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Q11Y93

- HEM1_CYTH3

UniProt

Q11Y93 - HEM1_CYTH3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
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 (22 Aug 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 sitei52 – 521NucleophileUniRule annotation
    Sitei101 – 1011Important for activityUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation
    Binding sitei122 – 1221SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi191 – 1966NADPUniRule 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

    BioCyciCHUT269798:GJ83-343-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:CHU_0333
    OrganismiCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
    Taxonomic identifieri269798 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga
    ProteomesiUP000001822: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 425425Glutamyl-tRNA reductasePRO_0000335025Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi269798.CHU_0333.

    Structurei

    3D structure databases

    ProteinModelPortaliQ11Y93.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 544Substrate bindingUniRule annotation
    Regioni116 – 1183Substrate 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.
    HOGENOMiHOG000109637.
    KOiK02492.
    OMAiVANGVHR.
    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.

    Q11Y93-1 [UniParc]FASTAAdd to Basket

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    MISNFKSISL TYRKAPLEIR ERVALNEAEC KSLMLRIKDF TDTAELLILS    50
    TCNRTEIYYT SNEDYSNDII KLLGVEKNIT GLIQQKEYFE IYNEQADAVL 100
    HLFEVGIGLD SQVVGDMQIV NQVKYAYQWS ADLNLAGPFL HRLMHTIFFT 150
    NKRVVQETAF RDGAASVSYA TVELSEELLS ATPNANILIV GLGEIGADVC 200
    RNFKANTSFK NITLTNRSPL KSEALAAECG IEHVPFETLW EAVAKADLVI 250
    SSVAKEEPLF TKEEIQKLSI LSHKYFIDLS VPRSVDARAE ELPGIIVYDI 300
    DHIQNRSNEA LENRLNAIPH VRKIILDSIV EFNEWSKEME VSPTINKLKN 350
    ALEQIRKEEL SRFVKQLSDE EAKKVDEITK SIMQKIIKLP VLQLKAACKR 400
    GEAETLIDVL NDLFNLDKQP EQIRD 425
    Length:425
    Mass (Da):48,224
    Last modified:August 22, 2006 - v1
    Checksum:iFFB74CC964E8F1FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000383 Genomic DNA. Translation: ABG57623.1.
    RefSeqiYP_676963.1. NC_008255.1.

    Genome annotation databases

    EnsemblBacteriaiABG57623; ABG57623; CHU_0333.
    GeneIDi4185515.
    KEGGichu:CHU_0333.
    PATRICi21591493. VBICytHut34013_0324.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000383 Genomic DNA. Translation: ABG57623.1 .
    RefSeqi YP_676963.1. NC_008255.1.

    3D structure databases

    ProteinModelPortali Q11Y93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 269798.CHU_0333.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG57623 ; ABG57623 ; CHU_0333 .
    GeneIDi 4185515.
    KEGGi chu:CHU_0333.
    PATRICi 21591493. VBICytHut34013_0324.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109637.
    KOi K02492.
    OMAi VANGVHR.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CHUT269798:GJ83-343-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33406 / NCIMB 9469.

    Entry informationi

    Entry nameiHEM1_CYTH3
    AccessioniPrimary (citable) accession number: Q11Y93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: August 22, 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, 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