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B5YJZ3

- HEM1_THEYD

UniProt

B5YJZ3 - HEM1_THEYD

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
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 (25 Nov 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 sitei51 – 511NucleophileUniRule annotation
    Sitei106 – 1061Important for activityUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation
    Binding sitei127 – 1271SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2016NADPUniRule 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

    BioCyciTYEL289376:GH9L-714-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:THEYE_A0716
    OrganismiThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
    Taxonomic identifieri289376 [NCBI]
    Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio
    ProteomesiUP000000718: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Glutamyl-tRNA reductasePRO_1000093176Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi289376.THEYE_A0716.

    Structurei

    3D structure databases

    ProteinModelPortaliB5YJZ3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni121 – 1233Substrate 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.
    OMAiLNKQFET.
    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.

    B5YJZ3-1 [UniParc]FASTAAdd to Basket

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    MSLIVIGLNH KTAPVEIREK IAFNSKEAIK EALKELIQRE GIGEVVIIST    50
    CNRVEIYVYT ANVSDLKREN QVEETIKAFL SNFHNIEIGE FENYLYVYKD 100
    TEAVEHLFKV ASSLDSMIVG EPQITGQVKE SYEIALSERT TSLILNYLMN 150
    RALFTAKRVR NETRIGENPV SVSYAAVGLI KKVFDELSKK SILLVGAGEM 200
    AELALRHLIG SGIKNVYLTN RTFQRAEEIA KEFNGVAVPF GNLKEQLVKT 250
    DIVICSTGAP HYVITEQMLK EVMPLRKHKP IFFIDISVPR NVDPACNELD 300
    NVYLYNIDDL QDVVDSNILE RKKEAEKALS IVQEETEKFF QWLNSLESVP 350
    VIVSIRNKAE QVRQEEIEKF KAKYKDLPPE LINSIDYLTQ SIINKIMHSP 400
    TVALKNNCEN KEILIFSARR LFGLDSEEE 429
    Length:429
    Mass (Da):48,820
    Last modified:November 25, 2008 - v1
    Checksum:iBEF10E3F580CE867
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI21817.1.
    RefSeqiWP_012546522.1. NC_011296.1.
    YP_002248558.1. NC_011296.1.

    Genome annotation databases

    EnsemblBacteriaiACI21817; ACI21817; THEYE_A0716.
    GeneIDi6941976.
    KEGGitye:THEYE_A0716.
    PATRICi23908453. VBITheYel104483_0708.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001147 Genomic DNA. Translation: ACI21817.1 .
    RefSeqi WP_012546522.1. NC_011296.1.
    YP_002248558.1. NC_011296.1.

    3D structure databases

    ProteinModelPortali B5YJZ3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 289376.THEYE_A0716.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI21817 ; ACI21817 ; THEYE_A0716 .
    GeneIDi 6941976.
    KEGGi tye:THEYE_A0716.
    PATRICi 23908453. VBITheYel104483_0708.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TYEL289376:GH9L-714-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. "The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
      Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51303 / DSM 11347 / YP87.

    Entry informationi

    Entry nameiHEM1_THEYD
    AccessioniPrimary (citable) accession number: B5YJZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: November 25, 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