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Entry version 65 (29 Sep 2021)
Sequence version 2 (13 Apr 2016)
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Protein

Bifunctional ribokinase/ribose-5-phosphate isomerase A

Gene

rbsK/rbiA

Organism
Fructilactobacillus sanfranciscensis (strain ATCC 27651 / DSM 20451 / JCM 5668 / CCUG 30143 / KCTC 3205 / NCIMB 702811 / NRRL B-3934 / L-12) (Lactobacillus sanfranciscensis)
Status
Reviewed-Annotation score:

Annotation score:4 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

Bifunctional enzyme that catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium, and the reversible conversion of ribose 5-phosphate to ribulose 5-phosphate.

By similarity

<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+By similarityNote: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.By similarity

<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 a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Also activated by ammonium ion. Ion binding induces a conformational change that may alter substrate affinity.By similarity

<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: D-ribose degradation

This protein is involved in step 2 of the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose.By similarity This subpathway is part of the pathway D-ribose degradation, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose, the pathway D-ribose degradation and in Carbohydrate metabolism.

Pathwayi: pentose phosphate pathway

This protein is involved in step 1 of the subpathway that synthesizes D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage).By similarity This subpathway is part of the pathway pentose phosphate pathway, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage), the pathway pentose phosphate pathway and in Carbohydrate degradation.

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 sitei141Substrate; for ribokinase activityBy similarity1
Binding sitei185ATPBy similarity1
<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 bindingi247PotassiumBy similarity1
Metal bindingi249Potassium; via carbonyl oxygenBy similarity1
<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 sitei253Proton acceptor; for ribokinase activityBy similarity1
Binding sitei253Substrate; for ribokinase activityBy similarity1
Metal bindingi284Potassium; via carbonyl oxygenBy similarity1
Metal bindingi287Potassium; via carbonyl oxygenBy similarity1
Metal bindingi289Potassium; via carbonyl oxygenBy similarity1
Metal bindingi293PotassiumBy similarity1
Active sitei417Proton acceptor; for ribose-5-phosphate isomerase activityBy similarity1
Binding sitei435Substrate; for ribose-5-phosphate isomerase activityBy similarity1

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 bindingi221 – 226ATPBy similarity6
Nucleotide bindingi252 – 253ATPBy similarity2

<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

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 functionIsomerase, Kinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00115;UER00412
UPA00916;UER00889

<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:
Bifunctional ribokinase/ribose-5-phosphate isomerase ACurated
Including the following 2 domains:
RibokinaseBy similarity (EC:2.7.1.15By similarity)
Ribose-5-phosphate isomerase ABy similarity (EC:5.3.1.6By similarity)
Alternative name(s):
Phosphoriboisomerase A
Short name:
PRI
<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:rbsK/rbiA
ORF Names:FD36_GL000739
<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>OrganismiFructilactobacillus sanfranciscensis (strain ATCC 27651 / DSM 20451 / JCM 5668 / CCUG 30143 / KCTC 3205 / NCIMB 702811 / NRRL B-3934 / L-12) (Lactobacillus sanfranciscensis)
<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 identifieri1423800 [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 lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeFructilactobacillus

<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

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_00002859831 – 540Bifunctional ribokinase/ribose-5-phosphate isomerase AAdd BLAST540

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By elevated hydrostatic pressure.1 Publication

<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
P83534

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>Regioni1 – 308RibokinaseAdd BLAST308
Regioni11 – 13Substrate binding; for ribokinase activityBy similarity3
Regioni39 – 44Substrate binding; for ribokinase activityBy similarity6
Regioni309 – 540Ribose-5-phosphate isomerase AAdd BLAST232
Regioni339 – 342Substrate binding; for ribose-5-phosphate isomerase activityBy similarity4
Regioni395 – 398Substrate binding; for ribose-5-phosphate isomerase activityBy similarity4
Regioni408 – 411Substrate binding; for ribose-5-phosphate isomerase activityBy similarity4

<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

In the N-terminal section; belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily.Curated
In the C-terminal section; belongs to the ribose 5-phosphate isomerase family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01174, ribokinase, 1 hit
cd01398, RPI_A, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1190.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01987, Ribokinase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011877, D_ribokin
IPR037171, NagB/RpiA_transferase-like
IPR011611, PfkB_dom
IPR002139, Ribo/fructo_kinase
IPR029056, Ribokinase-like
IPR004788, Ribose5P_isomerase_type_A

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00294, PfkB, 1 hit
PF06026, Rib_5-P_isom_A, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00990, RIBOKINASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF100950, SSF100950, 1 hit
SSF53613, SSF53613, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02152, D_ribokin_bact, 1 hit
TIGR00021, rpiA, 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.

P83534-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKIIVVGST NVDKVLNVEK YALPGETLAI NTYQQSHGGG KGANQAIAAA
60 70 80 90 100
RSGADTTFIT KLGNDEDAKM MVKGFKADGM NIDDVITTTD QETGKAYITV
110 120 130 140 150
DKSGQNSIYV YGGANMAMTP TDVDAHKSAI INADRVIAQL EIPVPAVIEA
160 170 180 190 200
FKIAKEHGVQ TILNPAPAKE LPEELLKLTD IITPNESEAA TLTGIEVKDE
210 220 230 240 250
TSMLANAKFF FERGIKMVII TVGGRGSFFA TPDDHALIPP FPAKVVDTTA
260 270 280 290 300
AGDTFIGSLA SQLEIDLSNI RKAMLYASHA SSLTIQVAGA QNSIPTREAI
310 320 330 340 350
LNVINQDQMT KTEIEKQKAQ AAAYAAKLVP DHIVLGLGSG TTAAYFVKAI
360 370 380 390 400
NQRINDEHLD IQCVATSVGT EKLAEKLGMR MLDVNTIDQV DLTVDGADVV
410 420 430 440 450
DHQLNGIKGG GAALLFEKLV ADMSKQNIWI VDQSKYTDSL AGHILTIEVI
460 470 480 490 500
PFGGMGVFRY LKENGYQPEF RFKDNGDILE TDSGNYLINI IIPKDADLEK
510 520 530 540
LSIDLKKQTG VVEHGLFLNV CDELIIGGDQ IKTIKRSDLS
Length:540
Mass (Da):58,137
Last modified:April 13, 2016 - 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:i8FB6CC65FBC243E8
GO

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 conflicti256I → L AA sequence (PubMed:12112860).Curated1
Sequence conflicti262Q → K AA sequence (PubMed:12112860).Curated1
Sequence conflicti265I → L AA sequence (PubMed:12112860).Curated1
Sequence conflicti267L → E AA sequence (PubMed:12112860).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
AYYM01000003 Genomic DNA Translation: KRM80848.1

NCBI Reference Sequences

More...
RefSeqi
WP_056957679.1, NZ_MIYJ01000023.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57099720

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1423800.3.peg.750

<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
AYYM01000003 Genomic DNA Translation: KRM80848.1
RefSeqiWP_056957679.1, NZ_MIYJ01000023.1

3D structure databases

SMRiP83534
ModBaseiSearch...

Genome annotation databases

GeneIDi57099720
PATRICifig|1423800.3.peg.750

Enzyme and pathway databases

UniPathwayiUPA00115;UER00412
UPA00916;UER00889

Family and domain databases

CDDicd01174, ribokinase, 1 hit
cd01398, RPI_A, 1 hit
Gene3Di3.40.1190.20, 1 hit
HAMAPiMF_01987, Ribokinase, 1 hit
InterProiView protein in InterPro
IPR011877, D_ribokin
IPR037171, NagB/RpiA_transferase-like
IPR011611, PfkB_dom
IPR002139, Ribo/fructo_kinase
IPR029056, Ribokinase-like
IPR004788, Ribose5P_isomerase_type_A
PfamiView protein in Pfam
PF00294, PfkB, 1 hit
PF06026, Rib_5-P_isom_A, 1 hit
PRINTSiPR00990, RIBOKINASE
SUPFAMiSSF100950, SSF100950, 1 hit
SSF53613, SSF53613, 1 hit
TIGRFAMsiTIGR02152, D_ribokin_bact, 1 hit
TIGR00021, rpiA, 1 hit

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 nameiRBSKI_FRUSL
<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: P83534
Secondary accession number(s): A0A0R2BNR0
<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: May 1, 2007
Last sequence update: April 13, 2016
Last modified: September 29, 2021
This is version 65 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

Direct protein sequencing

Documents

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