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A6W1C3

- HEM1_MARMS

UniProt

A6W1C3 - HEM1_MARMS

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Marinomonas sp. (strain MWYL1)
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 (21 Aug 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
    Sitei98 – 981Important for activityUniRule annotation
    Binding sitei108 – 1081SubstrateUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1936NADPUniRule 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

    BioCyciMSP400668:GHKD-3669-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:Mmwyl1_3600
    OrganismiMarinomonas sp. (strain MWYL1)
    Taxonomic identifieri400668 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesMarinomonas
    ProteomesiUP000001113: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Glutamyl-tRNA reductasePRO_1000075412Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi400668.Mmwyl1_3600.

    Structurei

    3D structure databases

    ProteinModelPortaliA6W1C3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni113 – 1153Substrate 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.

    A6W1C3-1 [UniParc]FASTAAdd to Basket

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    MPLITVGINH KTAPVSIRER VAFAPEKMID ALSSLISENK ANEAVIVSTC    50
    NRTELYCSVE DLSKVDDVIA WLGKYHGIAL PELQQYCYTH ADDDSVRHVM 100
    RVASGLDSLI LGEPQILGQV KSAYAVSQEG SCIGPELESL FQRTFSVAKR 150
    VRTDTAIGEN PVSIAFAAVS LAQRIFADIR NSTALLIGAG QTIELVARHL 200
    KENGIKHIIV ANRTLARAQI LADELNAEAI MLGDIGDYLS QADIVISSTA 250
    SQLPIIGKGM VERATSQRRH SPMLLIDIAV PRDIEPEVEE VNDAYLYTVD 300
    DLHSVIEENV RARQDAAKAA EQMIEEGVDS YRRVVESRKV SDLIVTFRQS 350
    AEAIKNTELE KALKGLEMGQ SPEQVLNKLA HGLMNKLIHA PTRYLRDAGA 400
    DADQDALIIA SNVLGIYEEK DN 422
    Length:422
    Mass (Da):46,233
    Last modified:August 21, 2007 - v1
    Checksum:iC5BF7E44F1415CA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000749 Genomic DNA. Translation: ABR72502.1.
    RefSeqiWP_012071267.1. NC_009654.1.
    YP_001342437.1. NC_009654.1.

    Genome annotation databases

    EnsemblBacteriaiABR72502; ABR72502; Mmwyl1_3600.
    GeneIDi5364818.
    KEGGimmw:Mmwyl1_3600.
    PATRICi22470765. VBIMarSp124341_3727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000749 Genomic DNA. Translation: ABR72502.1 .
    RefSeqi WP_012071267.1. NC_009654.1.
    YP_001342437.1. NC_009654.1.

    3D structure databases

    ProteinModelPortali A6W1C3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 400668.Mmwyl1_3600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR72502 ; ABR72502 ; Mmwyl1_3600 .
    GeneIDi 5364818.
    KEGGi mmw:Mmwyl1_3600.
    PATRICi 22470765. VBIMarSp124341_3727.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MSP400668:GHKD-3669-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: MWYL1.

    Entry informationi

    Entry nameiHEM1_MARMS
    AccessioniPrimary (citable) accession number: A6W1C3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: August 21, 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