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A0KMZ9

- HEM1_AERHH

UniProt

A0KMZ9 - HEM1_AERHH

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (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
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule 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

    BioCyciAHYD380703:GH2M-3149-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:AHA_3150
    OrganismiAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240)
    Taxonomic identifieri380703 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
    ProteomesiUP000000756: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Glutamyl-tRNA reductasePRO_0000335004Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi380703.AHA_3150.

    Structurei

    3D structure databases

    ProteinModelPortaliA0KMZ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    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.

    A0KMZ9-1 [UniParc]FASTAAdd to Basket

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    MSLLALGINH NTASVALRER VAFGPDCIDR ALRELVAQPG VSEAVIVSTC    50
    NRTELYCSLA QGQGEQVLQW LQRFHGLDAA EVVSAIYQHQ DEEAVRHLMR 100
    VACGLDSLVL GEPQILGQIK QSYAHAQQSE AVKGSLERLF QKSFSVAKRV 150
    RTDTEIGASA VSVAFAAVSL GRRIFSDLSQ TKVLLVGAGE TIELVARHLR 200
    EQNVTQMMVA NRTLQRAQLL AEEFGAQVMT LEEIPDYLHE ADIVISSTAS 250
    PLPIIGKGMV ERALKARRFK PMFLVDIAVP RDIEAEVDEL SDAYLYTVDD 300
    LQGIIEQNLE TRKRAAAEAE LIVQEERDDF MGWYRSQHSV DLIRDYRHQS 350
    QQVADEELQR ALLALQQGEN AEQALKALAH RLTNKLIHAP TQALRHAAAQ 400
    GDHHQLAQLR QMLGLSQES 419
    Length:419
    Mass (Da):46,547
    Last modified:May 20, 2008 - v2
    Checksum:iBA5E894610F3841E
    GO

    Sequence cautioni

    The sequence ABK39341.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000462 Genomic DNA. Translation: ABK39341.1. Different initiation.
    RefSeqiYP_857650.1. NC_008570.1.

    Genome annotation databases

    EnsemblBacteriaiABK39341; ABK39341; AHA_3150.
    GeneIDi4489791.
    KEGGiaha:AHA_3150.
    PATRICi20783918. VBIAerHyd135212_3151.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000462 Genomic DNA. Translation: ABK39341.1 . Different initiation.
    RefSeqi YP_857650.1. NC_008570.1.

    3D structure databases

    ProteinModelPortali A0KMZ9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 380703.AHA_3150.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK39341 ; ABK39341 ; AHA_3150 .
    GeneIDi 4489791.
    KEGGi aha:AHA_3150.
    PATRICi 20783918. VBIAerHyd135212_3151.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci AHYD380703:GH2M-3149-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 7966 / NCIB 9240.

    Entry informationi

    Entry nameiHEM1_AERHH
    AccessioniPrimary (citable) accession number: A0KMZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 67 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