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)

A9WPH1

- HEM1_RENSM

UniProt

A9WPH1 - HEM1_RENSM

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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 sitei41 – 411NucleophileUniRule annotation
    Sitei90 – 901Important for activityUniRule annotation
    Binding sitei100 – 1001SubstrateUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule 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

    BioCyciRSAL288705:GHX1-1218-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:RSal33209_1218
    OrganismiRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235)
    Taxonomic identifieri288705 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium
    ProteomesiUP000002007: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440Glutamyl-tRNA reductasePRO_0000335064Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi288705.RSal33209_1218.

    Structurei

    3D structure databases

    ProteinModelPortaliA9WPH1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni40 – 434Substrate bindingUniRule annotation
    Regioni105 – 1073Substrate 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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiPYLYVHY.

    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.

    A9WPH1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVVVLFSLV ATHADIDLET VARLSAGSAA VSTSTVVLAT CNRFEIYSAA    50
    ENPATARAEM EAALAHATGF APSLVSSSFK LLTGTDVAKH LFAVASGLDS 100
    AVVGEREIAG QVRRALIDAQ TAFPVPGPLV RLFQTASRTA KDVGSQTALG 150
    SQGRSIVSVA LDLAGDSSAT AWDQRKAVVF GTGAYAGVTM ALLRERGVSD 200
    LSVYSSSGRA ADFVASRGGT AAESLEEALG SADLVIGCSG SDQRVSAETL 250
    ADIRRRTGTA GEPLSVIDLA LSRDFDPAIT ELPGVELLTL ETVRLAAPSE 300
    QESALLQTQV IVSRAAADFE LSIATRSVDT AIVALRKHTM AVLDAEMERV 350
    RAQHGCTAAA EEVEFALRRM VKQLLHGPTV RARELAAAGQ QAEYIAALQS 400
    LYGIELESPT PAAQPVESIP AVEPASCPVN HNAVDRSQSA 440
    Length:440
    Mass (Da):45,781
    Last modified:February 5, 2008 - v1
    Checksum:iD97066F78C188072
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000910 Genomic DNA. Translation: ABY22956.1.
    RefSeqiWP_012244642.1. NC_010168.1.
    YP_001624370.1. NC_010168.1.

    Genome annotation databases

    EnsemblBacteriaiABY22956; ABY22956; RSal33209_1218.
    GeneIDi5822473.
    KEGGirsa:RSal33209_1218.
    PATRICi23075677. VBIRenSal21953_1259.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000910 Genomic DNA. Translation: ABY22956.1 .
    RefSeqi WP_012244642.1. NC_010168.1.
    YP_001624370.1. NC_010168.1.

    3D structure databases

    ProteinModelPortali A9WPH1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 288705.RSal33209_1218.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABY22956 ; ABY22956 ; RSal33209_1218 .
    GeneIDi 5822473.
    KEGGi rsa:RSal33209_1218.
    PATRICi 23075677. VBIRenSal21953_1259.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi PYLYVHY.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci RSAL288705:GHX1-1218-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. "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
      Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
      J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

    Entry informationi

    Entry nameiHEM1_RENSM
    AccessioniPrimary (citable) accession number: A9WPH1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 54 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