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)

Q6MEC8

- HEM1_PARUW

UniProt

Q6MEC8 - HEM1_PARUW

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Protochlamydia amoebophila (strain UWE25)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 sitei47 – 471NucleophileUniRule annotation
    Sitei93 – 931Important for activityUniRule annotation
    Binding sitei103 – 1031SubstrateUniRule annotation
    Binding sitei114 – 1141SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi183 – 1886NADPUniRule 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

    BioCyciPAMO264201:GH0M-356-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:pc0347
    OrganismiProtochlamydia amoebophila (strain UWE25)
    Taxonomic identifieri264201 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia
    ProteomesiUP000000529: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Glutamyl-tRNA reductasePRO_0000114051Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi264201.pc0347.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6MEC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 494Substrate bindingUniRule annotation
    Regioni108 – 1103Substrate 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.
    HOGENOMiHOG000112883.
    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.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6MEC8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRIGVIGINH KLADLKLRDA LAKACQKRFG ANQSVHDQHH FILLSTCNRT    50
    EVYFSSHDLT ATHSYLLSIL RQDVKEDFDH KLYSFFGMDC FSHLTRVTSG 100
    LDSAIVAETE IQGQVKNAYN LATTFLCLPK ELHFLFQKSM GIAKRIRSEL 150
    HLGRGLPNLE HAILQTGKYF FRNTQQPKIL FVGASEINRK ILHFLKSKQY 200
    SDMTICNRSE IRSKELAILY GLHLLPWCQL DSWHQYDWII FGTKSSEYLI 250
    KPEKNFIPAD NDKLIMDLCV PRNVEPKLGQ NAKITLLNID QINRLLKIRH 300
    RGMTQALIEA ENRVNLATYE HTNRYRQKED SKITIFAASA 340
    Length:340
    Mass (Da):39,232
    Last modified:July 5, 2004 - v1
    Checksum:i93824A5CBA5E3D40
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX908798 Genomic DNA. Translation: CAF23071.1.
    RefSeqiYP_007346.1. NC_005861.1.

    Genome annotation databases

    EnsemblBacteriaiCAF23071; CAF23071; pc0347.
    GeneIDi2779718.
    KEGGipcu:pc0347.
    PATRICi31995996. VBICanPro72727_0353.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX908798 Genomic DNA. Translation: CAF23071.1 .
    RefSeqi YP_007346.1. NC_005861.1.

    3D structure databases

    ProteinModelPortali Q6MEC8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264201.pc0347.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAF23071 ; CAF23071 ; pc0347 .
    GeneIDi 2779718.
    KEGGi pcu:pc0347.
    PATRICi 31995996. VBICanPro72727_0353.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000112883.
    KOi K02492.
    OMAi AETEIQG.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PAMO264201:GH0M-356-MONOMER.

    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.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UWE25.

    Entry informationi

    Entry nameiHEM1_PARUW
    AccessioniPrimary (citable) accession number: Q6MEC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 79 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