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P0C543

- HEM1_CORGL

UniProt

P0C543 - HEM1_CORGL

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (26 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 sitei50 – 501NucleophileUniRule annotation
    Sitei99 – 991Important for activityUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2016NADPUniRule 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

    BioCyciCGLU196627:GJDM-420-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:Cgl0417, cg0497
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Glutamyl-tRNA reductasePRO_0000114017Add
    BLAST

    Proteomic databases

    PRIDEiP0C543.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi196627.cg0497.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C543.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni114 – 1163Substrate 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.

    P0C543-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVLIVGMSH RSAPVSLLER LSMDDSVRGE TTQALLGRAS LSEALIVSTC    50
    NRLEVYTVTS SFHTGVNDVV EVLHEASGVD IETLRGYLYV RYADAAAEHM 100
    LVVTSGLDSM VLGEQQIIGQ VRTAYQAANE YGSVGPALHS LTQTALHTGK 150
    RVHSETAIDD AGASMVSFAV DRALVQMGLD SEAEAPLSGK TALVLGAGAM 200
    SSLAATHLGR AGISNLIMAN RTLERAERLA EHSLEAGVPA EVVEYDQRAS 250
    AYNRVDLVVS ATGADDFTVK PEDIPEGASL MLVDLSMPRD IDDACADLPG 300
    VDLVNIERLH KASREGGSGM APSEEEALAI VREELDSFTS EQRIRDIVPA 350
    VSALRRQAAS VGSDELDRLR QRAPGISEVE WGEVEKTVRR VVDKLLHEPT 400
    VRVKELAARS GSISYDSALQ ELFGLESLAS TAAPATTSVN ASELPDAGIV 450
    AFVNAPSATQ TRE 463
    Length:463
    Mass (Da):49,216
    Last modified:June 26, 2007 - v1
    Checksum:i89059D1B1C481E9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB97810.1.
    BX927149 Genomic DNA. Translation: CAF19133.1.
    RefSeqiNP_599664.2. NC_003450.3.
    YP_224719.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB97810; BAB97810; BAB97810.
    CAF19133; CAF19133; cg0497.
    GeneIDi1021437.
    KEGGicgb:cg0497.
    cgl:NCgl0402.
    PATRICi21492888. VBICorGlu203724_0415.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB97810.1 .
    BX927149 Genomic DNA. Translation: CAF19133.1 .
    RefSeqi NP_599664.2. NC_003450.3.
    YP_224719.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali P0C543.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg0497.

    Proteomic databases

    PRIDEi P0C543.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB97810 ; BAB97810 ; BAB97810 .
    CAF19133 ; CAF19133 ; cg0497 .
    GeneIDi 1021437.
    KEGGi cgb:cg0497.
    cgl:NCgl0402.
    PATRICi 21492888. VBICorGlu203724_0415.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CGLU196627:GJDM-420-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 Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
      Ikeda M., Nakagawa S.
      Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    Entry informationi

    Entry nameiHEM1_CORGL
    AccessioniPrimary (citable) accession number: P0C543
    Secondary accession number(s): Q8GMZ2, Q8NT91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 61 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