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A3MFT3

- HEM1_BURM7

UniProt

A3MFT3 - HEM1_BURM7

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Burkholderia mallei (strain NCTC 10247)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (03 Apr 2007)
      Previous versions | rss
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    • Comment

    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 sitei58 – 581NucleophileUniRule 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

    BioCyciBMAL320389:GH97-5461-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:BMA10247_A1942
    OrganismiBurkholderia mallei (strain NCTC 10247)
    Taxonomic identifieri320389 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002284: Chromosome II

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Glutamyl-tRNA reductasePRO_0000335014Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi320389.BMA10247_A1942.

    Structurei

    3D structure databases

    ProteinModelPortaliA3MFT3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 604Substrate 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.
    OMAiHEVTGEY.
    OrthoDBiEOG6C2WN5.

    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.

    A3MFT3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDMQLLTIGI NHHTAPVALR ERVAFPLEQI KPALSTFKSV FLGHPAPNAP    50
    EAAILSTCNR TELYCATNDR AARDAAIRWM SDYHRIPADE LAPHVYALPQ 100
    SEAVRHAFRV ASGLDSMVLG ETQILGQMKN AVRTASEAGS LGTYLNQLFQ 150
    RTFAVAKEVR GTTEIGAQSV SMAAAAVRLA QRIFEQVAQQ RVLFIGAGEM 200
    IELCATHFAA QGPRELVVAN RTAERGAKLA ERFGGRAMPL ADLPARMHEF 250
    DIIVSCTAST LPIIGLGAVE RAVKARRHRP IFMVDLAVPR DIEPEVGKLK 300
    DVFLYTVDDL GAIVREGNAS RQAAVAQAEA IIETRVQNFM QWLDARSIVP 350
    VIRHMHTQAD ALRRAEVERA RKMLARGDDP DAVLDALSQA LTNKLIHGPT 400
    SALNRANGAD RDSLIDLMRG FYQHAPRSSD TSDR 434
    Length:434
    Mass (Da):47,546
    Last modified:April 3, 2007 - v1
    Checksum:iD9DC915D8233453A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000547 Genomic DNA. Translation: ABO03720.1.
    RefSeqiYP_001079119.1. NC_009079.1.

    Genome annotation databases

    EnsemblBacteriaiABO03720; ABO03720; BMA10247_A1942.
    GeneIDi4889654.
    KEGGibmn:BMA10247_A1942.
    PATRICi19141485. VBIBurMal96640_1812.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000547 Genomic DNA. Translation: ABO03720.1 .
    RefSeqi YP_001079119.1. NC_009079.1.

    3D structure databases

    ProteinModelPortali A3MFT3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 320389.BMA10247_A1942.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO03720 ; ABO03720 ; BMA10247_A1942 .
    GeneIDi 4889654.
    KEGGi bmn:BMA10247_A1942.
    PATRICi 19141485. VBIBurMal96640_1812.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi HEVTGEY.
    OrthoDBi EOG6C2WN5.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci BMAL320389:GH97-5461-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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10247.

    Entry informationi

    Entry nameiHEM1_BURM7
    AccessioniPrimary (citable) accession number: A3MFT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 62 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

    Documents

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

    External Data

    Dasty 3