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A2SQU1

- HEM1_METLZ

UniProt

A2SQU1 - HEM1_METLZ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (06 Mar 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 sitei52 – 521NucleophileUniRule annotation
    Sitei89 – 891Important for activityUniRule annotation
    Binding sitei99 – 991SubstrateUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1846NADPUniRule 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

    BioCyciMLAB410358:GH7C-540-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:Mlab_0523
    OrganismiMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)
    Taxonomic identifieri410358 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum
    ProteomesiUP000000365: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Glutamyl-tRNA reductasePRO_0000335091Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi410358.Mlab_0523.

    Structurei

    3D structure databases

    ProteinModelPortaliA2SQU1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 544Substrate bindingUniRule annotation
    Regioni104 – 1063Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiMIICEEL.

    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A2SQU1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRTLLTDIA VATADHSKYG EEVLGLFRFK DETAFFEKAS KIFPGVVLLE    50
    TCNRVEILVH GSAKQLRDFL HGEQRFGFDI LEGEAALMHL LELAAGTKSM 100
    IIGEDQILGQ MRRALLLAES HDTNDVITDV CLNTAIREGV SIRQKTSINK 150
    GAVSIGSAAV LLAEELMGDL DGKNILVVGG GEMGTLVARA LCEKNLRAIY 200
    VTNRSFDRAV LLAEEIKGRA MRLDQLYPCI ALSDVVISCT GAPHLIIHAD 250
    ELAETMNERF WPLDLEPRHL LLIDIAQPRD IDDACRDVPG VSLKTLDDLK 300
    SISEKNLAAR KTECEHADVL VKAALPEFIK AFNRAASGDL TKNLYTWAEE 350
    IRQREKNKAL SRLRDADPYL ESVIDDLTSA LTKKLLEDAA KSIRASAECT 400
    DTQTAEILLK AIISGEVSCI RRSE 424
    Length:424
    Mass (Da):46,697
    Last modified:March 6, 2007 - v1
    Checksum:iE4D07EF8F46E4DCB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000559 Genomic DNA. Translation: ABN06697.1.
    RefSeqiWP_011832898.1. NC_008942.1.
    YP_001029964.1. NC_008942.1.

    Genome annotation databases

    EnsemblBacteriaiABN06697; ABN06697; Mlab_0523.
    GeneIDi4795403.
    KEGGimla:Mlab_0523.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000559 Genomic DNA. Translation: ABN06697.1 .
    RefSeqi WP_011832898.1. NC_008942.1.
    YP_001029964.1. NC_008942.1.

    3D structure databases

    ProteinModelPortali A2SQU1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 410358.Mlab_0523.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN06697 ; ABN06697 ; Mlab_0523 .
    GeneIDi 4795403.
    KEGGi mla:Mlab_0523.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi MIICEEL.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MLAB410358:GH7C-540-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43576 / DSM 4855 / Z.

    Entry informationi

    Entry nameiHEM1_METLZ
    AccessioniPrimary (citable) accession number: A2SQU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 64 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