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A0QR17

- HEM1_MYCS2

UniProt

A0QR17 - HEM1_MYCS2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      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 bindingi190 – 1956NADPUniRule 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

    BioCyciMSME246196:GJ4Y-952-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:MSMEG_0952, MSMEI_0927
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Glutamyl-tRNA reductasePRO_1000004647Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi246196.MSMEG_0952.

    Structurei

    3D structure databases

    ProteinModelPortaliA0QR17.
    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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiAITCGKK.
    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.

    A0QR17-1 [UniParc]FASTAAdd to Basket

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    MSVLLFGVSH RSAPVSVLEQ LSTNEAEQAK IIDQVLQSSL VTEAMVLSTC    50
    NRVEVYAVVE AFHGGLSVIG QVLAERSGMS LNDLTKYAYV RYAEAAVEHL 100
    FAVTSGLDSA VIGEQQVLGQ VRRAYATAEA NRTVGRTLHE LAQRALSVGK 150
    RVHSETGIDA AGASVVSVAL GMAETKLSGG LGGRTAAVVG AGAMGALAGA 200
    HLVRAGIERV HVVNRSLPRA ERLAKNLTEQ GVVADAVGLD DIARALVDAD 250
    VVLSSTGAVR PVVSLADVHY ALAQRTLAGA EHQMVVCDLG MPRDVDPAVS 300
    GLPGVWVVDM DRIQREPSAR AAAVDAEAAR NIVAAEVANY LAGQRMAEVT 350
    PTVTALRQRA ADVVEAELLR LDNRLPGLDA AHRDEVAKTV RRVVDKLLHA 400
    PTVRVKQLAS APGGDSYAEA LRELFELDPQ AVEAVAASEL PLITTDLDKT 450
    E 451
    Length:451
    Mass (Da):47,445
    Last modified:January 9, 2007 - v1
    Checksum:iDC09641545698C43
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71005.1.
    CP001663 Genomic DNA. Translation: AFP37407.1.
    RefSeqiWP_011727309.1. NC_018289.1.
    YP_006565702.1. NC_018289.1.
    YP_885355.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK71005; ABK71005; MSMEG_0952.
    AFP37407; AFP37407; MSMEI_0927.
    GeneIDi4534078.
    KEGGimsg:MSMEI_0927.
    msm:MSMEG_0952.
    PATRICi18074360. VBIMycSme59918_0941.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK71005.1 .
    CP001663 Genomic DNA. Translation: AFP37407.1 .
    RefSeqi WP_011727309.1. NC_018289.1.
    YP_006565702.1. NC_018289.1.
    YP_885355.1. NC_008596.1.

    3D structure databases

    ProteinModelPortali A0QR17.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246196.MSMEG_0952.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK71005 ; ABK71005 ; MSMEG_0952 .
    AFP37407 ; AFP37407 ; MSMEI_0927 .
    GeneIDi 4534078.
    KEGGi msg:MSMEI_0927.
    msm:MSMEG_0952.
    PATRICi 18074360. VBIMycSme59918_0941.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi AITCGKK.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MSME246196:GJ4Y-952-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. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.
    3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155.

    Entry informationi

    Entry nameiHEM1_MYCS2
    AccessioniPrimary (citable) accession number: A0QR17
    Secondary accession number(s): I7FXC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 69 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