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A4FPY4

- HEM1_SACEN

UniProt

A4FPY4 - HEM1_SACEN

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Saccharopolyspora erythraea (strain NRRL 23338)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (17 Apr 2007)
      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
    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

    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:SACE_6946
    OrganismiSaccharopolyspora erythraea (strain NRRL 23338)
    Taxonomic identifieri405948 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora
    ProteomesiUP000006728: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Glutamyl-tRNA reductasePRO_1000004682Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi405948.SACE_6946.

    Structurei

    3D structure databases

    ProteinModelPortaliA4FPY4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    A4FPY4-1 [UniParc]FASTAAdd to Basket

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    MNLLTVGLSH HSAPVRVLER VAIGADELGK VLHELLQRDH ICEAFVVSTC    50
    NRVEVYAVAE TFHGGLEDVT SVLARHSGSD VAELTDHMYV FYAGAAVEHL 100
    FSVAAGLDSM VVGEAQILGQ IRQSYGVADE AGTVGRTLHE LAQQALRVGK 150
    RVHAETGIDS EGASVVSEAL ADAETELGGL AGRRALLVGA GSMGGLAAAQ 200
    LRRAGIGEVV IANRTAVNGE RLAESLRTDG VPASAVALDG LRSAISWADL 250
    VVTCTGAVGA VVTTEHVETG DRGPLVFCDL GLPRDTAPEV AELPGVTVVD 300
    LATLQRRLSE QQGGNESERA AAIVAEEVRG YLAAQRSAEV TPTVTALRKR 350
    AAEVVDAELL RLDSKLPALE GDVRDELART VRRVVDKLLH APTVRVKQLA 400
    STPGGSGYAD ALRELFELDP QTAAVLGTAQ ADDGRARGSA SVAEARRAGA 450
    PGARDELRDL PAQDGDDR 468
    Length:468
    Mass (Da):48,954
    Last modified:April 17, 2007 - v1
    Checksum:i60560B145F6A7FFA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAM06109.1.
    RefSeqiWP_009943986.1. NZ_ABFV01000011.1.
    YP_001109034.1. NC_009142.1.

    Genome annotation databases

    EnsemblBacteriaiCAM06109; CAM06109; SACE_6946.
    GeneIDi4946678.
    KEGGisen:SACE_6946.
    PATRICi23421356. VBISacEry28377_6956.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM420293 Genomic DNA. Translation: CAM06109.1 .
    RefSeqi WP_009943986.1. NZ_ABFV01000011.1.
    YP_001109034.1. NC_009142.1.

    3D structure databases

    ProteinModelPortali A4FPY4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405948.SACE_6946.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM06109 ; CAM06109 ; SACE_6946 .
    GeneIDi 4946678.
    KEGGi sen:SACE_6946.
    PATRICi 23421356. VBISacEry28377_6956.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    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 genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
      Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
      Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NRRL 23338.

    Entry informationi

    Entry nameiHEM1_SACEN
    AccessioniPrimary (citable) accession number: A4FPY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 62 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