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C3N844

- HEM1_SULIY

UniProt

C3N844 - HEM1_SULIY

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (16 Jun 2009)
      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 sitei53 – 531NucleophileUniRule annotation
    Sitei100 – 1001Important for activityUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1956NADPUniRule 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

    BioCyciSISL439386:GHF0-2161-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:YG5714_2077
    OrganismiSulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1)
    Taxonomic identifieri439386 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000002308: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Glutamyl-tRNA reductasePRO_1000202647Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi439386.YG5714_2077.

    Structurei

    3D structure databases

    ProteinModelPortaliC3N844.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni115 – 1173Substrate 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.
    HOGENOMiHOG000107850.
    KOiK02492.
    OMAiYREADAN.

    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.

    C3N844-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSNEELLQN YCSILFTYKT IGISNLHLYY FRETEIKSLR QLINAEFAIL    50
    QTCNRVEIYL YSNTNTISEI NKMIQYLNNV HNEPIGNQAR VICGKDSIKH 100
    LFLVASGADS LSIGEYEILS QIRSTIDMFK KLGFSGKYLQ ILFERAIKVG 150
    RKVREETSIS KGKVGIYSLA IDEAKRQFNN FYDRKIVIVG AGEMGQKIAN 200
    MLYNEGVKNV TIMNRTVEKA KQLALKFGYN YEKLDLDKLG SFDIAFISIS 250
    HENLRLENKW NTLIVDITVP PLFTGNNVIT LEELEKISKL NFKAREEELV 300
    KINKLVEDGI DELIYDYKKE IYSEFMSKIM KRVETIRENE IVRAYKELEK 350
    LGINNQQVKE ILDLMTRSII KKSFQPLFDN VRSLVFDGEN SINYINFLID 400
    IFKDGNIPIF ETKKIKKKQI SKRSSS 426
    Length:426
    Mass (Da):49,336
    Last modified:June 16, 2009 - v1
    Checksum:i1C84F982D5E3DF96
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001403 Genomic DNA. Translation: ACP46331.1.
    RefSeqiYP_002838253.1. NC_012622.1.

    Genome annotation databases

    EnsemblBacteriaiACP46331; ACP46331; YG5714_2077.
    GeneIDi7807896.
    KEGGisiy:YG5714_2077.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001403 Genomic DNA. Translation: ACP46331.1 .
    RefSeqi YP_002838253.1. NC_012622.1.

    3D structure databases

    ProteinModelPortali C3N844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439386.YG5714_2077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACP46331 ; ACP46331 ; YG5714_2077 .
    GeneIDi 7807896.
    KEGGi siy:YG5714_2077.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000107850.
    KOi K02492.
    OMAi YREADAN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci SISL439386:GHF0-2161-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: Y.G.57.14 / Yellowstone #1.

    Entry informationi

    Entry nameiHEM1_SULIY
    AccessioniPrimary (citable) accession number: C3N844
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 43 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