Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q83FI9

- HEM1_TROWT

UniProt

Q83FI9 - HEM1_TROWT

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Tropheryma whipplei (strain Twist) (Whipple's bacillus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei46 – 461NucleophileUniRule 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

    BioCyciTWHI203267:GJDK-786-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:TWT_736
    OrganismiTropheryma whipplei (strain Twist) (Whipple's bacillus)
    Taxonomic identifieri203267 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma
    ProteomesiUP000002200: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447Glutamyl-tRNA reductasePRO_0000114082Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi203267.TWT736.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83FI9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 484Substrate 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.
    KOiK02492.
    OMAiMIICEEL.
    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.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q83FI9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLCVSANHK KTSFTVLEQL ARVSPDFASE LVEAEDIDGA AILSTCNRFE    50
    VYIDAIQKGD QDDVCKTGLL VQNRIGELCN ISPSTIIEQT SFLAGCEVSR 100
    HLFSVATGLE SMIIGETEIA GQVKRALTYA QKCRTTSPEL ERLFQRASAV 150
    NRHIRQSTKI NEVGQSLVSL SLDLASSRIG DWSGVRAIIV GTGKYASKAL 200
    ALLKERGVVD ISVYSPSGHV NNICNTEGVR NIFNLQTALS GCDLVVGCSS 250
    VDKPVITKQD IETAQASGSR TSRVRPVGRP STDLTAIEAS NRSRHVLIDL 300
    GLPRNFDPAI SDLPTADLID LDMLRVHAPF DNLAAEKMAH ELAIESSSQF 350
    VNDCKQHEAT PVIVSFRNYL ESLTQTSLRR TDNCKHAQHA LKHFVNSLIH 400
    IPLTRCKQLA ANGESHKFAE SMEILFDVKT DCTEGTQYQS SCGKSFD 447
    Length:447
    Mass (Da):48,838
    Last modified:June 1, 2003 - v1
    Checksum:i7E5EF8E73584B2F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014184 Genomic DNA. Translation: AAO44833.1.
    RefSeqiNP_787864.1. NC_004572.3.
    WP_011096687.1. NC_004572.3.

    Genome annotation databases

    EnsemblBacteriaiAAO44833; AAO44833; TWT_736.
    GeneIDi1482181.
    KEGGitwh:TWT736.
    PATRICi23998135. VBITroWhi72342_0919.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014184 Genomic DNA. Translation: AAO44833.1 .
    RefSeqi NP_787864.1. NC_004572.3.
    WP_011096687.1. NC_004572.3.

    3D structure databases

    ProteinModelPortali Q83FI9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203267.TWT736.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO44833 ; AAO44833 ; TWT_736 .
    GeneIDi 1482181.
    KEGGi twh:TWT736.
    PATRICi 23998135. VBITroWhi72342_0919.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi MIICEEL.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TWHI203267:GJDK-786-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.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a reduced genome."
      Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M., Claverie J.-M.
      Genome Res. 13:1800-1809(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Twist.

    Entry informationi

    Entry nameiHEM1_TROWT
    AccessioniPrimary (citable) accession number: Q83FI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 88 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