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Q897K9

- HEM1_CLOTE

UniProt

Q897K9 - HEM1_CLOTE

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei46 – 461NucleophileUniRule annotation
    Sitei91 – 911Important for activityUniRule annotation
    Binding sitei101 – 1011SubstrateUniRule annotation
    Binding sitei112 – 1121SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi177 – 1826NADPUniRule 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

    BioCyciCTET212717:GJAM-654-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:CTC_00725
    OrganismiClostridium tetani (strain Massachusetts / E88)
    Taxonomic identifieri212717 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001412: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 399399Glutamyl-tRNA reductasePRO_0000114014Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi212717.CTC00725.

    Structurei

    3D structure databases

    ProteinModelPortaliQ897K9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate bindingUniRule annotation
    Regioni106 – 1083Substrate 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.
    KOiK02492.
    OMAiCINDENC.
    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.
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q897K9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIGVLGVKTE VKLDIREKLS IIPKRYESSL MKLKEKCDEV VILSTCNRTE    50
    VYYSYKKHNE NIISHIFKCL NWDENYKKYT FHYKDDEAIN HLMRVICGFD 100
    SLILGEDQIL SQIKQAYEIA LSSKSVNRDL NKLFQMAITC GKEFRNKSQL 150
    YKIPVSSASI AVNEGRKHGG KNFMVLGYGA VGSLAVKYIL SGEFDKLYIV 200
    VRNPSVVDLR DDRMTIINFN ERGKYYKDVD CIISCTSAPH VVVDAFELPK 250
    HKNIVVYDLA VPRDVDEEVR YMKNVKLYDI DNISCINDEN CSKREDIMNN 300
    NLFVIEKYER EFEKWRKTSE ISPHIVNLKK KGDEVYKKRL TTFKNKKYTK 350
    DVDALAEIML KSTSNAYINK AIEVLKEEQL KGRGEECLRI IEKIFYSAQ 399
    Length:399
    Mass (Da):46,358
    Last modified:June 1, 2003 - v1
    Checksum:iA30CEFCCD73F5738
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO35327.1.
    RefSeqiNP_781390.1. NC_004557.1.

    Genome annotation databases

    EnsemblBacteriaiAAO35327; AAO35327; CTC_00725.
    GeneIDi1058948.
    KEGGictc:CTC00725.
    PATRICi19509275. VBICloTet101274_0686.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO35327.1 .
    RefSeqi NP_781390.1. NC_004557.1.

    3D structure databases

    ProteinModelPortali Q897K9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 212717.CTC00725.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO35327 ; AAO35327 ; CTC_00725 .
    GeneIDi 1058948.
    KEGGi ctc:CTC00725.
    PATRICi 19509275. VBICloTet101274_0686.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi CINDENC.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CTET212717:GJAM-654-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 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: Massachusetts / E88.

    Entry informationi

    Entry nameiHEM1_CLOTE
    AccessioniPrimary (citable) accession number: Q897K9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 89 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