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A1WI55

- HEM1_VEREI

UniProt

A1WI55 - HEM1_VEREI

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Verminephrobacter eiseniae (strain EF01-2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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 sitei53 – 531NucleophileUniRule annotation
    Sitei100 – 1001Important for activityUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi190 – 1956NADPUniRule 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

    BioCyciVEIS391735:GHY5-1565-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:Veis_1553
    OrganismiVerminephrobacter eiseniae (strain EF01-2)
    Taxonomic identifieri391735 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter
    ProteomesiUP000000374: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Glutamyl-tRNA reductasePRO_0000335079Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi391735.Veis_1553.

    Structurei

    3D structure databases

    ProteinModelPortaliA1WI55.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 554Substrate bindingUniRule annotation
    Regioni115 – 1173Substrate 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.
    HOGENOMiHOG000109650.
    KOiK02492.
    OMAiKMLHGTM.
    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.

    A1WI55-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVWALGINH STAPLDLRGR FAFALDQIAP RLQGLRQSLS SHPGVETAML    50
    STCNRTEIYC AAEQAAIDHT LGWLAHSGGV STALLRAHSY TLQDSRAARH 100
    AFRVASGLDS MVLGEAQILG QMKDAVRAAE TAGVLGSTLN QLFQRSFAVA 150
    KEVRSSTEIG AHSISMAAAA VRLAGQLFED LSQIRVLFVG AGAMIALCAT 200
    HFAAKNPLGL ALANRTLERG EQLAARFGAT VLRLADLPER LHEFDAVISC 250
    TASSLPIIGL GAVERALKKR RHRPMFMVDL AVPRDIEPEV KALGDVYLYT 300
    VDDLASVVQT GQASRQAAVA QAEAIIDAGV QSFMHWLAQR NPVGGVVPLI 350
    RQLNAQTEVW RASEIARAKK LLAKGEAPDA VLDALARGLT QKMLHGTMAE 400
    LRAGDADMRA QTAQTVARLF LRAQSNHDL 429
    Length:429
    Mass (Da):45,982
    Last modified:February 6, 2007 - v1
    Checksum:iF4B53E6605900240
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000542 Genomic DNA. Translation: ABM57312.1.
    RefSeqiYP_996330.1. NC_008786.1.

    Genome annotation databases

    EnsemblBacteriaiABM57312; ABM57312; Veis_1553.
    GeneIDi4690921.
    KEGGivei:Veis_1553.
    PATRICi24016649. VBIVerEis120356_1724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000542 Genomic DNA. Translation: ABM57312.1 .
    RefSeqi YP_996330.1. NC_008786.1.

    3D structure databases

    ProteinModelPortali A1WI55.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 391735.Veis_1553.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM57312 ; ABM57312 ; Veis_1553 .
    GeneIDi 4690921.
    KEGGi vei:Veis_1553.
    PATRICi 24016649. VBIVerEis120356_1724.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109650.
    KOi K02492.
    OMAi KMLHGTM.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci VEIS391735:GHY5-1565-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. "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: EF01-2.

    Entry informationi

    Entry nameiHEM1_VEREI
    AccessioniPrimary (citable) accession number: A1WI55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 67 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