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Q6NJK1

- HEM1_CORDI

UniProt

Q6NJK1 - HEM1_CORDI

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 bindingi191 – 1966NADPUniRule 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:DIP0400
    OrganismiCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
    Taxonomic identifieri257309 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000002198: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 438438Glutamyl-tRNA reductasePRO_0000114015Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi257309.DIP0400.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NJK1.
    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.
    OMAiPYLYVHY.
    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.

    Q6NJK1-1 [UniParc]FASTAAdd to Basket

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    MSVLVVGMSH RSAPVALLEK LSMDDGVRTN TVSDLVARPS LAEAMIVSTC    50
    NRLEVYAMTS SFHTGVNDVV EVLHDMSGVD MEELRGYLYV RYADAAAEHM 100
    MEVTSGLDSM VVGEQQIIGQ VRTAYHSATE AGTVGPALHG LVQASLHTGK 150
    RVHTETDIDD AGASMVSFAC DEALAQMSAT NFAGCRALVL GAGAMASLAA 200
    THLGRLGIEH ITVANRTFER AQRLADHAVE AGVAASAIEF ERRMDVLCDV 250
    DVVVSATGAN TFTIEAANIP AAHGDLMMID LSLPRDISDD VAEVPGVHLV 300
    NIEKLRDVAS SGEAKDHAAQ RIVAEELEAY TSAQRIRDVA PAVAALRRHA 350
    SSLIDSELAR LSTRVPSMDE DDFSEVQRTV RRVVDKLLHQ PTVRVKELAA 400
    QSGTVSYDTA IQELFGLAVE ATPVAVNVDE LPERINKR 438
    Length:438
    Mass (Da):46,918
    Last modified:July 5, 2004 - v1
    Checksum:i2BF1FD0E18AAF184
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248355 Genomic DNA. Translation: CAE48904.1.
    RefSeqiNP_938781.1. NC_002935.2.
    WP_010934271.1. NC_002935.2.

    Genome annotation databases

    EnsemblBacteriaiCAE48904; CAE48904; DIP0400.
    GeneIDi2650204.
    KEGGicdi:DIP0400.
    PATRICi21481957. VBICorDip47633_0383.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248355 Genomic DNA. Translation: CAE48904.1 .
    RefSeqi NP_938781.1. NC_002935.2.
    WP_010934271.1. NC_002935.2.

    3D structure databases

    ProteinModelPortali Q6NJK1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257309.DIP0400.

    Protocols and materials databases

    DNASUi 2650204.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE48904 ; CAE48904 ; DIP0400 .
    GeneIDi 2650204.
    KEGGi cdi:DIP0400.
    PATRICi 21481957. VBICorDip47633_0383.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi PYLYVHY.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

    Entry informationi

    Entry nameiHEM1_CORDI
    AccessioniPrimary (citable) accession number: Q6NJK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 81 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