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A6VND5

- HEM1_ACTSZ

UniProt

A6VND5 - HEM1_ACTSZ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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
    Sitei104 – 1041Important for activityUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation
    Binding sitei125 – 1251SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi204 – 2096NADPUniRule 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

    BioCyciASUC339671:GHDX-1180-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:Asuc_1116
    OrganismiActinobacillus succinogenes (strain ATCC 55618 / 130Z)
    Taxonomic identifieri339671 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
    ProteomesiUP000001114: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Glutamyl-tRNA reductasePRO_1000071245Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi339671.Asuc_1116.

    Structurei

    3D structure databases

    ProteinModelPortaliA6VND5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni119 – 1213Substrate 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.

    A6VND5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTILVLGINH KTATVALREK VAFSEEKRLS ALNQIEQLKL AQSTVILSTC    50
    NRTEVYLHNK FIQPEQNSAW IDECVAWFAA IHQIQLTDLQ DCLYFYQNQQ 100
    AVTHLMRVAC GLDSLILGEP QILGQVKQAY QLAEEYYQRA HGLGKSAVIS 150
    SELSRLFQKT FSTAKRVRTE TNIGESAVSV AYAACSLGRQ IFESLQELTI 200
    LLVGAGETIE LAARHLLRHG VKKLMIANRT RARAEALVAK LESPFIEILS 250
    LSELQDGLNQ ADIVISSTGS PTTLISYEMM KQAQIQRRYR PVLIVDIAVP 300
    RDVEESIVKL DSVYHYTVDD LQNIINHNLS EREKASEQAE EIIAEECAAF 350
    FEWLKVRQAS NLIRTYRESA DEIRQELLEK AQFSLSQGES ADKILDEFST 400
    KLMNKLLHSP TLVMQTMVKQ GDSRGLQNFL SVIKK 435
    Length:435
    Mass (Da):49,073
    Last modified:August 21, 2007 - v1
    Checksum:iF6A876382802D60B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000746 Genomic DNA. Translation: ABR74482.1.
    RefSeqiYP_001344417.1. NC_009655.1.

    Genome annotation databases

    EnsemblBacteriaiABR74482; ABR74482; Asuc_1116.
    GeneIDi5348066.
    KEGGiasu:Asuc_1116.
    PATRICi20760606. VBIActSuc117883_1182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000746 Genomic DNA. Translation: ABR74482.1 .
    RefSeqi YP_001344417.1. NC_009655.1.

    3D structure databases

    ProteinModelPortali A6VND5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 339671.Asuc_1116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR74482 ; ABR74482 ; Asuc_1116 .
    GeneIDi 5348066.
    KEGGi asu:Asuc_1116.
    PATRICi 20760606. VBIActSuc117883_1182.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci ASUC339671:GHDX-1180-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. "A genomic perspective on the potential of Actinobacillus succinogenes for industrial succinate production."
      McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., Burkhart K.B., Harkins V., Vieille C.
      BMC Genomics 11:680-680(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 55618 / 130Z.

    Entry informationi

    Entry nameiHEM1_ACTSZ
    AccessioniPrimary (citable) accession number: A6VND5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 56 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