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Entry version 132 (22 Apr 2020)
Sequence version 2 (22 Sep 2009)
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Protein

Imidazoleglycerol-phosphate dehydratase 2, chloroplastic

Gene

HISN5B

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

<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

Mn2+2 PublicationsNote: Binds 2 manganese ions per subunit (PubMed:26095028, PubMed:27717128). Substrate binding triggers a switch in the coordination state of the Mn2+ active site between six- and five-coordinate species; this switch is critical to prime the active site for catalysis, by facilitating the formation of a high-energy imidazolate intermediate (PubMed:26095028).2 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

Weakly inihibited by inorganic phosphate (Pi) (PubMed:26095028). Competitive inhibition by 2-hydroxy-3-(1,2,4-triazol-1-yl) (e.g. C348), a potential herbicide (PubMed:27717128).2 Publications

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

This protein is involved in step 6 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase 2, chloroplastic (HISN1B), ATP phosphoribosyltransferase 1, chloroplastic (HISN1A)
  2. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  3. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic (At2g36230), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic, 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic (AXX17_At2g32880), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic (HISN3)
  5. Imidazole glycerol phosphate synthase hisHF, chloroplastic (HISN4), Imidazole glycerol phosphate synthase hisHF (AXX17_At4g31050)
  6. Imidazoleglycerol-phosphate dehydratase 2, chloroplastic (HISN5B), Imidazoleglycerol-phosphate dehydratase (AXX17_At4g17260), Imidazoleglycerol-phosphate dehydratase (HISN5B), Imidazoleglycerol-phosphate dehydratase (At3g22425), Imidazoleglycerol-phosphate dehydratase (AXX17_At3g24180), Imidazoleglycerol-phosphate dehydratase 1, chloroplastic (HISN5A), Imidazoleglycerol-phosphate dehydratase (AXX17_At4g17260), Imidazoleglycerol-phosphate dehydratase (HISN5B)
  7. Histidinol-phosphate aminotransferase 2, chloroplastic (HISN6B), Histidinol-phosphate aminotransferase 1, chloroplastic (HISN6A)
  8. Bifunctional phosphatase IMPL2, chloroplastic (HISN7)
  9. Histidinol dehydrogenase, chloroplastic (AXX17_At5g63470), Histidinol dehydrogenase, chloroplastic (HISN8)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei86SubstrateCombined sources1 Publication1
<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 bindingi112Manganese 1; via tele nitrogenCombined sources2 Publications1
Metal bindingi138Manganese 2; via tele nitrogenCombined sources2 Publications1
Metal bindingi139Manganese 1; via tele nitrogenCombined sources2 Publications1
Metal bindingi142Manganese 2Combined sources2 Publications1
Binding sitei164SubstrateCombined sources2 Publications1
Binding sitei186SubstrateCombined sources2 Publications1
Metal bindingi210Manganese 2; via tele nitrogenCombined sources2 Publications1
Metal bindingi234Manganese 1; via tele nitrogenCombined sources2 Publications1
Metal bindingi235Manganese 2; via tele nitrogenCombined sources2 Publications1
Metal bindingi238Manganese 1Combined sources2 Publications1

<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 functionLyase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandManganese, Metal-binding

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00031;UER00011

<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:
Imidazoleglycerol-phosphate dehydratase 2, chloroplastic1 Publication (EC:4.2.1.191 Publication)
Short name:
IGPD 21 Publication
Alternative name(s):
Protein HISTIDINE BIOSYNTHESIS 5B1 Publication
<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:HISN5B1 Publication
Ordered Locus Names:At4g14910Imported
ORF Names:dl3495cImported
<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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G14910

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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

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>Mutagenesisi73E → Q: Loss of activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 52ChloroplastSequence analysisAdd BLAST52
<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_000015825453 – 272Imidazoleglycerol-phosphate dehydratase 2, chloroplasticAdd BLAST220

Proteomic databases

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

More...
PaxDbi
O23346

PRoteomics IDEntifications database

More...
PRIDEi
O23346

<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
O23346 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O23346 AT

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
12446, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-61567N

STRING: functional protein association networks

More...
STRINGi
3702.AT4G14910.2

<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

1272
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
O23346

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>Regioni112 – 120Substrate bindingCombined sources2 Publications9
Regioni138 – 142Substrate bindingCombined sources2 Publications5
Regioni234 – 242Substrate bindingCombined sources2 Publications9
Regioni264 – 266Substrate bindingCombined sources2 Publications3

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3143 Eukaryota
COG0131 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_044308_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O23346

KEGG Orthology (KO)

More...
KOi
K01693

Identification of Orthologs from Complete Genome Data

More...
OMAi
ARHGLFD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O23346

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07914 IGPD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.40, 2 hits

HAMAP database of protein families

More...
HAMAPi
MF_00076 HisB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038494 IGPD_sf
IPR000807 ImidazoleglycerolP_deHydtase
IPR020565 ImidazoleglycerP_deHydtase_CS
IPR020568 Ribosomal_S5_D2-typ_fold

The PANTHER Classification System

More...
PANTHERi
PTHR23133 PTHR23133, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00475 IGPD, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00954 IGP_DEHYDRATASE_1, 1 hit
PS00955 IGP_DEHYDRATASE_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 describes 1 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. According to EST sequences.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O23346-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MELLSSSPAQ LLRPNLSSRA LLPPRTSIAS SHPPPPRFLV MNSQSQHRPS
60 70 80 90 100
ISCASPPPGD NGFPAITTAS PIESARIGEV KRETKETNVS VKINLDGHGV
110 120 130 140 150
SDSSTGIPFL DHMLDQLASH GLFDVHVRAT GDTHIDDHHT NEDVALAIGT
160 170 180 190 200
ALLKALGERK GINRFGDFTA PLDEALIHVS LDLSGRPYLG YNLEIPTQRV
210 220 230 240 250
GTYDTQLVEH FFQSLVNTSG MTLHIRQLAG KNSHHIIEAT FKAFARALRQ
260 270
ATESDPRRGG TIPSSKGVLS RS
Length:272
Mass (Da):29,424
Last modified:September 22, 2009 - 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:i1A2EA7E3D2A5B9B0
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MQQ8A8MQQ8_ARATH
Imidazoleglycerol-phosphate dehydra...
HISN5B HISTIDINE BIOSYNTHESIS 5B, At4g14910, Dl3495c, FCAALL.36
308Annotation score:

Annotation score:2 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>
F4JIH9F4JIH9_ARATH
Imidazoleglycerol-phosphate dehydra...
HISN5B HISTIDINE BIOSYNTHESIS 5B, At4g14910, Dl3495c, FCAALL.36
282Annotation score:

Annotation score:2 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 CAB10270 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB78533 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z97337 Genomic DNA Translation: CAB10270.1 Sequence problems.
AL161540 Genomic DNA Translation: CAB78533.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE83520.1
AY048237 mRNA Translation: AAK82500.1
AY094021 mRNA Translation: AAM16177.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D71412

NCBI Reference Sequences

More...
RefSeqi
NP_567448.1, NM_117577.4 [O23346-1]

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT4G14910.1; AT4G14910.1; AT4G14910 [O23346-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
827149

Gramene; a comparative resource for plants

More...
Gramenei
AT4G14910.1; AT4G14910.1; AT4G14910 [O23346-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT4G14910

Keywords - Coding sequence diversityi

Alternative splicing

<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
Z97337 Genomic DNA Translation: CAB10270.1 Sequence problems.
AL161540 Genomic DNA Translation: CAB78533.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE83520.1
AY048237 mRNA Translation: AAK82500.1
AY094021 mRNA Translation: AAM16177.1
PIRiD71412
RefSeqiNP_567448.1, NM_117577.4 [O23346-1]

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
4MU0X-ray1.30A69-272[»]
4MU1X-ray1.50A54-272[»]
4MU3X-ray1.12A69-272[»]
4MU4X-ray1.41A69-272[»]
4QNJX-ray1.30A69-272[»]
4QNKX-ray1.75A/B/C/D/E/F/G/H70-272[»]
5EKWX-ray1.10A69-272[»]
5EL9X-ray1.10A69-272[»]
5ELWX-ray1.40A69-272[»]
6EZJelectron microscopy3.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X69-272[»]
SMRiO23346
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi12446, 1 interactor
DIPiDIP-61567N
STRINGi3702.AT4G14910.2

Proteomic databases

PaxDbiO23346
PRIDEiO23346

Genome annotation databases

EnsemblPlantsiAT4G14910.1; AT4G14910.1; AT4G14910 [O23346-1]
GeneIDi827149
GrameneiAT4G14910.1; AT4G14910.1; AT4G14910 [O23346-1]
KEGGiath:AT4G14910

Organism-specific databases

AraportiAT4G14910

Phylogenomic databases

eggNOGiKOG3143 Eukaryota
COG0131 LUCA
HOGENOMiCLU_044308_1_1_1
InParanoidiO23346
KOiK01693
OMAiARHGLFD
PhylomeDBiO23346

Enzyme and pathway databases

UniPathwayiUPA00031;UER00011

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O23346

Gene expression databases

ExpressionAtlasiO23346 baseline and differential
GenevisibleiO23346 AT

Family and domain databases

CDDicd07914 IGPD, 1 hit
Gene3Di3.30.230.40, 2 hits
HAMAPiMF_00076 HisB, 1 hit
InterProiView protein in InterPro
IPR038494 IGPD_sf
IPR000807 ImidazoleglycerolP_deHydtase
IPR020565 ImidazoleglycerP_deHydtase_CS
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR23133 PTHR23133, 1 hit
PfamiView protein in Pfam
PF00475 IGPD, 1 hit
SUPFAMiSSF54211 SSF54211, 2 hits
PROSITEiView protein in PROSITE
PS00954 IGP_DEHYDRATASE_1, 1 hit
PS00955 IGP_DEHYDRATASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiHIS5B_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: O23346
Secondary accession number(s): Q94AE6
<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: January 23, 2002
Last sequence update: September 22, 2009
Last modified: April 22, 2020
This is version 132 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 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. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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