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B2IA84

- HEM1_XYLF2

UniProt

B2IA84 - HEM1_XYLF2

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Xylella fastidiosa (strain M23)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      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
    Sitei91 – 911Important for activityUniRule annotation
    Binding sitei101 – 1011SubstrateUniRule annotation
    Binding sitei112 – 1121SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi181 – 1866NADPUniRule 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

    BioCyciXFAS405441:GJJI-2172-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:XfasM23_2122
    OrganismiXylella fastidiosa (strain M23)
    Taxonomic identifieri405441 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella
    ProteomesiUP000001698: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Glutamyl-tRNA reductasePRO_1000093179Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi405441.XfasM23_2122.

    Structurei

    3D structure databases

    ProteinModelPortaliB2IA84.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni106 – 1083Substrate 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.
    OMAiLAHKLTN.
    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.
    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.

    B2IA84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLWVLGLNH QTAPMELRER ASFVGDALPR ALDSLRNLPN VNEAALLSTC    50
    NRTELYAETT NAQMLLNWLE QHRPGLQNHL YQYRDAAAVR HLFRVATGLD 100
    SMVLGESQIL GQVKDSWSMA RTHGTLGNTL DRLFQHSFSV AKHARTNTRI 150
    GTNPVSIAST AVRLAQDAFS PLNESTVLLI GAGETIQLAA KHLSEGRVQR 200
    LLIANRTHAK AQMLASQHGG YALPLTELNL HLAEADIIFS ATAAPTPIVT 250
    QSNVESALHI RKRKPILLFD LAIPRDIETE VGTLTDAYLY TIDDLERAVE 300
    ENRHSRREAA ETAEAIIELQ VKRYMDTLQA QAHQAPLRRL RTFGTTTRDE 350
    LLTRARRQLA NGRPAEEVLE QLAHGLTNRL LHPPTAALRE AALANNTELV 400
    RAAEQLFPEK PGYHHPTLQT TIVKTDETDP AS 432
    Length:432
    Mass (Da):47,966
    Last modified:June 10, 2008 - v1
    Checksum:i7335D2E946015C84
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001011 Genomic DNA. Translation: ACB93520.1.
    RefSeqiYP_001830794.1. NC_010577.1.

    Genome annotation databases

    EnsemblBacteriaiACB93520; ACB93520; XfasM23_2122.
    GeneIDi6203196.
    KEGGixfn:XfasM23_2122.
    PATRICi24146967. VBIXylFas85937_2636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001011 Genomic DNA. Translation: ACB93520.1 .
    RefSeqi YP_001830794.1. NC_010577.1.

    3D structure databases

    ProteinModelPortali B2IA84.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405441.XfasM23_2122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB93520 ; ACB93520 ; XfasM23_2122 .
    GeneIDi 6203196.
    KEGGi xfn:XfasM23_2122.
    PATRICi 24146967. VBIXylFas85937_2636.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci XFAS405441:GJJI-2172-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. "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
      Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
      J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: M23.

    Entry informationi

    Entry nameiHEM1_XYLF2
    AccessioniPrimary (citable) accession number: B2IA84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 50 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3