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A0LDT6

- HEM1_MAGSM

UniProt

A0LDT6 - HEM1_MAGSM

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Magnetococcus sp. (strain MC-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (12 Dec 2006)
      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 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

    BioCyciMSP156889:GH36-3698-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:Mmc1_3644
    OrganismiMagnetococcus sp. (strain MC-1)
    Taxonomic identifieri156889 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
    ProteomesiUP000002586: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 421421Glutamyl-tRNA reductasePRO_1000004633Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi156889.Mmc1_3644.

    Structurei

    3D structure databases

    ProteinModelPortaliA0LDT6.
    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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiLAHKLTN.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A0LDT6-1 [UniParc]FASTAAdd to Basket

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    MKLVVVGLNH KSAPVSLREK VAYSSDTLPR SLQALTRLDA VHEGTILSTC    50
    NRVEIYMASR DPDAAAAQTS QWIARDHALD PADVTPHLYT KAESEAVRHG 100
    FCVASSLDSM VLGEAQILGQ MKQAYQDALS AGSTGVVLNR FFQHAFLTAK 150
    RVRTETSIAE NSVSVASAAV DLAKRIFGDL SGHSCLLIGA GEMCELAARH 200
    LVTHGVKEVL VTNRTFSRAV DLAQQFDGHA FPIEALAENL HRADIVISST 250
    GSTVYMVGPD MVKQALKSRR QRPIFLIDIA VPRDLDPEIG QVDSAFLYDM 300
    DDLNKIVNDN RQDRAEAAQA AMQIIEGETP LFIQWLDTLD VVPTIKQMRR 350
    KAEAAKDQLL QKHLAGWDLS DTDRQRVENL ARQLVNKLMH DPTERLRSLT 400
    NEHDGDRYID AARKLYKLDD D 421
    Length:421
    Mass (Da):46,617
    Last modified:December 12, 2006 - v1
    Checksum:i2E87386524797EA0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK46129.1.
    RefSeqiYP_867535.1. NC_008576.1.

    Genome annotation databases

    EnsemblBacteriaiABK46129; ABK46129; Mmc1_3644.
    GeneIDi4483835.
    KEGGimgm:Mmc1_3644.
    PATRICi22434017. VBIMagSp23654_3727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000471 Genomic DNA. Translation: ABK46129.1 .
    RefSeqi YP_867535.1. NC_008576.1.

    3D structure databases

    ProteinModelPortali A0LDT6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 156889.Mmc1_3644.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK46129 ; ABK46129 ; Mmc1_3644 .
    GeneIDi 4483835.
    KEGGi mgm:Mmc1_3644.
    PATRICi 22434017. VBIMagSp23654_3727.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MSP156889:GH36-3698-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MC-1.

    Entry informationi

    Entry nameiHEM1_MAGSM
    AccessioniPrimary (citable) accession number: A0LDT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 61 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