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Q6AB02

- HEM1_PROAC

UniProt

Q6AB02 - HEM1_PROAC

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      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 sitei42 – 421NucleophileUniRule annotation
    Binding sitei102 – 1021SubstrateUniRule annotation
    Binding sitei113 – 1131SubstrateUniRule 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

    BioCyciPACN267747:GHO9-308-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:PPA0307
    OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
    Taxonomic identifieri267747 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
    ProteomesiUP000000603: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Glutamyl-tRNA reductasePRO_0000335059Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi267747.PPA0307.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6AB02.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 444Substrate bindingUniRule annotation
    Regioni107 – 1093Substrate 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.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q6AB02-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVDHAEQGL GVVSEAAAQV DGLGLALTDH PQIRGALVLS TCNRVCLIVE    50
    TSPEAVAQGF DEAALRRCIA DHGANVLAES AQLVCENDAV WRLFRVAAGM 100
    ESMVFGEREV AGQMKRALSE ARREQTVSYT IGHVVEEALK TSRHVATETA 150
    LAAEGRTVVA VGLDLVAQRM DLDGARVLVM GTGSYAGASC AQLSSRGVAE 200
    IQVHSASGRA AGFARRHRVS EALDIDAALA QADLVVTCRG SGVPALSAEA 250
    ARRAVDARRG RDLMVLDLAI SGDVEEPVPA GVEVIDLETI RQAVPASAEA 300
    ERAAAEHIIA TGVRHFAVDL ERRRMAPAVV ALRDVISDLV TAELERLPEE 350
    GSVPVDEVAA SLRRLAASMA HIPSARARMA SEQGLGDRWL NSLSDVLGID 400
    VDIAAPVIDM SSFANADCMT CPVTGLRVED LATDAAPRGE ERTS 444
    Length:444
    Mass (Da):46,740
    Last modified:September 13, 2004 - v1
    Checksum:i5A500F3FE40A90AD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017283 Genomic DNA. Translation: AAT82064.1.
    RefSeqiYP_055022.1. NC_006085.1.

    Genome annotation databases

    EnsemblBacteriaiAAT82064; AAT82064; PPA0307.
    GeneIDi2932189.
    KEGGipac:PPA0307.
    PATRICi23035267. VBIProAcn64440_0318.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017283 Genomic DNA. Translation: AAT82064.1 .
    RefSeqi YP_055022.1. NC_006085.1.

    3D structure databases

    ProteinModelPortali Q6AB02.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267747.PPA0307.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT82064 ; AAT82064 ; PPA0307 .
    GeneIDi 2932189.
    KEGGi pac:PPA0307.
    PATRICi 23035267. VBIProAcn64440_0318.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci PACN267747:GHO9-308-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.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
      Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
      Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KPA171202 / DSM 16379.

    Entry informationi

    Entry nameiHEM1_PROAC
    AccessioniPrimary (citable) accession number: Q6AB02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 74 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