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A9FDP5

- HEM1_SORC5

UniProt

A9FDP5 - HEM1_SORC5

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 sitei48 – 481NucleophileUniRule annotation
    Sitei115 – 1151Important for activityUniRule annotation
    Binding sitei125 – 1251SubstrateUniRule annotation
    Binding sitei136 – 1361SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi205 – 2106NADPUniRule 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

    BioCyciSCEL448385:GJ75-1683-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:sce1624
    OrganismiSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
    Taxonomic identifieri448385 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium
    ProteomesiUP000002139: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Glutamyl-tRNA reductasePRO_0000335074Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi448385.sce1624.

    Structurei

    3D structure databases

    ProteinModelPortaliA9FDP5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni130 – 1323Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiLNKQFET.
    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. 2 hits.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A9FDP5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIFVGLSHKT APIEVRERLA IGRDRLPEVL ARLTAHPAIG EALVLSTCNR    50
    VEIYASPRQQ APAPPRPGSA PPPSDEELSR NNEALRAAVA TLVGLGGDAV 100
    RGHLAGRVGS DAVLHLFRVA ASLDSMVVGE PQILGQMKEA IEVARGAKTL 150
    GVRLGRAAHR AIKVGKRVRT ETAIGAGQVS VSSVAIDLAR QIFADLAGHT 200
    ALLIGAGDMA EAASKLLVRA GARLIVVNRS PDRAAALARE VGGEPRPWAD 250
    LERSVIDADI VISSTSSPNY VVTPDLVRRA RKARKGRSLF LIDIAVPRDI 300
    DPAVNKLDSV YLYDVDDLSQ IVAESVEGRA AEAARAEAIV ADEAQAFEAW 350
    TLERALTPTI VGLRARTRSI LVAEVERSLS GKLRHLGVAE RQALAMMIDA 400
    ATNKLLHVPT TRLRAMASDP RVAEHVDSLR ELFDIDGAPP ENAAASALAE 450
    GELRGAVDGP PTPRSARGAA PPASGARGGG SPRHADPRPQ AAEDNGVYAR 500
    QPGGRPAEAG VMAVANPAAA VSAAGLKGA 529
    Length:529
    Mass (Da):55,293
    Last modified:February 5, 2008 - v1
    Checksum:iC115B5E9345DF6EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM746676 Genomic DNA. Translation: CAN91782.1.
    RefSeqiWP_012234259.1. NC_010162.1.
    YP_001612262.1. NC_010162.1.

    Genome annotation databases

    EnsemblBacteriaiCAN91782; CAN91782; sce1624.
    GeneIDi5807028.
    KEGGiscl:sce1624.
    PATRICi23661093. VBISorCel80414_1772.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM746676 Genomic DNA. Translation: CAN91782.1 .
    RefSeqi WP_012234259.1. NC_010162.1.
    YP_001612262.1. NC_010162.1.

    3D structure databases

    ProteinModelPortali A9FDP5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 448385.sce1624.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAN91782 ; CAN91782 ; sce1624 .
    GeneIDi 5807028.
    KEGGi scl:sce1624.
    PATRICi 23661093. VBISorCel80414_1772.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi LNKQFET.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci SCEL448385:GJ75-1683-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. 2 hits.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the myxobacterium Sorangium cellulosum."
      Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.
      , Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., Puehler A., Mueller R.
      Nat. Biotechnol. 25:1281-1289(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: So ce56.

    Entry informationi

    Entry nameiHEM1_SORC5
    AccessioniPrimary (citable) accession number: A9FDP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 57 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