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A3MZC2

- HEM1_ACTP2

UniProt

A3MZC2 - HEM1_ACTP2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (03 Apr 2007)
      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 sitei50 – 501NucleophileUniRule annotation
    Sitei108 – 1081Important for activityUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi203 – 2086NADPUniRule 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

    BioCyciAPLE416269:GHV7-413-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:APL_0404
    OrganismiActinobacillus pleuropneumoniae serotype 5b (strain L20)
    Taxonomic identifieri416269 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
    ProteomesiUP000001432: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 436436Glutamyl-tRNA reductasePRO_1000004588Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi416269.APL_0404.

    Structurei

    3D structure databases

    ProteinModelPortaliA3MZC2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni123 – 1253Substrate 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.

    A3MZC2-1 [UniParc]FASTAAdd to Basket

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    MTILALGINH KTASVNLRSK VAFDDQKRQL AFEQIQHRAL AESVVILSTC    50
    NRTELYFHNA EITPREEHED NIAWREQCFE WFAEIHQLEH NELRECIYFK 100
    QNMESARHLM RVACGLDSLI LGEPQILGQV KQAYQYSENF YQSQNSHIST 150
    KLSRLFQRTF STAKRVRSET EIGSSAVSVA YAACGLARQI FDNFGKLRFL 200
    LVGAGETIEL VARYLIQHGA KNIMIANRTP QRAETLAERL NTPMQILSLS 250
    ALQIGLNQAD IVISSTGSPD MLISKEMVEI AQKQRQFDPM LLIDIAVPRD 300
    IDENAGELDA VYSYSVDDLQ HIIQRNMAQR EQAAEQAAQI VDEECKAFFE 350
    WLKQQQSSDL IKRYRQDAEQ TRQELLAKAL VALTSGQDSE KVLNELSYKL 400
    TNSLLHVPTQ ALQAMAKSGN SQGLQSFSKA LKLEEQ 436
    Length:436
    Mass (Da):49,467
    Last modified:April 3, 2007 - v1
    Checksum:i91663CBAE40792C4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000569 Genomic DNA. Translation: ABN73508.1.
    RefSeqiYP_001053113.1. NC_009053.1.

    Genome annotation databases

    EnsemblBacteriaiABN73508; ABN73508; APL_0404.
    GeneIDi4849853.
    KEGGiapl:APL_0404.
    PATRICi20745628. VBIActPle94089_0417.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000569 Genomic DNA. Translation: ABN73508.1 .
    RefSeqi YP_001053113.1. NC_009053.1.

    3D structure databases

    ProteinModelPortali A3MZC2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 416269.APL_0404.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN73508 ; ABN73508 ; APL_0404 .
    GeneIDi 4849853.
    KEGGi apl:APL_0404.
    PATRICi 20745628. VBIActPle94089_0417.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci APLE416269:GHV7-413-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. "The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
      Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
      J. Bacteriol. 190:1495-1496(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: L20.

    Entry informationi

    Entry nameiHEM1_ACTP2
    AccessioniPrimary (citable) accession number: A3MZC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 60 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