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Q8XVD1

- HEM1_RALSO

UniProt

Q8XVD1 - HEM1_RALSO

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei54 – 541NucleophileUniRule annotation
    Sitei106 – 1061Important for activityUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation
    Binding sitei127 – 1271SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2016NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciRSOL267608:GCVU-2948-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTRUniRule annotation
    Gene namesi
    Name:hemAUniRule annotation
    Ordered Locus Names:RSc2900
    ORF Names:RS00197
    OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
    Taxonomic identifieri267608 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
    ProteomesiUP000001436: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Glutamyl-tRNA reductasePRO_0000114061Add
    BLAST

    Proteomic databases

    PRIDEiQ8XVD1.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi267608.RSc2900.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8XVD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 564Substrate bindingUniRule annotation
    Regioni121 – 1233Substrate bindingUniRule annotation

    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.UniRule annotation

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0373.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8XVD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLLTLGINH HTAPLSLREK VAFPLEQLKP ALGTLRQHLP HRKSTAEAAI    50
    LSTCNRTELY CATDGNLPED TAHEHAIRWL AHHHNIDAGE LAPHVYALGQ 100
    SQAVRHAFRV ASGLDSMVLG ETQILGQMKD AVRTATEAGA LGTYLNQLFQ 150
    RTFAVAKEVR GTTEIGAHSV SMAAAAVRLA QRIFESIAEQ RVLFIGAGEM 200
    IELCATHFAA QKPRETVVAN RTLERGEKLA EALSNQGLNA RAVRLAELPA 250
    RLGEFDIVVS CTASTLPIIG LGAVERAIKQ RRHRPMFMVD LAVPRDIEPE 300
    VARLSDVFLY TVDDLGAIVR EGNALRQAAV AQAEAIIETR VQNFMHWLDA 350
    RSVVPIIRDL HAHAEALRQG ELERAQRMLA RGDDPALVLE ALSQALTKKF 400
    LHGPTHALNH AQGEGREQLI DLLPGLFRQS SHSER 435
    Length:435
    Mass (Da):47,753
    Last modified:March 1, 2002 - v1
    Checksum:i5C65825FEA1A5638
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL646052 Genomic DNA. Translation: CAD16607.1.
    RefSeqiNP_521021.1. NC_003295.1.

    Genome annotation databases

    EnsemblBacteriaiCAD16607; CAD16607; RSc2900.
    GeneIDi1221753.
    KEGGirso:RSc2900.
    PATRICi20264535. VBIRalSol70888_2953.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL646052 Genomic DNA. Translation: CAD16607.1 .
    RefSeqi NP_521021.1. NC_003295.1.

    3D structure databases

    ProteinModelPortali Q8XVD1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267608.RSc2900.

    Proteomic databases

    PRIDEi Q8XVD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD16607 ; CAD16607 ; RSc2900 .
    GeneIDi 1221753.
    KEGGi rso:RSc2900.
    PATRICi 20264535. VBIRalSol70888_2953.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci RSOL267608:GCVU-2948-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015896. 4pyrrol_synth_GluRdtase_dimer.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF00745. GlutR_dimer. 1 hit.
    PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GMI1000.

    Entry informationi

    Entry nameiHEM1_RALSO
    AccessioniPrimary (citable) accession number: Q8XVD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3