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Q1CUR3

- HEM1_HELPH

UniProt

Q1CUR3 - HEM1_HELPH

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Helicobacter pylori (strain HPAG1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (11 Jul 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 sitei59 – 591NucleophileUniRule annotation
    Sitei111 – 1111Important for activityUniRule annotation
    Binding sitei121 – 1211SubstrateUniRule annotation
    Binding sitei132 – 1321SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi203 – 2086NADPUniRule 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

    BioCyciHPYL357544:GH1F-250-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:HPAG1_0242
    OrganismiHelicobacter pylori (strain HPAG1)
    Taxonomic identifieri357544 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000008835: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 449449Glutamyl-tRNA reductasePRO_1000004627Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi357544.HPAG1_0242.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1CUR3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 614Substrate bindingUniRule annotation
    Regioni126 – 1283Substrate 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.
    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.

    Q1CUR3-1 [UniParc]FASTAAdd to Basket

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    MELETHLSKY FTLAFTHKSM SLEMREKLAI NSSATLKEFL QTIKNHCPNI    50
    KECMVLSTCN RFEIYASLRH GAHANEQKSA LLKILAQNKK MSVSDLEKCV 100
    LMNTDESAVH HVFSVCSSLD SLVVGETQIT GQMKNAYKFA FEEKFCSKDL 150
    TRLLHFAFKC AAKVRNLTGI SKQGVSISSV AVKEALNIFE KERIKDKKAL 200
    VIGLGEMAQL VIKHLLNKQF EALILGRNAA KFEDFIKELE EPKKVSFQNI 250
    ENLNAYINEY ELLFCATSSP HFIVQNSMLK ETIFRRFWFD LAVPRNIEKP 300
    VLDNIFLYSV DDLEPMVKEN VGNRQESRTK AYEIVGLATM EFYQWIQSLE 350
    VEPLIKDLRE LARISAQKEL QKALKKRYVP KEYESNIEKI LHNAFNTFLH 400
    HPTIALKKNA QKEESDVLVG AIKNLFNLDK SNANHAQNLN LYKCEYYEE 449
    Length:449
    Mass (Da):51,652
    Last modified:July 11, 2006 - v1
    Checksum:i0EF2F4F5815F4C74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000241 Genomic DNA. Translation: ABF84309.1.
    RefSeqiYP_626983.1. NC_008086.1.

    Genome annotation databases

    EnsemblBacteriaiABF84309; ABF84309; HPAG1_0242.
    GeneIDi4097976.
    KEGGihpa:HPAG1_0242.
    PATRICi20601807. VBIHelPyl56048_0255.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000241 Genomic DNA. Translation: ABF84309.1 .
    RefSeqi YP_626983.1. NC_008086.1.

    3D structure databases

    ProteinModelPortali Q1CUR3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 357544.HPAG1_0242.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF84309 ; ABF84309 ; HPAG1_0242 .
    GeneIDi 4097976.
    KEGGi hpa:HPAG1_0242.
    PATRICi 20601807. VBIHelPyl56048_0255.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci HPYL357544:GH1F-250-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 complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
      Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
      Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HPAG1.

    Entry informationi

    Entry nameiHEM1_HELPH
    AccessioniPrimary (citable) accession number: Q1CUR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 70 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3