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C3PKG1

- HEM1_CORA7

UniProt

C3PKG1 - HEM1_CORA7

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) (Corynebacterium nigricans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (16 Jun 2009)
      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 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

    BioCyciCAUR548476:GH9E-309-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:cauri_0298
    OrganismiCorynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) (Corynebacterium nigricans)
    Taxonomic identifieri548476 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000002077: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Glutamyl-tRNA reductasePRO_1000190514Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi169292.cauri_0298.

    Structurei

    3D structure databases

    ProteinModelPortaliC3PKG1.
    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.

    C3PKG1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVLVVGMSH QSAPVALLEK LSMDETVQND TCRAMVSAGS LSEAMIISTC    50
    NRLEVYTVTN SFHSGVQDVV HNLAEVSGVE EEKLRSYLYV RYADAAAEHL 100
    MMVTSGLDSM VVGEQQIIGQ VRTAYQFASE QGTVGPRIHA LAQSALRTGK 150
    RVHSETEIDE AGSSMVSFAF DQALSRMGRE DLAGKRVLIL GAGAMASLAA 200
    THAGRLGAHL IIANRTIARA ERVAQHAHEA GVYADVIDFS ERAQALRDVD 250
    VAISATGAQG FTITAADVER YHVADRELML VDLSLPRDID DAVAEAEGVD 300
    LINIERLNNS LQAADTDLAA GTSPHAQARR IVSEELESYA SEQRVRDVVP 350
    AVSALRKRAA NLVQCEVARM EQKHPELDER QMGDINRALK RVADKLLHEP 400
    TVRAKQLAAN SGTVSHETAL QELFGLQLEG SGVAVDMAEL PDAAQMEAAE 450
    NTKEEKDA 458
    Length:458
    Mass (Da):49,388
    Last modified:June 16, 2009 - v1
    Checksum:i925C261543213257
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001601 Genomic DNA. Translation: ACP31897.1.
    RefSeqiWP_010189811.1. NZ_ACLH01000069.1.
    YP_002833835.1. NC_012590.1.

    Genome annotation databases

    EnsemblBacteriaiACP31897; ACP31897; cauri_0298.
    GeneIDi7801153.
    KEGGicar:cauri_0298.
    PATRICi21476536. VBICorAur68407_0319.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001601 Genomic DNA. Translation: ACP31897.1 .
    RefSeqi WP_010189811.1. NZ_ACLH01000069.1.
    YP_002833835.1. NC_012590.1.

    3D structure databases

    ProteinModelPortali C3PKG1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 169292.cauri_0298.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACP31897 ; ACP31897 ; cauri_0298 .
    GeneIDi 7801153.
    KEGGi car:cauri_0298.
    PATRICi 21476536. VBICorAur68407_0319.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CAUR548476:GH9E-309-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. "Complete genome sequence and lifestyle of black-pigmented Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a vaginal swab of a woman with spontaneous abortion."
      Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.
      BMC Genomics 11:91-91(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700975 / DSM 44827 / CN-1.

    Entry informationi

    Entry nameiHEM1_CORA7
    AccessioniPrimary (citable) accession number: C3PKG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 41 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