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Q8R687

- HEM1_FUSNN

UniProt

Q8R687 - HEM1_FUSNN

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      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
    Binding sitei99 – 991SubstrateUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1846NADPUniRule 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

    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:FN0646
    OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
    Taxonomic identifieri190304 [NCBI]
    Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
    ProteomesiUP000002521: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Glutamyl-tRNA reductasePRO_0000114027Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi190304.FN0646.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R687.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 544Substrate bindingUniRule annotation
    Regioni104 – 1063Substrate 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.
    HOGENOMiHOG000109108.
    KOiK02492.
    OMAiAETEIQG.
    OrthoDBiEOG6MWNBM.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00087. Glu_tRNA_reductase.
    InterProiIPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLDLENIIVI GVSHENLSLL ERENFMRTRP KYIIERLYTE KKINAYINLS    50
    TCLRTEFYIE LNSNIKAKEI KNLFSVDMIV KSRVEAIEYL FKVGCGFYSV 100
    IKGEDQILAQ VKGAYAEALE NEHSSKFLNI IFNKSIELGK KFRTKSMIAH 150
    NALSLEAISL KFIKSKFPNI EDKNIFILGI GELAQDILTL LTKEQLKNIY 200
    IANRTYHKAE QIKKEFDIVN IVDYREKYPK MIEADVIISA TSAPHIVVEY 250
    DKFVAQMKEN KDYLFIDLAV PRDVDERLAN FKNIEIYNLD DIWEVYHLNS 300
    MNRDKLLEDY SYLIDEQMEK LIKTLNYYK 329
    Length:329
    Mass (Da):38,592
    Last modified:June 1, 2002 - v1
    Checksum:i675E1B115629E9E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009951 Genomic DNA. Translation: AAL94842.1.
    RefSeqiNP_603543.1. NC_003454.1.

    Genome annotation databases

    EnsemblBacteriaiAAL94842; AAL94842; FN0646.
    GeneIDi993220.
    KEGGifnu:FN0646.
    PATRICi21951055. VBIFusNuc122357_1210.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE009951 Genomic DNA. Translation: AAL94842.1 .
    RefSeqi NP_603543.1. NC_003454.1.

    3D structure databases

    ProteinModelPortali Q8R687.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 190304.FN0646.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL94842 ; AAL94842 ; FN0646 .
    GeneIDi 993220.
    KEGGi fnu:FN0646.
    PATRICi 21951055. VBIFusNuc122357_1210.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109108.
    KOi K02492.
    OMAi AETEIQG.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00087. Glu_tRNA_reductase.
    InterProi IPR000343. 4pyrrol_synth_GluRdtase.
    IPR015895. 4pyrrol_synth_GluRdtase_N.
    IPR018214. GluRdtase_CS.
    IPR016040. NAD(P)-bd_dom.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view ]
    Pfami PF05201. GlutR_N. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    [Graphical view ]
    SUPFAMi 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 25586 / CIP 101130 / JCM 8532 / LMG 13131.

    Entry informationi

    Entry nameiHEM1_FUSNN
    AccessioniPrimary (citable) accession number: Q8R687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 86 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

    Caution

    Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue.Curated

    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