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Protein

Ribose-phosphate pyrophosphokinase

Gene

prs

Organism
Bacillus subtilis (strain 168)
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) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).UniRule annotation1 Publication4 Publications

Miscellaneous

This enzyme uses a steady state ordered mechanism, where Mg2+ binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.1 Publication

<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

Mg2+1 PublicationUniRule annotation1 PublicationNote: Binds 2 Mg2+ ions per subunit. Each Mg2+ binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrates and water molecules to complete their coordination spheres (PubMed:2169413, PubMed:11790837). Can also use Mn2+ and Cd2+ ions, but the activity is less than that obtained with Mg2+ ions (PubMed:2169413, PubMed:11790837).1 Publication2 Publications

<p>This subsection of the ‘Function’ 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:2169413). In addition to form a complex with ATP, Mg2+ also acts as a cofactor (PubMed:2169413). Strongly inhibited by ADP through competitive binding at the activation site and at a specific allosteric site (PubMed:2169413, PubMed:16008562). Less strongly inhibited by alpha,beta-methylene ATP (mADP), AMP, GDP, GMP and UTP (PubMed:2169413, PubMed:16008562).2 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

  1. KM=191 µM for ATP (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=230 µM for Rib-5-P (at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=480 µM for Rib-5-P (at pH 8.2 and 37 degrees Celsius)1 Publication
  4. KM=660 µM for ATP (at pH 8.2 and 37 degrees Celsius)1 Publication
  1. Vmax=108 µmol/min/mg enzyme (at pH 8 and 37 degrees Celsius)1 Publication
  2. Vmax=250 µmol/min/mg enzyme (at pH 8.2 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8-8.5. Activities at pH 7 and pH 9.5 are 35% and 85% of the maximal activity, respectively.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: 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 annotation2 Publications
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei106Allosteric inhibitorCombined sources1 Publication1
Binding sitei110Allosteric inhibitorCombined sources2 Publications1
<p>This subsection of the ‘Function’ 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 bindingi136Magnesium 11 PublicationUniRule annotationCombined sources1 Publication1
Binding sitei141Allosteric inhibitorCombined sources1 Publication1
Metal bindingi175Magnesium 21 PublicationUniRule annotationCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 sitei1981 Publication1 Publication1
Binding sitei200Ribose-5-phosphateUniRule annotationBy similarity1
Binding sitei224Ribose-5-phosphateUniRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi43 – 45ATPUniRule annotation1 Publication3
Nucleotide bindingi102 – 103ATPUniRule annotationCombined sources1 Publication1 Publication2

<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

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: UniProtKB-UniRule
  • ribose phosphate diphosphokinase activity Source: GO_Central

GO - Biological processi

<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 processNucleotide biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU00510-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P14193

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

More...
UniPathwayi
UPA00087;UER00172

<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:
Ribose-phosphate pyrophosphokinase1 PublicationUniRule annotation (EC:2.7.6.1UniRule annotation2 Publications)
Short name:
RPPK1 PublicationUniRule annotation
Alternative name(s):
5-phospho-D-ribosyl alpha-1-diphosphate1 PublicationUniRule annotation
Phosphoribosyl diphosphate synthase1 PublicationUniRule annotation
Phosphoribosyl pyrophosphate synthase1 PublicationUniRule annotation
Short name:
P-Rib-PP synthase1 PublicationUniRule annotation
Short name:
PPRibP synthase1 Publication
Short name:
PRPP synthase1 PublicationUniRule annotation
Short name:
PRPPase1 PublicationUniRule 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:prs1 PublicationUniRule annotation
Ordered Locus Names:BSU00510
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<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
  • UP000001570 <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

<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

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>Mutagenesisi198K → A: Strong decrease of the Vmax value compared to that of the wild-type. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type. The cooperativity of ADP binding is reduced. 1 Publication1
Mutagenesisi200R → A: Strong decrease of the Vmax value compared to that of the wild-type enzyme. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type. 1 Publication1
Mutagenesisi202R → A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1
Mutagenesisi204N → A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1
Mutagenesisi207E → A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02798 Alpha-Methylene Adenosine Monophosphate
DB03148 Phosphomethylphosphonic Acid Adenosyl Ester

<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_00001411102 – 317Ribose-phosphate pyrophosphokinaseAdd BLAST316

Proteomic databases

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

More...
PaxDbi
P14193

PRoteomics IDEntifications database

More...
PRIDEi
P14193

<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

Homohexamer; trimer of dimers.1 Publication2 Publications

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P14193, 2 interactors

Molecular INTeraction database

More...
MINTi
P14193

STRING: functional protein association networks

More...
STRINGi
224308.Bsubs1_010100000260

<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

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P14193

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

More...
SMRi
P14193

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P14193

<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>Regioni149 – 150Allosteric inhibitor bindingCombined sources1 Publication2
Regioni228 – 232Ribose-5-phosphate bindingUniRule annotationCombined sources2 Publications5

<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
ENOG4105C5T Bacteria
COG0462 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000210451

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P14193

KEGG Orthology (KO)

More...
KOi
K00948

Identification of Orthologs from Complete Genome Data

More...
OMAi
FGWARQD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14193

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06223 PRTases_typeI, 1 hit

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

P14193-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI
60 70 80 90 100
EESIRGCDCY IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY
110 120 130 140 150
ARQDRKARSR EPITAKLFAN LLETAGATRV IALDLHAPQI QGFFDIPIDH
160 170 180 190 200
LMGVPILGEY FEGKNLEDIV IVSPDHGGVT RARKLADRLK APIAIIDKRR
210 220 230 240 250
PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL VENGAKEVYA
260 270 280 290 300
CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA
310
EAIIRVHEQQ SVSYLFS
Length:317
Mass (Da):34,868
Last modified:January 1, 1990 - 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:i0D37FC81668111EB
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
X16518 Genomic DNA Translation: CAA34523.1
D26185 Genomic DNA Translation: BAA05286.1
AL009126 Genomic DNA Translation: CAB11827.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S05372 KIBSRS

NCBI Reference Sequences

More...
RefSeqi
NP_387932.1, NC_000964.3
WP_003218353.1, NZ_JNCM01000028.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB11827; CAB11827; BSU00510

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
936985

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU00510

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.51

<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
X16518 Genomic DNA Translation: CAA34523.1
D26185 Genomic DNA Translation: BAA05286.1
AL009126 Genomic DNA Translation: CAB11827.1
PIRiS05372 KIBSRS
RefSeqiNP_387932.1, NC_000964.3
WP_003218353.1, NZ_JNCM01000028.1

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
1DKRX-ray2.30A/B1-317[»]
1DKUX-ray2.20A/B1-317[»]
1IBSX-ray2.80A/B1-317[»]
ProteinModelPortaliP14193
SMRiP14193
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP14193, 2 interactors
MINTiP14193
STRINGi224308.Bsubs1_010100000260

Chemistry databases

DrugBankiDB02798 Alpha-Methylene Adenosine Monophosphate
DB03148 Phosphomethylphosphonic Acid Adenosyl Ester

Proteomic databases

PaxDbiP14193
PRIDEiP14193

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11827; CAB11827; BSU00510
GeneIDi936985
KEGGibsu:BSU00510
PATRICifig|224308.179.peg.51

Phylogenomic databases

eggNOGiENOG4105C5T Bacteria
COG0462 LUCA
HOGENOMiHOG000210451
InParanoidiP14193
KOiK00948
OMAiFGWARQD
PhylomeDBiP14193

Enzyme and pathway databases

UniPathwayi
UPA00087;UER00172

BioCyciBSUB:BSU00510-MONOMER
SABIO-RKiP14193

Miscellaneous databases

EvolutionaryTraceiP14193

Protein Ontology

More...
PROi
PR:P14193

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
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...

<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_BACSU
<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: P14193
<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: January 1, 1990
Last sequence update: January 1, 1990
Last modified: December 5, 2018
This is version 150 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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