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B9DND0

- HEM1_STACT

UniProt

B9DND0 - HEM1_STACT

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Staphylococcus carnosus (strain TM300)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (24 Mar 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 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. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciSCAR396513:GJ9G-1289-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:Sca_1278
    OrganismiStaphylococcus carnosus (strain TM300)
    Taxonomic identifieri396513 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000444: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Glutamyl-tRNA reductasePRO_1000190541Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi396513.Sca_1278.

    Structurei

    3D structure databases

    ProteinModelPortaliB9DND0.
    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.
    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.

    B9DND0-1 [UniParc]FASTAAdd to Basket

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    MHIIAISINH RTADVALREK VAFKADAIRE SHLDLFETKS ILENVILSTC    50
    NRTEVYAVAD QIHTGRYYIQ RFLARKFGLE VDEIKEMSEV FVGDEAVEHI 100
    FRVTAGLDSI VLGETQILGQ MRDAFFIAQE EGTTGTIFNH LFKQAITFAK 150
    RAHHETDIAD NAVSVSYAAV ELAKKVFGNL KSKHAVIVGA GEMSELSLLN 200
    LLGAGIDNIT VVNRTKERAQ QLAEKHQTQY ADLSNLNELL VNADIVISST 250
    SAQNYVITQE MMNNVLDQRR HEPMVLIDIA VPRDIDPAIE LDMNVFSYDI 300
    DDLKGLVDAN LRERQAAADQ IAEQIPAEIN EHNDWVNMLG VVPVIRALRE 350
    KAMHIQQDTM DSIDRKLPDL SERERKVISK HTKSIINQML KDPIKQAKEL 400
    SNDKNSSEKL ELFQNIFDIE AESEYKKSLA KKERKLSARH ILGFE 445
    Length:445
    Mass (Da):50,269
    Last modified:March 24, 2009 - v1
    Checksum:iAF252B5A23497BF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM295250 Genomic DNA. Translation: CAL28184.1.
    RefSeqiWP_015900524.1. NC_012121.1.
    YP_002634369.1. NC_012121.1.

    Genome annotation databases

    GeneIDi7551686.
    KEGGisca:Sca_1278.
    PATRICi19603326. VBIStaCar105558_1277.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM295250 Genomic DNA. Translation: CAL28184.1 .
    RefSeqi WP_015900524.1. NC_012121.1.
    YP_002634369.1. NC_012121.1.

    3D structure databases

    ProteinModelPortali B9DND0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 396513.Sca_1278.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7551686.
    KEGGi sca:Sca_1278.
    PATRICi 19603326. VBIStaCar105558_1277.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci SCAR396513:GJ9G-1289-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. "Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
      Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F.
      Appl. Environ. Microbiol. 75:811-822(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TM300.

    Entry informationi

    Entry nameiHEM1_STACT
    AccessioniPrimary (citable) accession number: B9DND0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 47 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