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Entry version 130 (02 Dec 2020)
Sequence version 1 (29 Mar 2005)
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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli (strain K12)
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). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.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.

<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

Activated by Mg2+ ions. Inhibited by metal-chelating agents such as EDTA, EGTA, 1,10-phenanthroline, 2,2'-dipyridyl, and by PtCl4 and KPdCl4 as well as Ni2+ and Co2+. Also inhibited by iodoacetamide, N-tosyl-L-phenylalanine chloromethyl ketone, and 5,5'-dithiobis(2-nitrobenzoic acid), as well as glutamycin.1 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

  1. KM=24 µM for L-glutamyl-tRNA(Glu)1 Publication
  2. KM=39 µM for NADPH1 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: protoporphyrin-IX biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
    2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
    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 sitei50Nucleophile1
    <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>Sitei99Important for activity1
    <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 sitei109SubstrateCurated1
    Binding sitei120SubstrateBy 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 bindingi189 – 194NADPCurated6

    <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 functionOxidoreductase
    Biological processPorphyrin biosynthesis
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GLUTRNAREDUCT-MONOMER
    MetaCyc:GLUTRNAREDUCT-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.1.70, 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0A6X1

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

    More...
    UniPathwayi
    UPA00251;UER00316

    <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 (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:hemA
    Ordered Locus Names:b1210, JW1201
    <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>OrganismiEscherichia coli (strain K12)
    <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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <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
    • UP000000318 <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
    • UP000000625 Componenti: Chromosome

    <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>Mutagenesisi7G → D: Loss of activity. 1 Publication1
    Mutagenesisi49T → V: 10% and 5% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi50C → S: Loss of activity. 1 Publication1
    Mutagenesisi52R → K: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi52R → Q: Loss of activity. 1 Publication1
    Mutagenesisi54E → K: 6% and 2% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi74C → S: No effect. 1 Publication1
    Mutagenesisi99H → N: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi106G → N: Loss of activity. 1 Publication1
    Mutagenesisi109S → A: 28% and 25% of wild-type reductase and esterase activity, respectively. 1 Publication1
    Mutagenesisi114E → K: Loss of activity. 1 Publication1
    Mutagenesisi116Q → L: Loss of reductase activity. 30% of wild-type esterase activity. 1 Publication1
    Mutagenesisi145S → F: Loss of activity. 1 Publication1
    Mutagenesisi170C → S: No effect. 1 Publication1
    Mutagenesisi191G → D: Loss of reductase activity. Retains esterase activity. 1 Publication1
    Mutagenesisi314R → C: Loss of activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3309013

    <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_00001140231 – 418Glutamyl-tRNA reductaseAdd BLAST418

    Proteomic databases

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

    More...
    PaxDbi
    P0A6X1

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A6X1

    <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.

    Interacts with glutamate-1-semialdehyde 2,1-aminomutase (GSA-AM), which forms a metabolic channeling between both enzymes to protect the reactive aldehyde species GSA.

    2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    Database of interacting proteins

    More...
    DIPi
    DIP-9877N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A6X1, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1210

    <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
    P0A6X1

    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>Regioni49 – 52Substrate bindingCurated4
    Regioni114 – 116Substrate bindingCurated3

    <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

    Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization (By similarity).By similarity

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0373, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_035113_2_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A6X1

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A6X1

    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

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000445, 4pyrrol_synth_GluRdtase, 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.

    P0A6X1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC
    60 70 80 90 100
    NRTELYLSVE EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL
    110 120 130 140 150
    MRVASGLDSL VLGEPQILGQ VKKAFADSQK GHMKASELER MFQKSFSVAK
    160 170 180 190 200
    RVRTETDIGA SAVSVAFAAC TLARQIFESL STVTVLLVGA GETIELVARH
    210 220 230 240 250
    LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSDIDERL READIIISST
    260 270 280 290 300
    ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
    310 320 330 340 350
    DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS
    360 370 380 390 400
    QAEQVRDELT AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA
    410
    RDGDNERLNI LRDSLGLE
    Length:418
    Mass (Da):46,307
    Last modified:March 29, 2005 - 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:i3CEE59AC53610A88
    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 conflicti151 – 168RVRTE…SVAFA → PFALKQISVPALCLSLLP in CAA35476 (PubMed:2664455).CuratedAdd BLAST18
    Sequence conflicti172L → V in CAA35476 (PubMed:2664455).Curated1
    Sequence conflicti240L → M in CAA35476 (PubMed:2664455).Curated1
    Sequence conflicti243A → R (PubMed:2684779).Curated1
    Sequence conflicti243A → R (PubMed:7543480).Curated1
    Sequence conflicti365A → R in CAA35476 (PubMed:2664455).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
    M30785 Genomic DNA Translation: AAA23953.1
    M25323 Genomic DNA Translation: AAA23954.1
    X17434 Genomic DNA Translation: CAA35476.1
    U18555 Genomic DNA Translation: AAC43436.1
    U00096 Genomic DNA Translation: AAC74294.1
    AP009048 Genomic DNA Translation: BAA36068.1
    D10264 Genomic DNA Translation: BAA20969.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A45918, BVECHA

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_415728.1, NC_000913.3
    WP_001299679.1, NZ_SSZK01000010.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74294; AAC74294; b1210
    BAA36068; BAA36068; BAA36068

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    945777

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1201
    eco:b1210

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1074

    <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
    M30785 Genomic DNA Translation: AAA23953.1
    M25323 Genomic DNA Translation: AAA23954.1
    X17434 Genomic DNA Translation: CAA35476.1
    U18555 Genomic DNA Translation: AAC43436.1
    U00096 Genomic DNA Translation: AAC74294.1
    AP009048 Genomic DNA Translation: BAA36068.1
    D10264 Genomic DNA Translation: BAA20969.1
    PIRiA45918, BVECHA
    RefSeqiNP_415728.1, NC_000913.3
    WP_001299679.1, NZ_SSZK01000010.1

    3D structure databases

    SMRiP0A6X1
    ModBaseiSearch...

    Protein-protein interaction databases

    DIPiDIP-9877N
    IntActiP0A6X1, 1 interactor
    STRINGi511145.b1210

    Chemistry databases

    ChEMBLiCHEMBL3309013

    Proteomic databases

    PaxDbiP0A6X1
    PRIDEiP0A6X1

    Genome annotation databases

    EnsemblBacteriaiAAC74294; AAC74294; b1210
    BAA36068; BAA36068; BAA36068
    GeneIDi945777
    KEGGiecj:JW1201
    eco:b1210
    PATRICifig|1411691.4.peg.1074

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0422

    Phylogenomic databases

    eggNOGiCOG0373, Bacteria
    HOGENOMiCLU_035113_2_2_6
    InParanoidiP0A6X1
    PhylomeDBiP0A6X1

    Enzyme and pathway databases

    UniPathwayiUPA00251;UER00316
    BioCyciEcoCyc:GLUTRNAREDUCT-MONOMER
    MetaCyc:GLUTRNAREDUCT-MONOMER
    BRENDAi1.2.1.70, 2026
    SABIO-RKiP0A6X1

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0A6X1

    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
    PIRSFiPIRSF000445, 4pyrrol_synth_GluRdtase, 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

    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 nameiHEM1_ECOLI
    <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: P0A6X1
    Secondary accession number(s): P13580, Q59405
    <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: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: December 2, 2020
    This is version 130 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

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

    Keywords - Technical termi

    Direct protein sequencing, Reference proteome

    Documents

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