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A5WC75

- HEM1_PSYWF

UniProt

A5WC75 - HEM1_PSYWF

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Psychrobacter sp. (strain PRwf-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (10 Jul 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 sitei48 – 481NucleophileUniRule annotation
    Sitei122 – 1221Important for activityUniRule annotation
    Binding sitei132 – 1321SubstrateUniRule annotation
    Binding sitei143 – 1431SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi212 – 2176NADPUniRule 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

    BioCyciPPRW349106:GHZF-316-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:PsycPRwf_0311
    OrganismiPsychrobacter sp. (strain PRwf-1)
    Taxonomic identifieri349106 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
    ProteomesiUP000001993: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Glutamyl-tRNA reductasePRO_1000071248Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi349106.PsycPRwf_0311.

    Structurei

    3D structure databases

    ProteinModelPortaliA5WC75.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 504Substrate bindingUniRule annotation
    Regioni137 – 1393Substrate 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.
    OMAiLNKQFET.
    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. 2 hits.
    TIGRFAMsiTIGR01035. hemA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A5WC75-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLVVIGVNH KTAPVALRER LAFVGGDIQV AQAQLQQITA GSLIISTCNR    50
    TEIYALAPST QLLANSDAAL SKQSDLSLAD EPVSTVDLTE QLITWLADFK 100
    QVPLEETRPY LYDYVDGQAL THMLRVAAGL DSMILGEPQI FGQIKRSVNQ 150
    AKEQGFLTNQ LNWVVEQIFA AAKRVRNETD VGTQAISLGY AASKLVTQIF 200
    DRPEETTFLL IAAGEMNRLV AQNIAGLGVK RILICNRTPE RANLLAQELA 250
    HLGIQIEVHP LTELDSLLYQ ADIVSSCSGS MDMLIDKAMT RRALKKRRYK 300
    PMLMVDLAVP RDIDSSVGKL DDVYLYSIDD LQHVIAGNLE KRRQAAVEAE 350
    LLVSHLVVEI ERRFQVRKVG QDIHDYRALA AQKAEAVLNE ALHELRTSEA 400
    TAEEVMTELT RRLTQTLVHA PSSLMRRAAR DGNNEAIDLI ILGLKDAYRK 450
    K 451
    Length:451
    Mass (Da):50,055
    Last modified:July 10, 2007 - v1
    Checksum:i5CC9E2785FFB4E97
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ93266.1.
    RefSeqiWP_011959600.1. NC_009524.1.
    YP_001279216.1. NC_009524.1.

    Genome annotation databases

    EnsemblBacteriaiABQ93266; ABQ93266; PsycPRwf_0311.
    GeneIDi5204520.
    KEGGiprw:PsycPRwf_0311.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000713 Genomic DNA. Translation: ABQ93266.1 .
    RefSeqi WP_011959600.1. NC_009524.1.
    YP_001279216.1. NC_009524.1.

    3D structure databases

    ProteinModelPortali A5WC75.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349106.PsycPRwf_0311.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ93266 ; ABQ93266 ; PsycPRwf_0311 .
    GeneIDi 5204520.
    KEGGi prw:PsycPRwf_0311.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PPRW349106:GHZF-316-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. 2 hits.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PRwf-1.

    Entry informationi

    Entry nameiHEM1_PSYWF
    AccessioniPrimary (citable) accession number: A5WC75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 61 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