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Q3AQF4

- HEM1_CHLCH

UniProt

Q3AQF4 - HEM1_CHLCH

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlorobium chlorochromatii (strain CaD3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      Previous versions | rss
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    • Comment

    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

    BioCyciCCHL340177:GHBW-1527-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:Cag_1516
    OrganismiChlorobium chlorochromatii (strain CaD3)
    Taxonomic identifieri340177 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium
    ProteomesiUP000002708: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Glutamyl-tRNA reductasePRO_1000004607Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi340177.Cag_1516.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3AQF4.
    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.
    OMAiSETNISC.
    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.

    Q3AQF4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIISVGVNH KTAPIEIRER ISLSEVQNKE FITGLVSSGL AHEAMVLSTC    50
    NRTELYVVPA MHEVTGEFLK EYLISYRDAR KEVRPEHFFS RFYCSTARHL 100
    FEVASAIDSL VLGEGQILGQ VKNAYRIAAE AQCAGIMITR LCHTAFSVAK 150
    KVKTKTRIME GAVSVSYAAV ELAQKIFSNL SLKKVLLVGA GETGELAAKH 200
    MFAKNARNIV ITNRTISKAE ALAEELGTNQ VLPYESYKEH LHEFDIIITA 250
    VSTKDYALTE ADMQPAMARR KLKPVIILDL GLPRNVDPNI SKLQNMFLKD 300
    IDDLKHIIDK NLEKRRRELP KVHAIIEEEL IAFGQWINTL KVRPTIVDLQ 350
    SKFIEIKEKE LERYRYKVSE EELQRMEHLT DRILKKILHH PIKMLKAPID 400
    TTDSIPSRVN LVRNVFDLEE PNQSHF 426
    Length:426
    Mass (Da):48,479
    Last modified:November 22, 2005 - v1
    Checksum:i44FE3ABFCC05A77E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000108 Genomic DNA. Translation: ABB28771.1.
    RefSeqiYP_379814.1. NC_007514.1.

    Genome annotation databases

    EnsemblBacteriaiABB28771; ABB28771; Cag_1516.
    GeneIDi3747149.
    KEGGicch:Cag_1516.
    PATRICi21370739. VBIChlChl46571_1572.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000108 Genomic DNA. Translation: ABB28771.1 .
    RefSeqi YP_379814.1. NC_007514.1.

    3D structure databases

    ProteinModelPortali Q3AQF4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 340177.Cag_1516.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB28771 ; ABB28771 ; Cag_1516 .
    GeneIDi 3747149.
    KEGGi cch:Cag_1516.
    PATRICi 21370739. VBIChlChl46571_1572.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .
    BioCyci CCHL340177:GHBW-1527-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 sequence of Chlorobium chlorochromatii CaD3."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CaD3.

    Entry informationi

    Entry nameiHEM1_CHLCH
    AccessioniPrimary (citable) accession number: Q3AQF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 72 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