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Q2LQU3

- HEM1_SYNAS

UniProt

Q2LQU3 - HEM1_SYNAS

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Syntrophus aciditrophicus (strain SB)
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 2 (20 May 2008)
      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 sitei50 – 501NucleophileUniRule annotation
    Sitei101 – 1011Important for activityUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation
    Binding sitei122 – 1221SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi191 – 1966NADPUniRule 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

    BioCyciSACI56780:GHXT-583-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:SYNAS_05720
    ORF Names:SYN_02274
    OrganismiSyntrophus aciditrophicus (strain SB)
    Taxonomic identifieri56780 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus
    ProteomesiUP000001933: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 423423Glutamyl-tRNA reductasePRO_0000335076Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi56780.SYN_02274.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2LQU3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni116 – 1183Substrate 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.
    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.

    Q2LQU3-1 [UniParc]FASTAAdd to Basket

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    MGILLIGMSH KTSPLAVRER FSLSCENRDH PLDRIRQMPS IREALYLATC    50
    NRVEVLVSAA EEAEQAVEEG LKALMAERGG ISGQELERCL YTLSGAEAVR 100
    HLFRVASSLD SLVMGEPQIL GQVKEAYREA VEHGVTGILL NRILHHAFQV 150
    AKRVRTETGI ADNAVSVGYA AVELAKKIFG RLDGKVILLV GAGEMSELAA 200
    RHLLKQGIKS IFVANRTHAR ALEMAEQFEG KAVVLEQVPE VLKSVDIVIS 250
    STGASNYVLT RDMVAAALRR RKNRFLFLID IAVPRDIEPA AGDIDNVYLY 300
    NIDHLQELVD ENRNHRLREA EKAEAIIEEE VGNHTAWLST LDVVPTIVEF 350
    REKIEGIMKA ELGKSASWRH SLSEIDQRHV ESLMASIVNK ILHEPTACLR 400
    EQSRNRNGKA YAAALRKLFK LER 423
    Length:423
    Mass (Da):47,114
    Last modified:May 20, 2008 - v2
    Checksum:iFD4811CCA61A5ED5
    GO

    Sequence cautioni

    The sequence ABC76451.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000252 Genomic DNA. Translation: ABC76451.1. Different initiation.
    RefSeqiYP_460619.1. NC_007759.1.

    Genome annotation databases

    EnsemblBacteriaiABC76451; ABC76451; SYN_02274.
    GeneIDi3885135.
    KEGGisat:SYN_02274.
    PATRICi23861605. VBISynAci70500_0623.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000252 Genomic DNA. Translation: ABC76451.1 . Different initiation.
    RefSeqi YP_460619.1. NC_007759.1.

    3D structure databases

    ProteinModelPortali Q2LQU3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 56780.SYN_02274.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABC76451 ; ABC76451 ; SYN_02274 .
    GeneIDi 3885135.
    KEGGi sat:SYN_02274.
    PATRICi 23861605. VBISynAci70500_0623.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci SACI56780:GHXT-583-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. "The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
      Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SB.

    Entry informationi

    Entry nameiHEM1_SYNAS
    AccessioniPrimary (citable) accession number: Q2LQU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 68 of the entry and version 2 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