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A5CNH4

- HEM1_CLAM3

UniProt

A5CNH4 - HEM1_CLAM3

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (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 sitei47 – 471NucleophileUniRule 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

    BioCyciCMIC443906:GCI2-606-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:CMM_0586
    OrganismiClavibacter michiganensis subsp. michiganensis (strain NCPPB 382)
    Taxonomic identifieri443906 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter
    ProteomesiUP000001564: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Glutamyl-tRNA reductasePRO_1000004612Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi443906.CMM_0586.

    Structurei

    3D structure databases

    ProteinModelPortaliA5CNH4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 494Substrate 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.
    HOGENOMiHOG000109649.
    KOiK02492.
    OMAiPYLYVHY.
    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.

    A5CNH4-1 [UniParc]FASTAAdd to Basket

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    MLICLTASHH NASFEVLEKL SVAAPSVAGA LMEQNDFIAG AVVLATCNRF    50
    EAYLDVEEPL TAARALAVEA TVDVVSGASG IARDDVRGSV DVKCGDAVAE 100
    HLFAVSSGLE SVVVGEGEIA GQVRRALEGA RTGGTTSTGL ERLFQTASNT 150
    SRGVKTRTGL QSAGRSMVRL ALDLAESRIA DWSATRVLLV GTGAYAGASL 200
    AALRDRGVVD VHVYSPSGRA QKFAGPHGIP AVEGRDLLRA LAASDMVVTC 250
    STAPTAVLAA HHMQGAAAVS GDGRRRLVID LGLPRNVDPD VVTVDGVELL 300
    DLETISLHAP LRDLTATDDA REIVSTAAAE FRAASAEDEV APAVVALRTH 350
    IFDVLEGELE RVRKRGDSSD ATEKALRHLV SVLVHQPSVR ARELARQGEG 400
    ARVVDAVQAL FGLDVEMPAA VSSPVAVALS RTAEAGQAS 439
    Length:439
    Mass (Da):45,607
    Last modified:June 12, 2007 - v1
    Checksum:i9820C8DD238F7EA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM711867 Genomic DNA. Translation: CAN00611.1.
    RefSeqiWP_011931806.1. NC_009480.1.
    YP_001221326.1. NC_009480.1.

    Genome annotation databases

    EnsemblBacteriaiCAN00611; CAN00611; CMM_0586.
    GeneIDi5173135.
    KEGGicmi:CMM_0586.
    PATRICi21451871. VBIClaMic82482_0670.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM711867 Genomic DNA. Translation: CAN00611.1 .
    RefSeqi WP_011931806.1. NC_009480.1.
    YP_001221326.1. NC_009480.1.

    3D structure databases

    ProteinModelPortali A5CNH4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 443906.CMM_0586.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAN00611 ; CAN00611 ; CMM_0586 .
    GeneIDi 5173135.
    KEGGi cmi:CMM_0586.
    PATRICi 21451871. VBIClaMic82482_0670.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109649.
    KOi K02492.
    OMAi PYLYVHY.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CMIC443906:GCI2-606-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. "The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
      Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.
      , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
      J. Bacteriol. 190:2138-2149(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCPPB 382.

    Entry informationi

    Entry nameiHEM1_CLAM3
    AccessioniPrimary (citable) accession number: A5CNH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 57 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