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A6VI77

- HEM1_METM7

UniProt

A6VI77 - HEM1_METM7

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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 sitei39 – 391NucleophileUniRule annotation
    Sitei75 – 751Important for activityUniRule annotation
    Binding sitei85 – 851SubstrateUniRule annotation
    Binding sitei96 – 961SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi164 – 1696NADPUniRule 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

    BioCyciMMAR426368:GHHL-1118-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:MmarC7_1087
    OrganismiMethanococcus maripaludis (strain C7 / ATCC BAA-1331)
    Taxonomic identifieri426368 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
    ProteomesiUP000002298: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 382382Glutamyl-tRNA reductasePRO_1000004640Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi426368.MmarC7_1087.

    Structurei

    3D structure databases

    ProteinModelPortaliA6VI77.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 414Substrate bindingUniRule annotation
    Regioni90 – 923Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiMIICEEL.

    Family and domain databases

    Gene3Di1.10.1200.70. 1 hit.
    3.40.50.720. 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.

    A6VI77-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVVKADYKK YPIPVLEKMR IDEDEFYKKY EACVVVQTCN RIEAYFDTEV    50
    NSNVDDILKD FQGFDILKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS 100
    FQKAREFKKT SRYLDSLFLK AIHVGQRART ETKINEGGVS IGSAAVELAE 150
    KNFGLTNRNV LLIGAGEIGT LVAKALVEKH IKAVIVANRT YERAETLAKE 200
    LKGMAVHFDK LREAVNFSDV IICATSSPHY ILEKEDLIDV GNKIIIDIAN 250
    PRDVDDSVRE LENIELYTID DLRNISDKNL QRRIEEIPTV EKIIEEEYDV 300
    LMKQIEKINV EEVLKEFNTY IEEIRVKELE KAIKLSKSKD PEEIMENFSK 350
    AFAKRITHDF VSYSLNTSKE DLMNSAWWKN GK 382
    Length:382
    Mass (Da):43,779
    Last modified:August 21, 2007 - v1
    Checksum:i88183D579031E9B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000745 Genomic DNA. Translation: ABR66153.1.
    RefSeqiWP_011977465.1. NC_009637.1.
    YP_001330304.1. NC_009637.1.

    Genome annotation databases

    EnsemblBacteriaiABR66153; ABR66153; MmarC7_1087.
    GeneIDi5329330.
    KEGGimmz:MmarC7_1087.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000745 Genomic DNA. Translation: ABR66153.1 .
    RefSeqi WP_011977465.1. NC_009637.1.
    YP_001330304.1. NC_009637.1.

    3D structure databases

    ProteinModelPortali A6VI77.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 426368.MmarC7_1087.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR66153 ; ABR66153 ; MmarC7_1087 .
    GeneIDi 5329330.
    KEGGi mmz:MmarC7_1087.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi MIICEEL.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MMAR426368:GHHL-1118-MONOMER.

    Family and domain databases

    Gene3Di 1.10.1200.70. 1 hit.
    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: C7 / ATCC BAA-1331.

    Entry informationi

    Entry nameiHEM1_METM7
    AccessioniPrimary (citable) accession number: A6VI77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 54 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3