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A4QB58

- HEM1_CORGB

UniProt

A4QB58 - HEM1_CORGB

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium glutamicum (strain R)
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 2 (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

    BioCyciCGLU340322:GJBE-511-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:cgR_0488
    OrganismiCorynebacterium glutamicum (strain R)
    Taxonomic identifieri340322 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000006698: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Glutamyl-tRNA reductasePRO_0000291541Add
    BLAST

    Proteomic databases

    PRIDEiA4QB58.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi340322.cgR_0488.

    Structurei

    3D structure databases

    ProteinModelPortaliA4QB58.
    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.
    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.

    A4QB58-1 [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 AGISKLIMAN RTLERAERLA EHSLEAGVPA EVVEYDQRAS 250
    AYNRVDLVVS ATGADDFTVK PEDIPEGASL MLVDLSMPRD IDDACADLPG 300
    VDLVNIERLH KASREGGSGM APSEEEALAI VREELDSFTS EQRIRDIVPA 350
    VSALRRQAAS VGSDELDRLR QRAPGISEVE WGEVEKTVRR VVDKLLHQPT 400
    VRVKELAARS GSISYDSALQ ELFGLESLAS TAAPATTSVN ASELPDAGIV 450
    AFVNAPSATQ TRE 463
    Length:463
    Mass (Da):49,229
    Last modified:June 26, 2007 - v2
    Checksum:i884940DB03E5DE9D
    GO

    Sequence cautioni

    The sequence BAF53455.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF545862 Genomic DNA. Translation: AAN38289.1.
    AP009044 Genomic DNA. Translation: BAF53455.1. Different initiation.
    RefSeqiYP_001137357.1. NC_009342.1.

    Genome annotation databases

    EnsemblBacteriaiBAF53455; BAF53455; cgR_0488.
    GeneIDi4994524.
    KEGGicgt:cgR_0488.
    PATRICi21505461. VBICorGlu58097_0510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF545862 Genomic DNA. Translation: AAN38289.1 .
    AP009044 Genomic DNA. Translation: BAF53455.1 . Different initiation.
    RefSeqi YP_001137357.1. NC_009342.1.

    3D structure databases

    ProteinModelPortali A4QB58.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 340322.cgR_0488.

    Proteomic databases

    PRIDEi A4QB58.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAF53455 ; BAF53455 ; cgR_0488 .
    GeneIDi 4994524.
    KEGGi cgt:cgR_0488.
    PATRICi 21505461. VBICorGlu58097_0510.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci CGLU340322:GJBE-511-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. "Evolutionary considerations on the heme biosynthetic pathway of Corynebacteria and Mycobacteria."
      Vertes A.A., Kos P.B., Inui M., Yukawa H.
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
      Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
      Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: R.

    Entry informationi

    Entry nameiHEM1_CORGB
    AccessioniPrimary (citable) accession number: A4QB58
    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 57 of the entry and version 2 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