Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B1MHI6

- HEM1_MYCA9

UniProt

B1MHI6 - HEM1_MYCA9

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    BioCyciMABS36809-WGS:GSQO-4013-MONOMER.
    MABS561007:GJTG-4013-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:MAB_3993c
    OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196)
    Taxonomic identifieri561007 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus
    ProteomesiUP000007137: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Glutamyl-tRNA reductasePRO_1000093152Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi561007.MAB_3993c.

    Structurei

    3D structure databases

    ProteinModelPortaliB1MHI6.
    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.
    OMAiHEVTGEY.
    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.

    B1MHI6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVLLFGASH RSAPVPVLEK LAIGEADQPK IIEHILQSPL VTEVMVLSTC    50
    NRVEVYAVVE AFHGGLTVIG EAIARHAGMG MNELTKYAYV RYSEAAVEHL 100
    FAVASGLDSM VVGEQQVLGQ VRNAYATAES HQAVGRVLHE LSQSALRVGK 150
    RVHSETGIDA AGASVVSVAL NLADNKLDGL PGRTAAVVGA GSMGSLATAQ 200
    LIRAGIDNLW VVNRSAERAR RLAATAREAG VNAQAITLDN LDQALAQADV 250
    VVSCTGAVRP VISLADVHHA LEGGRQLVFC DLGMPRDVDP TVAGLPGVVV 300
    VDMERIQREP TARAAANDAG AARQIVNDEV ARYLTGERMA EVTPTVTALR 350
    QRAAEVVEAE LLRLDGRLPG LAGAERDEVA KTVRRVVDKL LHAPTVRVKQ 400
    LASAPGGDSY AEALRELFEL DPHTVEAVAT AGELPLATKE LHE 443
    Length:443
    Mass (Da):46,794
    Last modified:April 29, 2008 - v1
    Checksum:i8A722AE7C1AFCD99
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU458896 Genomic DNA. Translation: CAM64067.1.
    RefSeqiYP_001704721.1. NC_010397.1.

    Genome annotation databases

    EnsemblBacteriaiCAM64067; CAM64067; MAB_3993c.
    GeneIDi5966456.
    KEGGimab:MAB_3993c.
    PATRICi17979804. VBIMycAbs55940_4067.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU458896 Genomic DNA. Translation: CAM64067.1 .
    RefSeqi YP_001704721.1. NC_010397.1.

    3D structure databases

    ProteinModelPortali B1MHI6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 561007.MAB_3993c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM64067 ; CAM64067 ; MAB_3993c .
    GeneIDi 5966456.
    KEGGi mab:MAB_3993c.
    PATRICi 17979804. VBIMycAbs55940_4067.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MABS36809-WGS:GSQO-4013-MONOMER.
    MABS561007:GJTG-4013-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. "Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
      Genoscope
      Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
      Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 19977 / DSM 44196.

    Entry informationi

    Entry nameiHEM1_MYCA9
    AccessioniPrimary (citable) accession number: B1MHI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 57 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