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P48077

- HEM1_CYAPA

UniProt

P48077 - HEM1_CYAPA

Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Cyanophora paradoxa
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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

    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
    Encoded oniPlastid; Cyanelle
    OrganismiCyanophora paradoxa
    Taxonomic identifieri2762 [NCBI]
    Taxonomic lineageiEukaryotaGlaucocystophyceaeCyanophoraceaeCyanophora

    Subcellular locationi

    GO - Cellular componenti

    1. cyanelle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cyanelle, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Glutamyl-tRNA reductasePRO_0000114096Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP48077.
    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

    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.

    P48077-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIIVVGLSH KTAPVDFREK LSIPKVRIGE AIRELCNYPH IEEVAILSTC    50
    NRLEIYLLTS DTYQGIREAT QFLADSSDLS LPELRQHLFI LLHQDAVMHL 100
    MRVTAGLDSL IIGEGQILSQ VKQCYQLGQQ YQGIGPVLNN IFKQAISAGK 150
    RVRTETQIST GAVSISSAAV ELAQIKKQDL RTANITILGA GKMSRLLVQH 200
    LLSKRVKDIN IVNRSVERAK LLVDQFKEAN INIYNLSELK TILQNSDIVF 250
    TGTSSQEPII TPELINDCDN LPSELMLFDI AVPRNVDPNV SQFDNIKVFN 300
    VDDLKVVVSQ NQQTRRKMAK AAEILLEEEL SAFNIWWGSL EAIPTINKLR 350
    EKAEIIRVKE LEKAISRLGN EFVSDHQEIV ESLTRGIVNK ILHDPMVQLR 400
    AQQDIEIRGR ALKILQTLFN LDTIKNGMSP TL 432
    Length:432
    Mass (Da):48,542
    Last modified:February 1, 1996 - v1
    Checksum:iF14378FC72FFD05B
    GO

    Sequence cautioni

    The sequence CAC35456.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30821 Genomic DNA. Translation: AAA81194.1.
    X17063 Genomic DNA. Translation: CAC35456.1. Different initiation.
    PIRiT06851.
    RefSeqiNP_043163.1. NC_001675.1.

    Genome annotation databases

    GeneIDi801525.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30821 Genomic DNA. Translation: AAA81194.1 .
    X17063 Genomic DNA. Translation: CAC35456.1 . Different initiation.
    PIRi T06851.
    RefSeqi NP_043163.1. NC_001675.1.

    3D structure databases

    ProteinModelPortali P48077.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 801525.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .
    UPA00668 .

    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. "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."
      Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., Bryant D.A.
      Plant Mol. Biol. Rep. 13:327-332(1995)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UTEX LB 555 / Pringsheim.
    2. "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the genetic complexity of a primitive plastid."
      Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.
      (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W. (eds.); Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997)
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UTEX LB 555 / Pringsheim.
    3. "The cyanelle genome of Cyanophora paradoxa encodes ribosomal proteins not encoded by the chloroplasts genomes of higher plants."
      Bryant D.A., Stirewalt V.L.
      FEBS Lett. 259:273-280(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-432.
      Strain: UTEX LB 555 / Pringsheim.

    Entry informationi

    Entry nameiHEM1_CYAPA
    AccessioniPrimary (citable) accession number: P48077
    Secondary accession number(s): Q9BA13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3