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UniProtKB - A1A6H3 (RBSK_ARATH)

Entry version 122 (23 Feb 2022)
Sequence version 1 (23 Jan 2007)
Previous versions | rss
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Protein

Ribokinase

Gene

RBSK

Organism
Arabidopsis thaliana (Mouse-ear cress)
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 phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity) (PubMed:27601466).

Can also use xylose and fructose as carbohydrate substrates with a low efficiency (PubMed:27601466).

Can use GTP, and, to a lower extent, CTP and UTP as alternative phosphoryl donors (PubMed:27601466).

UniRule annotation1 Publication

Caution

Cleavage site of the transit peptide is likely localized before the predicted cleavage site at Val-74, probably around His-67.1 Publication

<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 annotationNote: 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.UniRule annotation

<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. Ion binding induces a conformational change that may alter substrate affinity (By similarity) (PubMed:27601466). Repressed by calcium, rubidium and sodium (PubMed:27601466). Substrate inhibition is observed in the presence of high ATP concentration (Ki=2.44 mM) (PubMed:27601466).UniRule annotation1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2 sec(-1).1 Publication
  1. KM=150 µM for D-ribose1 Publication
  2. KM=45 µM for ATP1 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: D-ribose degradation

This protein is involved in step 2 of the subpathway that synthesizes D-ribose 5-phosphate from beta-D-ribopyranose.UniRule annotation 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.

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 sitei210SubstrateUniRule annotation1
Binding sitei255ATPUniRule annotation1
<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 bindingi319PotassiumUniRule annotation1
Metal bindingi321Potassium; via carbonyl oxygenUniRule 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 sitei325Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi355Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi358Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi360Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi364PotassiumUniRule 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 bindingi291 – 296ATPUniRule annotation6
Nucleotide bindingi324 – 325ATPUniRule 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

  • ATP binding Source: UniProtKB-UniRule
  • metal ion binding Source: UniProtKB-KW
  • ribokinase activity Source: TAIR
Complete GO annotation on QuickGO ...

GO - Biological processi

  • D-ribose catabolic process Source: UniProtKB-UniRule
  • nucleoside metabolic process Source: TAIR
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 functionKinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		ARA:AT1G17160-MONOMER

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

More...UniPathwayi		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:
RibokinaseUniRule annotation (EC:2.7.1.15UniRule annotation1 Publication)
Short name:
AtRBSK1 Publication
Short name:
RKUniRule 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:RBSK1 Publication
Ordered Locus Names:At1g17160Imported
ORF Names:F20D23.14Imported
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
<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
  • UP000006548 <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 1

Organism-specific databases

Arabidopsis Information Portal

More...Araporti		AT1G17160

The Arabidopsis Information Resource

More...TAIRi		locus:2020337, AT1G17160

<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

Chloroplast, Plastid

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abnormal accumulation of D-ribose. D-ribose hypersensitivity; normal growth except in the presence of D-ribose, which leads to chlorosis and growth inhibition.1 Publication

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>Mutagenesisi1 – 74Missing : Loss of ribokinase activity. 1 PublicationAdd BLAST74

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?Chloroplast1 Publication
<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_0000446983? – 379Ribokinase

Proteomic databases

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

More...PaxDbi		A1A6H3

PRoteomics IDEntifications database

More...PRIDEi		A1A6H3

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		181456

<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		A1A6H3, baseline and differential

<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 annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		3702.AT1G17160.1

<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

1379
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		A1A6H3

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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>Regioni78 – 80Substrate bindingUniRule annotation3
Regioni106 – 110Substrate 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 carbohydrate kinase PfkB family. Ribokinase subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2855, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_027634_2_2_1

Identification of Orthologs from Complete Genome Data

More...OMAi		DIVLIQQ

Database of Orthologous Groups

More...OrthoDBi		918144at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		A1A6H3

Family and domain databases

Conserved Domains Database

More...CDDi		cd01174, ribokinase, 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
IPR002173, Carboh/pur_kinase_PfkB_CS
IPR011877, D_ribokin
IPR011611, PfkB_dom
IPR002139, Ribo/fructo_kinase
IPR029056, Ribokinase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00294, PfkB, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00990, RIBOKINASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53613, SSF53613, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00584, PFKB_KINASES_2, 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>Sequence (1+)i

<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.

<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 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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

A1A6H3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMKGISSVSQ SINYNPYIEF NRPQLQISTV NPNPAQSRFS RPRSLRVLSL 
        60         70         80         90        100
SADPSANRNP KSAVDAHAPP LVVVGSANAD IYVEIERLPK EGETISAKTG 
       110        120        130        140        150
QTLAGGKGAN QAACGAKLMY PTYFVGRLGE DAHGKLIAEA LGDDGCGVHL 
       160        170        180        190        200
DYVRSVNNEP TGHAVVMLQS DGQNSIIIVG GANMKAWPEI MSDDDLEIVR 
       210        220        230        240        250
NAGIVLLQRE IPDSINIQVA KAVKKAGVPV ILDVGGMDTP IPNELLDSID 
       260        270        280        290        300
ILSPNETELS RLTGMPTETF EQISQAVAKC HKLGVKQVLV KLGSKGSALF 
       310        320        330        340        350
IQGEKPIQQS IIPAAQVVDT TGAGDTFTAA FAVAMVEGKS HEECLRFAAA 
       360        370 
AASLCVQVKG AIPSMPDRKS VLKLLKFSI
Length:379
Mass (Da):40,189
Last modified:January 23, 2007 - 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:i5EF5A99F01E3BF6D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MQX7A8MQX7_ARATH
Ribokinase
At1g17160, F20D23.14, F20D23_14
355Annotation 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>

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

The sequence AAD50017 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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
AC007651 Genomic DNA Translation: AAD50017.1 Different initiation.
CP002684 Genomic DNA Translation: AEE29552.1
BT029492 mRNA Translation: ABL66749.1

Protein sequence database of the Protein Information Resource

More...PIRi		F86307

NCBI Reference Sequences

More...RefSeqi		NP_173159.1, NM_101577.5

Genome annotation databases

Ensembl plant genome annotation project

More...EnsemblPlantsi		AT1G17160.1; AT1G17160.1; AT1G17160

Database of genes from NCBI RefSeq genomes

More...GeneIDi		838287

Gramene; a comparative resource for plants

More...Gramenei		AT1G17160.1; AT1G17160.1; AT1G17160

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ath:AT1G17160

<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
AC007651 Genomic DNA Translation: AAD50017.1 Different initiation.
CP002684 Genomic DNA Translation: AEE29552.1
BT029492 mRNA Translation: ABL66749.1
PIRiF86307
RefSeqiNP_173159.1, NM_101577.5

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
6ILRX-ray1.97A/B68-379[»]
6ILSX-ray1.80A/B68-379[»]
6ILTX-ray2.20A/B68-379[»]
SMRiA1A6H3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G17160.1

Proteomic databases

PaxDbiA1A6H3
PRIDEiA1A6H3
ProteomicsDBi181456

Genome annotation databases

EnsemblPlantsiAT1G17160.1; AT1G17160.1; AT1G17160
GeneIDi838287
GrameneiAT1G17160.1; AT1G17160.1; AT1G17160
KEGGiath:AT1G17160

Organism-specific databases

AraportiAT1G17160
TAIRilocus:2020337, AT1G17160

Phylogenomic databases

eggNOGiKOG2855, Eukaryota
HOGENOMiCLU_027634_2_2_1
OMAiDIVLIQQ
OrthoDBi918144at2759
PhylomeDBiA1A6H3

Enzyme and pathway databases

UniPathwayiUPA00916;UER00889
BioCyciARA:AT1G17160-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:A1A6H3

Gene expression databases

ExpressionAtlasiA1A6H3, baseline and differential

Family and domain databases

CDDicd01174, ribokinase, 1 hit
Gene3Di3.40.1190.20, 1 hit
HAMAPiMF_01987, Ribokinase, 1 hit
InterProiView protein in InterPro
IPR002173, Carboh/pur_kinase_PfkB_CS
IPR011877, D_ribokin
IPR011611, PfkB_dom
IPR002139, Ribo/fructo_kinase
IPR029056, Ribokinase-like
PfamiView protein in Pfam
PF00294, PfkB, 1 hit
PRINTSiPR00990, RIBOKINASE
SUPFAMiSSF53613, SSF53613, 1 hit
PROSITEiView protein in PROSITE
PS00584, PFKB_KINASES_2, 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 nameiRBSK_ARATH
<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: A1A6H3
Secondary accession number(s): Q9SHH5
<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 8, 2019
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 122 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 programPlant 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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