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B9L0Q1

- HEM1_THERP

UniProt

B9L0Q1 - HEM1_THERP

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (24 Mar 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
    Sitei97 – 971Important for activityUniRule annotation
    Binding sitei107 – 1071SubstrateUniRule annotation
    Binding sitei118 – 1181SubstrateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi187 – 1926NADPUniRule 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

    BioCyciTROS309801:GI0S-1110-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:trd_1122
    OrganismiThermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2)
    Taxonomic identifieri309801 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiThermomicrobialesThermomicrobiaceaeThermomicrobium
    ProteomesiUP000000447: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 406406Glutamyl-tRNA reductasePRO_1000190542Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi309801.trd_1122.

    Structurei

    3D structure databases

    ProteinModelPortaliB9L0Q1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 524Substrate bindingUniRule annotation
    Regioni112 – 1143Substrate 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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiNISRGPR.
    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]
    SUPFAMiSSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B9L0Q1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTMTLSVVAV THRTAPVTIR ERLSLPVEQQ CQWLQRWGNQ VPEIVLLVTC    50
    HRTEVYWLDG EETAHRGVEW LAELGGLTVE ELERWVLQRS GAEAVRHAFC 100
    VAAGLDSRVV GEPQILGQVR RARDLARAAG TLGPILDRLF SCSLATGRMV 150
    RVRAGWSTGK RSLARVAVRE AARLCSDLQS ARVLVLGAGE TGRDVIAALC 200
    RCQPAVVWWT NRSPGRLAQI PSEEPVRIVD WSEWPRLVTE ADVVFVATNA 250
    PEPIVRLEHV TRHARLPRLL VDLAVPRNVD PAISDVPGIR VVTIDDLPAD 300
    PVPVAAWDGV AVEPYVERAV QRYLRWLEAR SIAAEIRAAH ETLQSMLERE 350
    LEKVLRLALR DPARTGEVKR VAAASMARKT LFPLFRALES EPQRVALALR 400
    LLAYDR 406
    Length:406
    Mass (Da):45,246
    Last modified:March 24, 2009 - v1
    Checksum:iF6684624F5083664
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001275 Genomic DNA. Translation: ACM05350.1.
    RefSeqiWP_015922075.1. NC_011959.1.
    YP_002522331.1. NC_011959.1.

    Genome annotation databases

    EnsemblBacteriaiACM05350; ACM05350; trd_1122.
    GeneIDi7355377.
    KEGGitro:trd_1122.
    PATRICi23913416. VBITheRos91376_1058.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001275 Genomic DNA. Translation: ACM05350.1 .
    RefSeqi WP_015922075.1. NC_011959.1.
    YP_002522331.1. NC_011959.1.

    3D structure databases

    ProteinModelPortali B9L0Q1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 309801.trd_1122.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM05350 ; ACM05350 ; trd_1122 .
    GeneIDi 7355377.
    KEGGi tro:trd_1122.
    PATRICi 23913416. VBITheRos91376_1058.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.
    KOi K02492.
    OMAi NISRGPR.
    OrthoDBi EOG6MWNBM.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    BioCyci TROS309801:GI0S-1110-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 ]
    SUPFAMi SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the aerobic CO-oxidizing thermophile Thermomicrobium roseum."
      Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L., Eisen J.A.
      PLoS ONE 4:E4207-E4207(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27502 / DSM 5159 / P-2.

    Entry informationi

    Entry nameiHEM1_THERP
    AccessioniPrimary (citable) accession number: B9L0Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 48 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