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B1YJV2

- HEM1_EXIS2

UniProt

B1YJV2 - HEM1_EXIS2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (20 May 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. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciESIB262543:GHBP-2217-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:Exig_2138
    OrganismiExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
    Taxonomic identifieri262543 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium
    ProteomesiUP000001681: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446Glutamyl-tRNA reductasePRO_1000093136Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi262543.Exig_2138.

    Structurei

    3D structure databases

    ProteinModelPortaliB1YJV2.
    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.
    OMAiLAHKLTN.
    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.

    B1YJV2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHIVVVGLNN KTAPVSIREQ VSFGEHEMKG AVVALRDEKS IFESVIVSTC    50
    NRTELYVVTD QPHTGRYYTK RFLANWFGLT MEELEPYLFI HEGFDAMKHL 100
    FRVTSGLDSM IVGETQILGQ VKTSFFTAQK LETTGTVFNK LFKEAVTLAK 150
    RAHAETGIGE NAVSVSAAAV TLAEQLLGSL EDKSIVVIGA GETGELTTLN 200
    LYEAGARDIT VFNRTLAKAE EVANRFEGSA HSINEMQCGL LRADIVISST 250
    GAKRAIIKRE DIAAAQLFRS DRPFLLIDIA VPRDIEPTAG DLPGVHLYDV 300
    DDLTSIVQQN MAERMKEAAK IERRIEAAIA EFEGWMTTLG VVPIITELRD 350
    QSLKIQQETM QSLERKLPNM TNREKTVIGK HMKSIINQLL REPLSYIKDA 400
    AAKPDAEQRI AQFMDTFALD EELFDSAAEE MVLQEETTAE RKAVNR 446
    Length:446
    Mass (Da):49,612
    Last modified:May 20, 2008 - v1
    Checksum:iE5BA8203399D6D7F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001022 Genomic DNA. Translation: ACB61590.1.
    RefSeqiYP_001814607.1. NC_010556.1.

    Genome annotation databases

    EnsemblBacteriaiACB61590; ACB61590; Exig_2138.
    GeneIDi6174318.
    KEGGiesi:Exig_2138.
    PATRICi32137902. VBIExiSib53410_2174.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001022 Genomic DNA. Translation: ACB61590.1 .
    RefSeqi YP_001814607.1. NC_010556.1.

    3D structure databases

    ProteinModelPortali B1YJV2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262543.Exig_2138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB61590 ; ACB61590 ; Exig_2138 .
    GeneIDi 6174318.
    KEGGi esi:Exig_2138.
    PATRICi 32137902. VBIExiSib53410_2174.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ESIB262543:GHBP-2217-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: DSM 17290 / JCM 13490 / 255-15.

    Entry informationi

    Entry nameiHEM1_EXIS2
    AccessioniPrimary (citable) accession number: B1YJV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 51 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