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Q21YY8

- HEM1_ALBFT

UniProt

Q21YY8 - HEM1_ALBFT

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (18 Apr 2006)
      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
    Sitei98 – 981Important for activityUniRule annotation
    Binding sitei108 – 1081SubstrateUniRule annotation
    Binding sitei119 – 1191SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1936NADPUniRule 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

    BioCyciAFER338969:GHU9-1285-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:Rfer_1281
    OrganismiAlbidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens)
    Taxonomic identifieri338969 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax
    ProteomesiUP000008332: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Glutamyl-tRNA reductasePRO_0000335066Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi338969.Rfer_1281.

    Structurei

    3D structure databases

    ProteinModelPortaliQ21YY8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni50 – 534Substrate bindingUniRule annotation
    Regioni113 – 1153Substrate 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.

    Q21YY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVWTLGINH TTAPLDLRGR FAFALDQVEP TLRALRGSLS RQPEAALIST    50
    CNRTEIYCAG EKPELEHTLD WLAQTGGVSS SLLRTHSYTL QDDLAARHAF 100
    RVASGLDSMV LGETQILGQI KNAVRAAEAA GALGNTLSQL FQRSFAVAKE 150
    VRSSTEIGAH SISMAAAAVR LAGQLFEDLG QVKILFVGAG EMIELCATHF 200
    AAKSPKAIAI ANRSLENGEK LASRFGAEVM RLADLPDRLH EFDAVVSCTA 250
    STLPIIGLGA VERALKRRKR RPMFMVDLAV PRDIEIEVKA LEDVYLYTVD 300
    DLASVVQTAQ ASRQAAVAQA EAIVDAGVLS FMHWVDQRGS VPLIQQLNAQ 350
    ADEWRAAELA RARKLLAKGE DVEAVLEALS KGLTQKMLHG AMTELRASDT 400
    AARERASAAI QHFFLRKER 419
    Length:419
    Mass (Da):45,460
    Last modified:April 18, 2006 - v1
    Checksum:iA16CEB6A75242010
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000267 Genomic DNA. Translation: ABD69015.1.
    RefSeqiWP_011463583.1. NC_007908.1.
    YP_522546.1. NC_007908.1.

    Genome annotation databases

    EnsemblBacteriaiABD69015; ABD69015; Rfer_1281.
    GeneIDi3962154.
    KEGGirfr:Rfer_1281.
    PATRICi23235115. VBIRhoFer131161_1581.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000267 Genomic DNA. Translation: ABD69015.1 .
    RefSeqi WP_011463583.1. NC_007908.1.
    YP_522546.1. NC_007908.1.

    3D structure databases

    ProteinModelPortali Q21YY8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 338969.Rfer_1281.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD69015 ; ABD69015 ; Rfer_1281 .
    GeneIDi 3962154.
    KEGGi rfr:Rfer_1281.
    PATRICi 23235115. VBIRhoFer131161_1581.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci AFER338969:GHU9-1285-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 of Rhodoferax ferrireducens DSM 15236."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.
      , Kyrpides N., Ivanova N., Richardson P.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-621 / DSM 15236 / T118.

    Entry informationi

    Entry nameiHEM1_ALBFT
    AccessioniPrimary (citable) accession number: Q21YY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 75 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