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A5D3L4

- HEM1_PELTS

UniProt

A5D3L4 - HEM1_PELTS

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      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

    BioCyciPTHE370438:GCGQ-1007-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:PTH_0971
    OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
    Taxonomic identifieri370438 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
    ProteomesiUP000006556: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Glutamyl-tRNA reductasePRO_1000075416Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi370438.PTH_0971.

    Structurei

    3D structure databases

    ProteinModelPortaliA5D3L4.
    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.
    HOGENOMiHOG000109651.
    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.
    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.

    A5D3L4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLILVVGLNH RTAPVEVREK LSFSAKSLQG ALAQLKSYPV IEGCAILSTC    50
    NRTEIYAATL EMDDGLNAIW DFLSRWSGVG ISEIKNFTYS HTLYDTIRHL 100
    FRVAAGLDSM ILGETQILGQ VREAYQRAIE YESTNRVLNT LFQQAITVGK 150
    RVRTETGIDR NAVSISYAAV ELARQHLGSL DGRSVLVIGA GKMSELTARH 200
    LVANGVSSVI VSNRSFERAV ALAEQFRGRA VRFDELYRCM EAADIVISCT 250
    AASHCVVKAE EVSRVMDKRR GRAIFMVDIA VPRDIEAEVG NLAGVTLFDI 300
    DDLKNVIDQN LAERKQAAVK AEEIIEEELD GFMKWLGMQF VVPTISALKK 350
    WGDEIKQKEL CRALNRLGNI SEHDRKVICS MANSIVNQIL HVPVAQLKSY 400
    ALTTEGHLYT EILQNLFNLD VPGQKPKKQP APAGIKEPVL AKKG 444
    Length:444
    Mass (Da):49,167
    Last modified:June 12, 2007 - v1
    Checksum:iCE7874AB66E30749
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009389 Genomic DNA. Translation: BAF59152.1.
    RefSeqiWP_012032142.1. NC_009454.1.
    YP_001211521.1. NC_009454.1.

    Genome annotation databases

    EnsemblBacteriaiBAF59152; BAF59152; PTH_0971.
    GeneIDi5140131.
    KEGGipth:PTH_0971.
    PATRICi22908973. VBIPelThe8413_1091.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009389 Genomic DNA. Translation: BAF59152.1 .
    RefSeqi WP_012032142.1. NC_009454.1.
    YP_001211521.1. NC_009454.1.

    3D structure databases

    ProteinModelPortali A5D3L4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 370438.PTH_0971.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAF59152 ; BAF59152 ; PTH_0971 .
    GeneIDi 5140131.
    KEGGi pth:PTH_0971.
    PATRICi 22908973. VBIPelThe8413_1091.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PTHE370438:GCGQ-1007-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 Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
      Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
      Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13744 / JCM 10971 / SI.

    Entry informationi

    Entry nameiHEM1_PELTS
    AccessioniPrimary (citable) accession number: A5D3L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 59 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