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B1VEJ5

- HEM1_CORU7

UniProt

B1VEJ5 - HEM1_CORU7

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 53 (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 sitei59 – 591NucleophileUniRule annotation
    Sitei108 – 1081Important for activityUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation
    Binding sitei129 – 1291SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi205 – 2106NADPUniRule 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

    BioCyciCURE504474:GJ8Y-230-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:cu0224
    OrganismiCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
    Taxonomic identifieri504474 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000001727: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Glutamyl-tRNA reductasePRO_1000093129Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi504474.cur_0224.

    Structurei

    3D structure databases

    ProteinModelPortaliB1VEJ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 614Substrate bindingUniRule annotation
    Regioni123 – 1253Substrate 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.
    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.

    B1VEJ5-1 [UniParc]FASTAAdd to Basket

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    MAGHVHTGSA AVLLVGLSFR SAPVSLLEQV STVDTDLPKL ENALLDHDSL    50
    SEALVLSTCN RMEFYTVANA FHPGLDHIVD TIATYSGLDD SELEPHLYVH 100
    YSDAAVEHML NVASGLDSMV LGEQQIIGQL RGAYEESKGA GTVGRTLHDL 150
    TQRALRTGKR VHSETEIDSA GSSMVSFALD RALTVLGIPE ASSDALSGRR 200
    AVVIGAGAMA SLASTHLGRL GIEHVTVANR TVDRAEQLAS HAVEAGVPAR 250
    GIGLDELPAA LTGADIVVSA TGAVGTVVSA ADIKAAQQVR DGRQQVLIDL 300
    SMPRDIEQAT ADVPGVALLN IEELTGMTED TIEDEDAARG IVAEELESFL 350
    EQQRAQAVVP TVKALRQQAM DALSNEMLAL QRQTPGMSDE DREAVNRSMR 400
    RLVEKLLHTP TVQAKKLSAA GQSVSYPDAL AALFNLPTGM TQQVSAVKGA 450
    NAGSGQRKKQ KPQENRVSTA RAVYRSTYQD LTQASTPGGK DDDQ 494
    Length:494
    Mass (Da):52,334
    Last modified:May 20, 2008 - v1
    Checksum:iBB6FE258AC21C0C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM942444 Genomic DNA. Translation: CAQ04184.1.
    RefSeqiWP_012359490.1. NC_010545.1.
    YP_001799618.1. NC_010545.1.

    Genome annotation databases

    EnsemblBacteriaiCAQ04184; CAQ04184; cu0224.
    GeneIDi6186320.
    KEGGicur:cur_0224.
    PATRICi21520146. VBICorUre58120_0220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM942444 Genomic DNA. Translation: CAQ04184.1 .
    RefSeqi WP_012359490.1. NC_010545.1.
    YP_001799618.1. NC_010545.1.

    3D structure databases

    ProteinModelPortali B1VEJ5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 504474.cur_0224.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAQ04184 ; CAQ04184 ; cu0224 .
    GeneIDi 6186320.
    KEGGi cur:cur_0224.
    PATRICi 21520146. VBICorUre58120_0220.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CURE504474:GJ8Y-230-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 lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
      Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
      J. Biotechnol. 136:11-21(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43042 / DSM 7109.

    Entry informationi

    Entry nameiHEM1_CORU7
    AccessioniPrimary (citable) accession number: B1VEJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 53 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