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Q72C23

- HEM1_DESVH

UniProt

Q72C23 - HEM1_DESVH

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 sitei51 – 511NucleophileUniRule 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

    BioCyciDVUL882:GJIL-1492-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:DVU_1461
    OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
    Taxonomic identifieri882 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
    ProteomesiUP000002194: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Glutamyl-tRNA reductasePRO_0000114021Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi882.DVU1461.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72C23.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate 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.
    KOiK02492.
    OMAiLAHKLTN.
    OrthoDBiEOG6MWNBM.
    PhylomeDBiQ72C23.

    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.

    Q72C23-1 [UniParc]FASTAAdd to Basket

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    MERDIYLIGL NHRTAGVEVR ERFALTDCNV LEQGVVPIDD VVSEVLILST    50
    CNRVEILAVG RGPEVVSRVL RGWSAARGQC EHDLAPYVYT HKGPEAIRHL 100
    FRVASSLDSM VVGEPQILGQ LKDAYRKAIE RNCTRVILNR LLHKAFSVAK 150
    RVRTETGVAS SAVSISYAAV ELAKRIFGEM NQYKAMLIGA GEMAELAATH 200
    LLHAGISKIY VANRTFERGR ELARQFNGEA IHFEDLFERL ADADIIISST 250
    GAHEAIIRAR DIKDVLRRRK HRPMFFIDIA VPRDIDPDVN NLDNVYLYDI 300
    DDLKEVVEEN LAQRREEASK ALTIVEEETG KFGQWLRSLE LQPTIVDLIR 350
    RSERIAQDEL ARTLKRLGPV DDETRDALEA MLSSMVRKLN HEPITFLKRR 400
    HSEEDAGPRY IDIARRMFNL DDDNVPPDAH CDRRRHDEDN 440
    Length:440
    Mass (Da):50,045
    Last modified:July 5, 2004 - v1
    Checksum:iD166E5291B50E3BF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017285 Genomic DNA. Translation: AAS95939.1.
    RefSeqiWP_010938754.1. NC_002937.3.
    YP_010680.1. NC_002937.3.

    Genome annotation databases

    EnsemblBacteriaiAAS95939; AAS95939; DVU_1461.
    GeneIDi2794879.
    KEGGidvu:DVU1461.
    PATRICi32062756. VBIDesVul119526_1360.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017285 Genomic DNA. Translation: AAS95939.1 .
    RefSeqi WP_010938754.1. NC_002937.3.
    YP_010680.1. NC_002937.3.

    3D structure databases

    ProteinModelPortali Q72C23.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 882.DVU1461.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS95939 ; AAS95939 ; DVU_1461 .
    GeneIDi 2794879.
    KEGGi dvu:DVU1461.
    PATRICi 32062756. VBIDesVul119526_1360.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.
    PhylomeDBi Q72C23.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci DVUL882:GJIL-1492-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: Hildenborough / ATCC 29579 / NCIMB 8303.

    Entry informationi

    Entry nameiHEM1_DESVH
    AccessioniPrimary (citable) accession number: Q72C23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 82 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