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A5FLE3

- HEM11_FLAJ1

UniProt

A5FLE3 - HEM11_FLAJ1

Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (12 Jun 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 sitei58 – 581NucleophileUniRule annotation
    Sitei103 – 1031Important for activityUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule annotation
    Binding sitei124 – 1241SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi193 – 1986NADPUniRule 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

    BioCyciFJOH376686:GIXN-963-MONOMER.
    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
    Short name:
    GluTR 1UniRule annotation
    Gene namesi
    Name:hemA1UniRule annotation
    Ordered Locus Names:Fjoh_0942
    OrganismiFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae)
    Taxonomic identifieri376686 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium
    ProteomesiUP000006694: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Glutamyl-tRNA reductase 1PRO_0000335032Add
    BLAST

    Proteomic databases

    PRIDEiA5FLE3.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi376686.Fjoh_0942.

    Structurei

    3D structure databases

    ProteinModelPortaliA5FLE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni57 – 604Substrate bindingUniRule annotation
    Regioni118 – 1203Substrate 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.
    HOGENOMiHOG000251726.
    KOiK02492.
    OMAiSETNISC.
    OrthoDBiEOG6QG8G0.

    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.

    A5FLE3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENNNVPKHL YFYSVGLSYK KADAEVRGQF SLDAVAKTRL LEQAKNDGIE    50
    SLLVTSTCNR TEIYGFAEHP FQLIKLICDN SNGSVDAFQK VGFVYKNQEA 100
    INHMFRVGTG LDSQILGDFE IISQIKTSFT HSKSMGLANA FMERLVNAVI 150
    QASKRIKTET EISSGATSVS FASVQYILKN VEDISNKNIL LFGTGKIGRN 200
    TCENLVKHTK NEHITLINRT KDKAEKLAGK LNLIVKDYSE LHLELQKADV 250
    VVVATGAQNP TVDKAILNLK KPLLILDLSI PKNVNENVEE LEGVTLIHMD 300
    YLSQLTDETL ENRKLHIPAA EAIIEEIKEE FVTWMKGRKF APTINALKEK 350
    LNAIKASELD FQSKKIADFN EEQAEIISNR IIQKITTHFA NHLKDDDTMV 400
    DESIEWIEKV FKIKAS 416
    Length:416
    Mass (Da):46,757
    Last modified:June 12, 2007 - v1
    Checksum:i3C213457520C9667
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000685 Genomic DNA. Translation: ABQ03976.1.
    RefSeqiYP_001193295.1. NC_009441.1.

    Genome annotation databases

    EnsemblBacteriaiABQ03976; ABQ03976; Fjoh_0942.
    GeneIDi5091356.
    KEGGifjo:Fjoh_0942.
    PATRICi21896167. VBIFlaJoh53613_0968.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000685 Genomic DNA. Translation: ABQ03976.1 .
    RefSeqi YP_001193295.1. NC_009441.1.

    3D structure databases

    ProteinModelPortali A5FLE3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 376686.Fjoh_0942.

    Proteomic databases

    PRIDEi A5FLE3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ03976 ; ABQ03976 ; Fjoh_0942 .
    GeneIDi 5091356.
    KEGGi fjo:Fjoh_0942.
    PATRICi 21896167. VBIFlaJoh53613_0968.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000251726.
    KOi K02492.
    OMAi SETNISC.
    OrthoDBi EOG6QG8G0.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci FJOH376686:GIXN-963-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. "Novel features of the polysaccharide-digesting gliding bacterium Flavobacterium johnsoniae as revealed by genome sequence analysis."
      McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., Cheng Y.Q., Stein J.L.
      Appl. Environ. Microbiol. 75:6864-6875(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17061 / DSM 2064 / UW101.

    Entry informationi

    Entry nameiHEM11_FLAJ1
    AccessioniPrimary (citable) accession number: A5FLE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 65 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