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P42809

- HEM1_METTM

UniProt

P42809 - HEM1_METTM

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei46 – 461NucleophileBy similarity
    Sitei78 – 781Important for activityBy similarity
    Binding sitei88 – 881SubstrateBy similarity
    Binding sitei99 – 991SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi168 – 1736NADPBy similarity

    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

    BioCyciMMAR79929:GH5J-1398-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:hemA
    Ordered Locus Names:MTBMA_c13940
    OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri79929 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    ProteomesiUP000000345: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398Glutamyl-tRNA reductasePRO_0000114106Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP42809.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate bindingBy similarity
    Regioni93 – 953Substrate bindingBy similarity

    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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiHEVTGEY.

    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.

    P42809-1 [UniParc]FASTAAdd to Basket

    « Hide

    MILNIRLDHK TSDVKTMETA SGRIEEIVGE LEALGAVTEK VPLMTCNRVE    50
    YYLHVTGVPP EFDFNGFTVE KDEDALLHLL RLASGLESMI IGEDQILGQI 100
    KAARLQALRE GTCGPLLDMV FTKAVHVGQT VRRKTKINRG SVSIGSAAVD 150
    LAESIHGDLK CKKVLVIGAG KMGTLVARAL AEKHLKAIMV ANRTYERAYQ 200
    LACELGGDAI HFDRLNRALR DADVVISATG SPHYILTRER VMDAVPPERR 250
    SSIVMVDIAN PRDIEESVRE LGVRLFTIDD LRGVAEENRK RREAEAREAE 300
    GIVRAELELL LRAMKHREVE PLLAEIRGRM ESLRQREAGK AIKKIENSKD 350
    PERVVEGLTR SIVDKIFHDI ALKIRDAAER DDREFLRMCS ELFDCDES 398
    Length:398
    Mass (Da):44,536
    Last modified:November 1, 1995 - v1
    Checksum:i7A2C457D9E48CB67
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83691 Genomic DNA. Translation: CAA58664.1.
    CP001710 Genomic DNA. Translation: ADL58981.1.
    PIRiS51136.
    RefSeqiYP_003850294.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL58981; ADL58981; MTBMA_c13940.
    GeneIDi9705103.
    KEGGimmg:MTBMA_c13940.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83691 Genomic DNA. Translation: CAA58664.1 .
    CP001710 Genomic DNA. Translation: ADL58981.1 .
    PIRi S51136.
    RefSeqi YP_003850294.1. NC_014408.1.

    3D structure databases

    ProteinModelPortali P42809.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL58981 ; ADL58981 ; MTBMA_c13940 .
    GeneIDi 9705103.
    KEGGi mmg:MTBMA_c13940.

    Phylogenomic databases

    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi HEVTGEY.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci MMAR79929:GH5J-1398-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 hemA gene encoding glutamyl-tRNA reductase from the archaeon Methanobacterium thermoautotrophicum strain Marburg."
      Hungerer C., Weiss D.S., Thauer R.K., Jahn D.
      Bioorg. Med. Chem. 4:1089-1095(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
      Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
      J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiHEM1_METTM
    AccessioniPrimary (citable) accession number: P42809
    Secondary accession number(s): D9PXN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 102 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 By similarity.By similarity

    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