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Entry version 172 (02 Jun 2021)
Sequence version 2 (03 Apr 2002)
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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

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 NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.

2 Publications

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA (By similarity).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 <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

Negatively regulated by FLU and heme.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: chlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu). This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei144NucleophileBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei193Important for activityBy similarity1
<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 sitei203SubstrateBy similarity1
Binding sitei214SubstrateBy 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 bindingi285 – 290NADPBy similarity6

<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

  • glutamyl-tRNA reductase activity Source: TAIR
  • NADP binding Source: InterPro

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 functionOxidoreductase
Biological processChlorophyll biosynthesis, Porphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT1G58290-MONOMER
MetaCyc:AT1G58290-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.70, 399

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

More...
UniPathwayi
UPA00251;UER00316
UPA00668

<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:
Glutamyl-tRNA reductase 1, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
<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:HEMA1
Synonyms:HEMA
Ordered Locus Names:At1g58290
ORF Names:F19C14.9
<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 1

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT1G58290

The Arabidopsis Information Resource

More...
TAIRi
locus:2016605, AT1G58290

<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, Membrane, Plastid

<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 – 61ChloroplastCuratedAdd BLAST61
<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_000001330762 – 543Glutamyl-tRNA reductase 1, chloroplasticAdd BLAST482

Proteomic databases

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

More...
PaxDbi
P42804

PRoteomics IDEntifications database

More...
PRIDEi
P42804

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
247356

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Strongly expressed in photosynthetic tissues. Detected in all tissues tested.3 Publications

<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

Circadian-regulation. Up-regulated by light.4 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P42804, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P42804, 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

<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

Part of the FLU-containing chloroplast membrane complex composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1.

Interacts (via C-terminus) with FLU, only in the absence of light.

Interacts with GLUTRBP and forms a heterotetramer of two GLUTRBP and two HEMA1 subunits.

Interacts with CLPF (PubMed:26419670).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
27423, 5 interactors

Protein interaction database and analysis system

More...
IntActi
P42804, 4 interactors

Molecular INTeraction database

More...
MINTi
P42804

STRING: functional protein association networks

More...
STRINGi
3702.AT1G58290.1

<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

1543
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
P42804

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>Regioni20 – 44DisorderedSequence analysisAdd BLAST25
Regioni143 – 146Substrate bindingBy similarity4
Regioni208 – 210Substrate bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi20 – 38Polar residuesSequence analysisAdd BLAST19

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus (65-92) is required for heme inhibition, but not for activity.1 Publication

<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 glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QQ1H, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_035113_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P42804

Identification of Orthologs from Complete Genome Data

More...
OMAi
FAFKCAA

Database of Orthologous Groups

More...
OrthoDBi
571265at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P42804

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.460.30, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00087, Glu_tRNA_reductase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000343, 4pyrrol_synth_GluRdtase
IPR015896, 4pyrrol_synth_GluRdtase_dimer
IPR015895, 4pyrrol_synth_GluRdtase_N
IPR018214, GluRdtase_CS
IPR036453, GluRdtase_dimer_dom_sf
IPR036343, GluRdtase_N_sf
IPR036291, NAD(P)-bd_dom_sf
IPR006151, Shikm_DH/Glu-tRNA_Rdtase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00745, GlutR_dimer, 1 hit
PF05201, GlutR_N, 1 hit
PF01488, Shikimate_DH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit
SSF69075, SSF69075, 1 hit
SSF69742, SSF69742, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01035, hemA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00747, GLUTR, 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.

<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.

P42804-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR
60 70 80 90 100
TRRGLIQKAR CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI
110 120 130 140 150
GLSIHTAPVE MREKLAIPEA EWPRAIAELC GLNHIEEAAV LSTCNRMEIY
160 170 180 190 200
VLALSQHRGV KEVTEWMSKT SGIPVSEICQ HRFLLYNKDA TQHIFEVSAG
210 220 230 240 250
LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI TVGKRVRTET
260 270 280 290 300
NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK
310 320 330 340 350
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA
360 370 380 390 400
SETPLFLKEH VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN
410 420 430 440 450
VDDLKEVVAA NKEDRMRKAM EAQTIITEES TQFEAWRDSL ETVPTIKKLR
460 470 480 490 500
AYAERIRVAE LEKCMSKMGD DINKKTTRAV DDLSRGIVNR FLHGPMQHLR
510 520 530 540
CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ QQK
Length:543
Mass (Da):59,515
Last modified:April 3, 2002 - 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:i04A095FEC96CC014
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 conflicti62E → V in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti169K → N in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti291K → L in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti443V → G in BAE98482 (Ref. 5) Curated1
Sequence conflicti542Q → H in AAA19118 (PubMed:7908550).Curated1

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
U03774 Genomic DNA Translation: AAA19118.1
AC008051 Genomic DNA Translation: AAF82258.1
CP002684 Genomic DNA Translation: AEE33532.1
AY072223 mRNA Translation: AAL60044.1
AY096600 mRNA Translation: AAM20250.1
AK226332 mRNA Translation: BAE98482.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E96616

NCBI Reference Sequences

More...
RefSeqi
NP_176125.1, NM_104609.4

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT1G58290.1; AT1G58290.1; AT1G58290

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
842198

Gramene; a comparative resource for plants

More...
Gramenei
AT1G58290.1; AT1G58290.1; AT1G58290

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G58290

<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
U03774 Genomic DNA Translation: AAA19118.1
AC008051 Genomic DNA Translation: AAF82258.1
CP002684 Genomic DNA Translation: AEE33532.1
AY072223 mRNA Translation: AAL60044.1
AY096600 mRNA Translation: AAM20250.1
AK226332 mRNA Translation: BAE98482.1
PIRiE96616
RefSeqiNP_176125.1, NM_104609.4

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
4N7RX-ray2.80A/B73-543[»]
4YVQX-ray2.40A440-543[»]
5CHEX-ray3.20A/B73-543[»]
5YJLX-ray2.70A/B73-543[»]
SMRiP42804
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi27423, 5 interactors
IntActiP42804, 4 interactors
MINTiP42804
STRINGi3702.AT1G58290.1

Proteomic databases

PaxDbiP42804
PRIDEiP42804
ProteomicsDBi247356

Genome annotation databases

EnsemblPlantsiAT1G58290.1; AT1G58290.1; AT1G58290
GeneIDi842198
GrameneiAT1G58290.1; AT1G58290.1; AT1G58290
KEGGiath:AT1G58290

Organism-specific databases

AraportiAT1G58290
TAIRilocus:2016605, AT1G58290

Phylogenomic databases

eggNOGiENOG502QQ1H, Eukaryota
HOGENOMiCLU_035113_2_1_1
InParanoidiP42804
OMAiFAFKCAA
OrthoDBi571265at2759
PhylomeDBiP42804

Enzyme and pathway databases

UniPathwayiUPA00251;UER00316
UPA00668
BioCyciARA:AT1G58290-MONOMER
MetaCyc:AT1G58290-MONOMER
BRENDAi1.2.1.70, 399

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P42804

Gene expression databases

ExpressionAtlasiP42804, baseline and differential
GenevisibleiP42804, AT

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087, Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343, 4pyrrol_synth_GluRdtase
IPR015896, 4pyrrol_synth_GluRdtase_dimer
IPR015895, 4pyrrol_synth_GluRdtase_N
IPR018214, GluRdtase_CS
IPR036453, GluRdtase_dimer_dom_sf
IPR036343, GluRdtase_N_sf
IPR036291, NAD(P)-bd_dom_sf
IPR006151, Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF00745, GlutR_dimer, 1 hit
PF05201, GlutR_N, 1 hit
PF01488, Shikimate_DH, 1 hit
SUPFAMiSSF51735, SSF51735, 1 hit
SSF69075, SSF69075, 1 hit
SSF69742, SSF69742, 1 hit
TIGRFAMsiTIGR01035, hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747, GLUTR, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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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 nameiHEM11_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: P42804
Secondary accession number(s): Q0WWL6, Q9LQB9
<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: November 1, 1995
Last sequence update: April 3, 2002
Last modified: June 2, 2021
This is version 172 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. 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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