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A6TJD3

- HEM1_ALKMQ

UniProt

A6TJD3 - HEM1_ALKMQ

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Alkaliphilus metalliredigens (strain QYMF)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (21 Aug 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 sitei50 – 501NucleophileUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi189 – 1946NADPUniRule 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

    BioCyciAMET293826:GI5P-75-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:Amet_0058
    OrganismiAlkaliphilus metalliredigens (strain QYMF)
    Taxonomic identifieri293826 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus
    ProteomesiUP000001572: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 424424Glutamyl-tRNA reductasePRO_1000057567Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi293826.Amet_0058.

    Structurei

    3D structure databases

    ProteinModelPortaliA6TJD3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni114 – 1163Substrate 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.
    OMAiAITCGKK.
    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.
    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.

    Sequencei

    Sequence statusi: Complete.

    A6TJD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIIVFGITH KKATIDLREK VAFSQSKKQE AYSLLKESPF IHEAVILSTC    50
    NRSEVFAVVQ DTSIARRWFK RFYTDFFQLK ETALEGCNHF EKGREAVQYL 100
    YHVCVGVDSL VIGEDQILGQ VKEAHAEALD FAATGKILNK LFLEAVTTAK 150
    EVKTETAISE NALSISSIAV KQMENHLKGL VGKTVLVVGF GKMSRIAIEN 200
    LLCKGIKRLY ICNRTKESVQ ELIEKHPQIH YLSYDQKYEM LNGVDAVISA 250
    TGAPHFIFYK EDMEKIYQKH RPMCMIDIAL PRDIDPAVKE IEGIELFHID 300
    DLKEIANENL AYRMDCIEII KQSINEAIEK YEGWYQCLPI YPRIQAIKAY 350
    SETLTDQELE KLFKRLDHMA EEDRQVIEVV VKSLVKKMWK TPILQLKDAG 400
    IRGNGEAFAA FVDEFLGLDA GCGK 424
    Length:424
    Mass (Da):48,297
    Last modified:August 21, 2007 - v1
    Checksum:iAFB0A1080D7E55C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000724 Genomic DNA. Translation: ABR46301.1.
    RefSeqiWP_011971210.1. NC_009633.1.
    YP_001317960.1. NC_009633.1.

    Genome annotation databases

    EnsemblBacteriaiABR46301; ABR46301; Amet_0058.
    GeneIDi5310101.
    KEGGiamt:Amet_0058.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000724 Genomic DNA. Translation: ABR46301.1 .
    RefSeqi WP_011971210.1. NC_009633.1.
    YP_001317960.1. NC_009633.1.

    3D structure databases

    ProteinModelPortali A6TJD3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 293826.Amet_0058.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABR46301 ; ABR46301 ; Amet_0058 .
    GeneIDi 5310101.
    KEGGi amt:Amet_0058.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci AMET293826:GI5P-75-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of Alkaliphilus metalliredigens QYMF."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.
      , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: QYMF.

    Entry informationi

    Entry nameiHEM1_ALKMQ
    AccessioniPrimary (citable) accession number: A6TJD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 55 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