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Q93ST4

- HEM1_CHLTE

UniProt

Q93ST4 - HEM1_CHLTE

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (30 Aug 2002)
      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 bindingi189 – 1946NADPUniRule annotation

    GO - Molecular functioni

    1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciCTEP194439:GHN0-1465-MONOMER.
    UniPathwayiUPA00251; UER00316.
    UPA00668.

    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:CT1426
    OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
    Taxonomic identifieri194439 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
    ProteomesiUP000001007: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Glutamyl-tRNA reductasePRO_0000114007Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi194439.CT1426.

    Structurei

    3D structure databases

    ProteinModelPortaliQ93ST4.
    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.
    HOGENOMiHOG000109651.
    KOiK02492.
    OMAiLAHKLTN.
    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.

    Q93ST4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIISVGVNH KTAPIEIRER IALSEVQNKE LVTDLVSSGL ASEAMVVSTC    50
    NRTELYVVPG MPEVNCDYLK DYIISYKNAR NAVRPEHFFS RFYCGTARHL 100
    FEVSCAIDSL VLGEGQILGQ VKNAYRIAAE VGTAGILLTR LCHTAFSVAK 150
    KVKTRTKLME GAVSVSYAAV ELAQKIFSNL SMKKVLLIGA GETGELAAKH 200
    MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH LHEFDIIITA 250
    VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 300
    IDALKHIIDK NLERRRAELP KVKAIIDEEL VAFGQWLNTL KVRPTIVDLQ 350
    SKFLEIKEKE LERYRYKVSE EELRRMEHLT DRILKKILHH PIKMLKAPVD 400
    TADNIPSKVN LVRNIFDLEE PNQSLQ 426
    Length:426
    Mass (Da):48,133
    Last modified:August 30, 2002 - v2
    Checksum:iA7122C2C947D2429
    GO

    Sequence cautioni

    The sequence AAG12432.1 differs from that shown. Reason: Frameshift at position 319.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY005138 Genomic DNA. Translation: AAG12432.1. Frameshift.
    AE006470 Genomic DNA. Translation: AAM72654.1.
    RefSeqiNP_662312.1. NC_002932.3.
    WP_010933093.1. NC_002932.3.

    Genome annotation databases

    EnsemblBacteriaiAAM72654; AAM72654; CT1426.
    GeneIDi1006241.
    KEGGicte:CT1426.
    PATRICi21400779. VBIChlTep116050_1294.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY005138 Genomic DNA. Translation: AAG12432.1 . Frameshift.
    AE006470 Genomic DNA. Translation: AAM72654.1 .
    RefSeqi NP_662312.1. NC_002932.3.
    WP_010933093.1. NC_002932.3.

    3D structure databases

    ProteinModelPortali Q93ST4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 194439.CT1426.

    Protocols and materials databases

    DNASUi 1006241.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM72654 ; AAM72654 ; CT1426 .
    GeneIDi 1006241.
    KEGGi cte:CT1426.
    PATRICi 21400779. VBIChlTep116050_1294.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci CTEP194439:GHN0-1465-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. "Molecular evidence for the early evolution of photosynthesis."
      Xiong J., Fischer W.M., Inoue K., Nakahara M., Bauer C.E.
      Science 289:1724-1730(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 49652 / DSM 12025 / TLS.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49652 / DSM 12025 / TLS.

    Entry informationi

    Entry nameiHEM1_CHLTE
    AccessioniPrimary (citable) accession number: Q93ST4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2002
    Last sequence update: August 30, 2002
    Last modified: October 1, 2014
    This is version 102 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, 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