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B3QWI0

- HEM1_CHLT3

UniProt

B3QWI0 - HEM1_CHLT3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (02 Sep 2008)
      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
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciCTHA517418:GHTO-2331-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    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:Ctha_2289
    OrganismiChloroherpeton thalassium (strain ATCC 35110 / GB-78)
    Taxonomic identifieri517418 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton
    ProteomesiUP000001208: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 437437Glutamyl-tRNA reductasePRO_1000093125Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi517418.Ctha_2289.

    Structurei

    3D structure databases

    ProteinModelPortaliB3QWI0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni114 – 1163Substrate 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.
    OMAiHVEILPP.
    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.

    B3QWI0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLIAVGVNH NTAPIELREK ISLTDSMARS LLTELIDSKL ASEALVLSTC    50
    NRTELYVVPA MPEVTANYLK DYLIAHKGVR KEVTRDHFFN YFACGAARHF 100
    YNVACAIDSL ILGEVQIIGQ VKTAYNRAVE MKTVGPILNK MCHTGFGLAN 150
    RVRSKTKLTA GAVSVSYAAV ELTQKIYSDV STKNILLVGA GDTAKLAAKN 200
    LLDKRVRDFY ITNRTYEKAE LLAQELGTGK ILPLEEMTER LHEFDIVVTA 250
    VGGNDHIIKK EHVAAAMQKR HRDPILILDL GLPRNVAPEV GQVNNVFLKD 300
    IDDLKMIIDS NLEKRRAEIP KVKHFIQKEL IEYARWYFSL EVKPTIVDLQ 350
    EKFFEIKALE LARIKNKVSA EEYERMEQLS DRIIKKLLHF PITTLKQQTA 400
    DTTDPVSFIR NIFDLKEQEE EFPGLTFPIN LKEQNNN 437
    Length:437
    Mass (Da):49,497
    Last modified:September 2, 2008 - v1
    Checksum:i20C5230775AC0FBB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001100 Genomic DNA. Translation: ACF14740.1.
    RefSeqiYP_001997187.1. NC_011026.1.

    Genome annotation databases

    EnsemblBacteriaiACF14740; ACF14740; Ctha_2289.
    GeneIDi6423371.
    KEGGicts:Ctha_2289.
    PATRICi21433767. VBIChlTha99257_2675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001100 Genomic DNA. Translation: ACF14740.1 .
    RefSeqi YP_001997187.1. NC_011026.1.

    3D structure databases

    ProteinModelPortali B3QWI0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 517418.Ctha_2289.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACF14740 ; ACF14740 ; Ctha_2289 .
    GeneIDi 6423371.
    KEGGi cts:Ctha_2289.
    PATRICi 21433767. VBIChlTha99257_2675.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi HVEILPP.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci CTHA517418:GHTO-2331-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. "Complete sequence of Chloroherpeton thalassium ATCC 35110."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F.
      , Overmann J., Bryant D.A., Richardson P.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35110 / GB-78.

    Entry informationi

    Entry nameiHEM1_CHLT3
    AccessioniPrimary (citable) accession number: B3QWI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 48 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