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A9KP81

- HEM11_CLOPH

UniProt

A9KP81 - HEM11_CLOPH

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Lachnoclostridium phytofermentans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 sitei46 – 461NucleophileUniRule annotation
    Sitei93 – 931Important for activityUniRule annotation
    Binding sitei103 – 1031SubstrateUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi183 – 1886NADPUniRule 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

    BioCyciCPHY357809:GHCL-1410-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 1UniRule annotation
    Gene namesi
    Name:hemA1UniRule annotation
    Ordered Locus Names:Cphy_1368
    OrganismiClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Lachnoclostridium phytofermentans)
    Taxonomic identifieri357809 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesLachnospiraceae
    ProteomesiUP000000370: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 403403Glutamyl-tRNA reductase 1PRO_0000335023Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi357809.Cphy_1368.

    Structurei

    3D structure databases

    ProteinModelPortaliA9KP81.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate bindingUniRule annotation
    Regioni108 – 1103Substrate 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.
    HOGENOMiHOG000069583.
    KOiK02492.
    OMAiAETEIQG.
    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.
    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]
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A9KP81-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME    50
    VWVSCFEEFE TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG 100
    LKSKIIGEDQ ILTQVREALE LSRENYCTDS VLETLFRFAI TSAKQVKTQI 150
    HLSVVNSSVI HHVVHELKLS NYLFKGKKCL VIGNGEMGKL AATKLEEEGS 200
    DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS ATSSPNMTIH 250
    LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE 300
    MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT 350
    MKKIEMDSND KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK 400
    NIY 403
    Length:403
    Mass (Da):46,029
    Last modified:February 5, 2008 - v1
    Checksum:i497F1715C4F6418F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000885 Genomic DNA. Translation: ABX41743.1.
    RefSeqiWP_012199397.1. NC_010001.1.
    YP_001558482.1. NC_010001.1.

    Genome annotation databases

    EnsemblBacteriaiABX41743; ABX41743; Cphy_1368.
    GeneIDi5742318.
    KEGGicpy:Cphy_1368.
    PATRICi19502358. VBICloPhy16213_1418.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000885 Genomic DNA. Translation: ABX41743.1 .
    RefSeqi WP_012199397.1. NC_010001.1.
    YP_001558482.1. NC_010001.1.

    3D structure databases

    ProteinModelPortali A9KP81.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 357809.Cphy_1368.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX41743 ; ABX41743 ; Cphy_1368 .
    GeneIDi 5742318.
    KEGGi cpy:Cphy_1368.
    PATRICi 19502358. VBICloPhy16213_1418.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000069583.
    KOi K02492.
    OMAi AETEIQG.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CPHY357809:GHCL-1410-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.
    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 ]
    SUPFAMi SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700394 / DSM 18823 / ISDg.

    Entry informationi

    Entry nameiHEM11_CLOPH
    AccessioniPrimary (citable) accession number: A9KP81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 56 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