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A5UU33

- HEM1_ROSS1

UniProt

A5UU33 - HEM1_ROSS1

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Roseiflexus sp. (strain RS-1)
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 (10 Jul 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 sitei48 – 481NucleophileUniRule annotation
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciRSP357808:GH5Z-1770-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    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:RoseRS_1746
    OrganismiRoseiflexus sp. (strain RS-1)
    Taxonomic identifieri357808 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesRoseiflexineaeRoseiflexaceaeRoseiflexus
    ProteomesiUP000006554: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 425425Glutamyl-tRNA reductasePRO_1000004680Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi357808.RoseRS_1746.

    Structurei

    3D structure databases

    ProteinModelPortaliA5UU33.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    HOGENOMiHOG000109649.
    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.

    A5UU33-1 [UniParc]FASTAAdd to Basket

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    MQITLIGVHQ RNTPVTVRER LAFNLYELPD ALLALRRYVD EGIILSTCNR    50
    VEVCAVTRNG VAGDEALKTF LVEQRGVDQA LFAPSLYVYH NEAVVRHLYR 100
    LAAGLDSMVL GEDQIVGQVK EALAIAHAAG AIGPVLHRVL HGALAAGKRA 150
    RTHTGIATGH VSVVSVAIDA MRQYPDLLKR GRALVIGAGH IAELSLKHLL 200
    AGGCSAITIV NRTEARADAL AQRYGVAWRP WSDLEDALAA SDIVVSCTSA 250
    PGIVLSQQMV ERAAAGRSTP LLLFDLAVPR DIDQGVAEIP GVYLHDVDAL 300
    EPICRTNRAL RAAEAERAET IIEGEVAKFM EWWAVQQAVP TIRALRKRAE 350
    DIRDAEIRRA LARCPELSPQ QRETVIALST AIINKLLHEP IVALRDPEAS 400
    GELLTAVRRL FNIDDTAVYT SANMT 425
    Length:425
    Mass (Da):46,193
    Last modified:July 10, 2007 - v1
    Checksum:i54D8BE788641CEF4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000686 Genomic DNA. Translation: ABQ90136.1.
    RefSeqiWP_011956483.1. NC_009523.1.
    YP_001276086.1. NC_009523.1.

    Genome annotation databases

    EnsemblBacteriaiABQ90136; ABQ90136; RoseRS_1746.
    GeneIDi5208703.
    KEGGirrs:RoseRS_1746.
    PATRICi23351698. VBIRosSp109359_1907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000686 Genomic DNA. Translation: ABQ90136.1 .
    RefSeqi WP_011956483.1. NC_009523.1.
    YP_001276086.1. NC_009523.1.

    3D structure databases

    ProteinModelPortali A5UU33.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 357808.RoseRS_1746.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ90136 ; ABQ90136 ; RoseRS_1746 .
    GeneIDi 5208703.
    KEGGi rrs:RoseRS_1746.
    PATRICi 23351698. VBIRosSp109359_1907.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi LAHKLTN.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci RSP357808:GH5Z-1770-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: RS-1.

    Entry informationi

    Entry nameiHEM1_ROSS1
    AccessioniPrimary (citable) accession number: A5UU33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 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