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Q46CH3

- HEM1_METBF

UniProt

Q46CH3 - HEM1_METBF

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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 sitei49 – 491NucleophileUniRule annotation
    Sitei89 – 891Important for activityUniRule annotation
    Binding sitei99 – 991SubstrateUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1846NADPUniRule 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

    BioCyciMBAR269797:GHUW-1494-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:Mbar_A1462
    OrganismiMethanosarcina barkeri (strain Fusaro / DSM 804)
    Taxonomic identifieri269797 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000008156: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Glutamyl-tRNA reductasePRO_1000004636Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi269797.Mbar_A1462.

    Structurei

    3D structure databases

    ProteinModelPortaliQ46CH3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni104 – 1063Substrate 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.
    OMAiEHMIEDE.

    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.

    Q46CH3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEISSMVIS HKKAKIEEME SAWHGDLDGL LHNLYNHEYI HECVVLKTCN    50
    RVEIYVVSPS SSILFSFAKE MGASTHIIDF YGHDESLEHL LRLAGGLESM 100
    IVGEDQILGQ IKELYAYSKK AGTTGKILDT AFDKAIQVGK RIRNETRINK 150
    GSVSIGSAAV DLAEEILDGL AGKSVLVIGA GEIGVLVAKA LAAKDIEAIY 200
    IANRTFKKAE ELAYELGGYA VKLNDVQTQL KNADVVISGT GAPHYILTRE 250
    IVEKAIEERD KTRKLLLIDI ANPRDIEESV AELDNVKLCN IDNLRVISEK 300
    TLKMRKEEAK KAEAIIQEEI KLLNLQYKRQ RADKIISDLY KQIYDVRIRE 350
    REKAVNRLCA YHTIGKIETD VLDDLTHSIA NKILAEPTKV LRQAAELGND 400
    EFLDVAARIF CLEKDKVKAE KIKSDCGIKV EKMKPDCESA TDRVSEKGN 449
    Length:449
    Mass (Da):50,081
    Last modified:September 13, 2005 - v1
    Checksum:i923A7749FF2E4A86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000099 Genomic DNA. Translation: AAZ70419.1.
    RefSeqiWP_011306465.1. NC_007355.1.
    YP_304999.1. NC_007355.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ70419; AAZ70419; Mbar_A1462.
    GeneIDi3627743.
    KEGGimba:Mbar_A1462.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000099 Genomic DNA. Translation: AAZ70419.1 .
    RefSeqi WP_011306465.1. NC_007355.1.
    YP_304999.1. NC_007355.1.

    3D structure databases

    ProteinModelPortali Q46CH3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269797.Mbar_A1462.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ70419 ; AAZ70419 ; Mbar_A1462 .
    GeneIDi 3627743.
    KEGGi mba:Mbar_A1462.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MBAR269797:GHUW-1494-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. "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
      Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
      J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fusaro / DSM 804.

    Entry informationi

    Entry nameiHEM1_METBF
    AccessioniPrimary (citable) accession number: Q46CH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 73 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