 µmol/min/mg enzyme with ATP as substrate1 Publication
  2. Vmax=530 µmol/min/mg enzyme with Rib-5-P as substrate1 Publication
  3. Vmax=1.41 µmol/min/mg enzyme with Rib-5-P as substrate1 Publication
  4. Vmax=1.12 µmol/min/mg enzyme with ATP as substrate1 Publication
  5. Vmax=0.264 µmol/min/mg enzyme with UTP as substrate1 Publication
  6. Vmax=0.237 µmol/min/mg enzyme with GTP as substrate1 Publication
  7. Vmax=0.237 µmol/min/mg enzyme with CTP as substrate1 Publication

pH dependencei

Optimum pH is close to 8 (PubMed:21085589). Activities at pH 7 and pH 9.5 are 57% and 70% of the maximal activity, respectively (PubMed:21085589, PubMed:21045009).2 Publications

Temperature dependencei

Thermostable.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase (prs)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Pathwayi: cell wall polysaccharide biosynthesis

This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi138Magnesium 1UniRule annotation1
Metal bindingi178Magnesium 2UniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei202UniRule annotation1
<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 sitei204Ribose-5-phosphateUniRule annotation1
Binding sitei230Ribose-5-phosphateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi45 – 47ATPUniRule annotation3
Nucleotide bindingi104 – 105ATPUniRule annotation2

<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 functionAllosteric enzyme, Kinase, Transferase
Biological processCell wall biogenesis/degradation, Nucleotide biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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

More...UniPathwayi		UPA00087;UER00172
UPA00963

<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:
Ribose-phosphate pyrophosphokinaseUniRule annotation (EC:2.7.6.1UniRule annotation3 Publications)
Short name:
RPPKUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphateUniRule annotation
Phosphoribosyl diphosphate synthaseUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthaseUniRule annotation
Short name:
PRPP synthase1 PublicationUniRule annotation
Short name:
PRPPase1 PublicationUniRule 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:prsUniRule annotation
Ordered Locus Names:Rv1017c
ORF Names:MTCY10G2.32
<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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<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 identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
<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
  • UP000001584 <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

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...TubercuListi		Rv1017c

<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 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_00001411641 – 326Ribose-phosphate pyrophosphokinaseAdd BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki29Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P9WKE3

<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

Homohexamer.

1 Publication2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		83332.Rv1017c

<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

3D structure databases

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

More...SMRi		P9WKE3

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni234 – 238Ribose-5-phosphate bindingUniRule annotation5

<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 ribose-phosphate pyrophosphokinase family. Class I subfamily.1 PublicationUniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0462, Bacteria

Identification of Orthologs from Complete Genome Data

More...OMAi		FGWARQD

Database for complete collections of gene phylogenies

More...PhylomeDBi		P9WKE3

Family and domain databases

Conserved Domains Database

More...CDDi		cd06223, PRTases_typeI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.2020, 2 hits

HAMAP database of protein families

More...HAMAPi		MF_00583_B, RibP_PPkinase_B, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000842, PRib_PP_synth_CS
IPR029099, Pribosyltran_N
IPR000836, PRibTrfase_dom
IPR029057, PRTase-like
IPR005946, Rib-P_diPkinase
IPR037515, Rib-P_diPkinase_bac

The PANTHER Classification System

More...PANTHERi		PTHR10210, PTHR10210, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14572, Pribosyl_synth, 1 hit
PF13793, Pribosyltran_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53271, SSF53271, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01251, ribP_PPkin, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00114, PRPP_SYNTHASE, 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.

P9WKE3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSHDWTDNRK NLMLFAGRAH PELAEQVAKE LDVHVTSQDA REFANGEIFV 
        60         70         80         90        100
RFHESVRGCD AFVLQSCPAP VNRWLMEQLI MIDALKRGSA KRITAVMPFY 
       110        120        130        140        150
PYARQDKKHR GREPISARLI ADLLKTAGAD RIVTVDLHTD QIQGFFDGPV 
       160        170        180        190        200
DHMRGQNLLT GYIRDNYPDG NMVVVSPDSG RVRIAEKWAD ALGGVPLAFI 
       210        220        230        240        250
HKTRDPRVPN QVVSNRVVGD VAGRTCVLID DMIDTGGTIA GAVALLHNDG 
       260        270        280        290        300
AGDVIIAATH GVLSDPAAQR LASCGAREVI VTNTLPIGED KRFPQLTVLS 
       310        320 
IAPLLASTIR AVFENGSVTG LFDGDA
Length:326
Mass (Da):35,477
Last modified:April 16, 2014 - 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:i4CE64D17E783AC37
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
AL123456 Genomic DNA Translation: CCP43767.1

Protein sequence database of the Protein Information Resource

More...PIRi		D70622

NCBI Reference Sequences

More...RefSeqi		NP_215533.1, NC_000962.3
WP_003405263.1, NZ_NVQJ01000018.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CCP43767; CCP43767; Rv1017c

Database of genes from NCBI RefSeq genomes

More...GeneIDi		23492851
885993

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mtu:Rv1017c
mtv:RVBD_1017c

<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
AL123456 Genomic DNA Translation: CCP43767.1
PIRiD70622
RefSeqiNP_215533.1, NC_000962.3
WP_003405263.1, NZ_NVQJ01000018.1

3D structure databases

SMRiP9WKE3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1017c

Proteomic databases

PaxDbiP9WKE3

Genome annotation databases

EnsemblBacteriaiCCP43767; CCP43767; Rv1017c
GeneIDi23492851
885993
KEGGimtu:Rv1017c
mtv:RVBD_1017c

Organism-specific databases

TubercuListiRv1017c

Phylogenomic databases

eggNOGiCOG0462, Bacteria
OMAiFGWARQD
PhylomeDBiP9WKE3

Enzyme and pathway databases

UniPathwayiUPA00087;UER00172
UPA00963

Family and domain databases

CDDicd06223, PRTases_typeI, 1 hit
Gene3Di3.40.50.2020, 2 hits
HAMAPiMF_00583_B, RibP_PPkinase_B, 1 hit
InterProiView protein in InterPro
IPR000842, PRib_PP_synth_CS
IPR029099, Pribosyltran_N
IPR000836, PRibTrfase_dom
IPR029057, PRTase-like
IPR005946, Rib-P_diPkinase
IPR037515, Rib-P_diPkinase_bac
PANTHERiPTHR10210, PTHR10210, 1 hit
PfamiView protein in Pfam
PF14572, Pribosyl_synth, 1 hit
PF13793, Pribosyltran_N, 1 hit
SUPFAMiSSF53271, SSF53271, 1 hit
TIGRFAMsiTIGR01251, ribP_PPkin, 1 hit
PROSITEiView protein in PROSITE
PS00114, PRPP_SYNTHASE, 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 nameiKPRS_MYCTU
<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: P9WKE3
Secondary accession number(s): L0T8D7, P65232, P96383
<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: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 2, 2020
This is version 38 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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