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A1TTC3

- HEM1_ACIAC

UniProt

A1TTC3 - HEM1_ACIAC

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (06 Feb 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 sitei56 – 561NucleophileUniRule annotation
    Sitei103 – 1031Important for activityUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation
    Binding sitei124 – 1241SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1986NADPUniRule 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

    BioCyciACIT397945:GI5W-3706-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:Aave_3663
    OrganismiAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli)
    Taxonomic identifieri397945 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax
    ProteomesiUP000002596: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Glutamyl-tRNA reductasePRO_0000335001Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi397945.Aave_3663.

    Structurei

    3D structure databases

    ProteinModelPortaliA1TTC3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 584Substrate bindingUniRule annotation
    Regioni118 – 1203Substrate 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.
    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.

    A1TTC3-1 [UniParc]FASTAAdd to Basket

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    MAVWALGINH TTAPLDLRGR FAFAIDQIAP TLQGLRQSLG GATRHPQVET    50
    AILSTCNRTE IYCAGQQPAL DHTLDWLAHS GGVSPSLLRS HSYTLEESLV 100
    ARHAFRVASG LDSMVLGEAQ ILGQMKDAVR AAETAGALGT TLNQLFQRSF 150
    AVAKEVRTST EIGAHSISMA AAAVRLAGQL FEDLTEIRIL FVGAGEMIEL 200
    AATHFAAKNP KSLAIANRTL ERGEKLASRF GGEVMRLADL PDRLHEFDAV 250
    VSCTASSLPI IGLGAVERAL KKRRHRPMFM VDLAVPRDIE PEVKALEDIY 300
    LYTVDDLASV VQTAQASRQA AVAQAEAIID AGVQSFMHWM DQRSPVGGVV 350
    PLIQQIHAQA DEWRALEIAR AKKLIARGED MDAVLEALSR GLTQKMLHGT 400
    LAELRAGDAD TRAQTAQTVS RLFLRSQSRS GL 432
    Length:432
    Mass (Da):46,734
    Last modified:February 6, 2007 - v1
    Checksum:iF1AF378B845BE924
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000512 Genomic DNA. Translation: ABM34211.1.
    RefSeqiWP_011796705.1. NC_008752.1.
    YP_971985.1. NC_008752.1.

    Genome annotation databases

    EnsemblBacteriaiABM34211; ABM34211; Aave_3663.
    GeneIDi4665154.
    KEGGiaav:Aave_3663.
    PATRICi20682495. VBIAciCit38535_3716.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000512 Genomic DNA. Translation: ABM34211.1 .
    RefSeqi WP_011796705.1. NC_008752.1.
    YP_971985.1. NC_008752.1.

    3D structure databases

    ProteinModelPortali A1TTC3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 397945.Aave_3663.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM34211 ; ABM34211 ; Aave_3663 .
    GeneIDi 4665154.
    KEGGi aav:Aave_3663.
    PATRICi 20682495. VBIAciCit38535_3716.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ACIT397945:GI5W-3706-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 Acidovorax avenae subsp. citrulli AAC00-1."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AAC00-1.

    Entry informationi

    Entry nameiHEM1_ACIAC
    AccessioniPrimary (citable) accession number: A1TTC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 68 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