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Q47Y92

- HEM1_COLP3

UniProt

Q47Y92 - HEM1_COLP3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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
    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

    BioCyciCPSY167879:GI48-3554-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:CPS_3554
    OrganismiColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus)
    Taxonomic identifieri167879 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia
    ProteomesiUP000000547: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Glutamyl-tRNA reductasePRO_1000004615Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi167879.CPS_3554.

    Structurei

    3D structure databases

    ProteinModelPortaliQ47Y92.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate 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.
    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.

    Q47Y92-1 [UniParc]FASTAAdd to Basket

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    MSIVAVGINH KTAPVAVREK ISFNPDKLSI ALQEMLNAVQ CREVAILSTC    50
    NRTELYLVQD GDFDVTQQRL IKWLESFHNV PASTILPSLY WHKDQQAVNH 100
    MMRVACGLDS LVLGEPQILG QMKQAYSQAK AAGSMSLIMD RLFQRTFGVA 150
    KQVRTETEIG ASAVSVAFAS VNLAKHIFGG LEKTKVLLVG AGETIELVAK 200
    HLYENNVGKI TVANRTLARA ENMATKIGAD VITLAQIPEH MCNADIVISS 250
    TGSTLPIIGK GMVEQALASR KHQPIFMVDL AVPRDIEEQV SELEDVFLYT 300
    VDDLQGIIAK NIANRRKAAV QAESIVNSQS DNFMAWLRGL NTQDTVISYR 350
    KQCLDNRDVL LEKAFIQLKN GKNSEAVLAE LANKLTNKFM HAPTSALQSA 400
    AQGGELDKLI YLRDIFNIDS QE 422
    Length:422
    Mass (Da):46,447
    Last modified:September 13, 2005 - v1
    Checksum:iFAA4B2312F68FD8E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000083 Genomic DNA. Translation: AAZ26562.1.
    RefSeqiWP_011044314.1. NC_003910.7.
    YP_270228.1. NC_003910.7.

    Genome annotation databases

    EnsemblBacteriaiAAZ26562; AAZ26562; CPS_3554.
    GeneIDi3520815.
    KEGGicps:CPS_3554.
    PATRICi21470039. VBIColPsy94388_3218.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000083 Genomic DNA. Translation: AAZ26562.1 .
    RefSeqi WP_011044314.1. NC_003910.7.
    YP_270228.1. NC_003910.7.

    3D structure databases

    ProteinModelPortali Q47Y92.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 167879.CPS_3554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ26562 ; AAZ26562 ; CPS_3554 .
    GeneIDi 3520815.
    KEGGi cps:CPS_3554.
    PATRICi 21470039. VBIColPsy94388_3218.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CPSY167879:GI48-3554-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 34H / ATCC BAA-681.

    Entry informationi

    Entry nameiHEM1_COLP3
    AccessioniPrimary (citable) accession number: Q47Y92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 71 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