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Q8PW60

- HEM1_METMA

UniProt

Q8PW60 - HEM1_METMA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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 sitei49 – 491NucleophileUniRule annotation
    Sitei90 – 901Important for activityUniRule annotation
    Binding sitei100 – 1001SubstrateUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi180 – 1856NADPUniRule 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

    BioCyciMMAZ192952:GCK2-1784-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:MM_1741
    OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
    Taxonomic identifieri192952 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000000595: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 448448Glutamyl-tRNA reductasePRO_0000114103Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi192952.MM_1741.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8PW60.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 514Substrate bindingUniRule annotation
    Regioni105 – 1073Substrate 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.
    OMAiLAHKLTN.

    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.

    Q8PW60-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEISSMVIS HKKAKVEEME SAWHGDLDGL LRNLYKHEYV YECVVLKTCN    50
    RVEIYVVSPK SSSVLFSFAK EMGASTHIID FYGHDESLEH LLRLAGGLES 100
    MIVGEDQILG QIKDLYAYSK KAGTTGKILE TAFEKAIQVG KRIRNETRIN 150
    KGSVSIGSAA VDLAEDIFGG LTGKNVLVIG AGEIGVLVAK ALAEKDIEAI 200
    YIANRTYKKA EEIAYELGGH AVRLDDIRDY LPGADVVISG TGAPHYILTR 250
    EIVEEAIKCR ERKLLLIDIA NPRDIEESVV ELENVELCNI DNLRVISERT 300
    LRMRKEEAKK AEAIIQEEIR LLNLQYKRQK ADRLISELYK QVYDVRLRER 350
    QKAVNRLSSY HTIGDIETEV LDDLTRSIVN KILGEPTKVL RQAAELGNEE 400
    FLDVVSRVFC LDKEKVRFEK IKQAKFDQIK PGCTKEQAEV KEEYAVKD 448
    Length:448
    Mass (Da):50,562
    Last modified:October 1, 2002 - v1
    Checksum:i0733780153168AD9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008384 Genomic DNA. Translation: AAM31437.1.
    RefSeqiNP_633765.1. NC_003901.1.

    Genome annotation databases

    EnsemblBacteriaiAAM31437; AAM31437; MM_1741.
    GeneIDi1480083.
    KEGGimma:MM_1741.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008384 Genomic DNA. Translation: AAM31437.1 .
    RefSeqi NP_633765.1. NC_003901.1.

    3D structure databases

    ProteinModelPortali Q8PW60.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 192952.MM_1741.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM31437 ; AAM31437 ; MM_1741 .
    GeneIDi 1480083.
    KEGGi mma:MM_1741.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MMAZ192952:GCK2-1784-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 genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
      Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
      , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
      J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

    Entry informationi

    Entry nameiHEM1_METMA
    AccessioniPrimary (citable) accession number: Q8PW60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 92 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