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P46724

- HEM1_MYCLE

UniProt

P46724 - HEM1_MYCLE

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    • 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

    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:ML2422
    ORF Names:B2168_C3_261
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML2422.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 467467Glutamyl-tRNA reductasePRO_0000114040Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272631.ML2422.

    Structurei

    3D structure databases

    ProteinModelPortaliP46724.
    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.
    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.

    P46724-1 [UniParc]FASTAAdd to Basket

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    MSILLFGVSH RSAPVSVLEQ LSLDRSDQIK IVDRVLQSPL VTEAMVLSTC    50
    NRVEVYAVVE AFHAGLSVIG QVLSEYSAMS IGDLTKYAYV RYSEAAVEHL 100
    FTVASGLDSA VVGEQQVLGQ VRRAYAAAEA NRTVGQVLHE VAQRALSVGK 150
    RVHSETAIDA AGVSVVSVAL GIAGRTLGGL AGRIAVVIGA GAMGALSSSY 200
    LTQANVGRIH VLNRSLSRAR RLAGKIGESG VPADVWTLNH LDEALADADL 250
    VVSCTGAVSP VVSLADVHHA LAAMRRDETT RPLVICDLGM PRDVDPAVAK 300
    LPGVWVVDVE GVQREPSARA SAADVDAARR IVAAEVATYL TRQRMAEVAP 350
    TVTALRQRAA DVVEAELLRL DHRLPGLESA QREEVARTVR RVVDKLLHAP 400
    TVRIKQLASA PGGDSYTEAL RELFELDQTA VDAVATAGEL PVMVSGFSDT 450
    TRYGTSPAQS SSKYHAE 467
    Length:467
    Mass (Da):49,483
    Last modified:November 1, 1995 - v1
    Checksum:iF93245F6861F96E9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00018 Genomic DNA. Translation: AAA17243.1.
    AL583925 Genomic DNA. Translation: CAC31938.1.
    PIRiS72907.
    RefSeqiNP_302567.1. NC_002677.1.
    WP_010908887.1. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC31938; CAC31938; CAC31938.
    GeneIDi909785.
    KEGGimle:ML2422.
    PATRICi18059489. VBIMycLep78757_4659.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00018 Genomic DNA. Translation: AAA17243.1 .
    AL583925 Genomic DNA. Translation: CAC31938.1 .
    PIRi S72907.
    RefSeqi NP_302567.1. NC_002677.1.
    WP_010908887.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali P46724.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML2422.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC31938 ; CAC31938 ; CAC31938 .
    GeneIDi 909785.
    KEGGi mle:ML2422.
    PATRICi 18059489. VBIMycLep78757_4659.

    Organism-specific databases

    Lepromai ML2422.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    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. Smith D.R., Robison K.
      Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TN.

    Entry informationi

    Entry nameiHEM1_MYCLE
    AccessioniPrimary (citable) accession number: P46724
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 109 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