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P0C587

- HEM1_ORYSJ

UniProt

P0C587 - HEM1_ORYSJ

Protein

Glutamyl-tRNA reductase, chloroplastic

Gene

Os10g0502400

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).By similarity

    Catalytic activityi

    L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei135 – 1351NucleophileBy similarity
    Sitei184 – 1841Important for activityBy similarity
    Binding sitei194 – 1941SubstrateBy similarity
    Binding sitei205 – 2051SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi276 – 2816NADPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. chlorophyll biosynthetic process Source: UniProtKB-KW
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    3. response to oxidative stress Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00251; UER00316.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl-tRNA reductase, chloroplastic (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Ordered Locus Names:Os10g0502400, LOC_Os10g35840
    ORF Names:OSJNBa0078O01.14, OSJNBb0073N24.1
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
    ProteomesiUP000000763: Chromosome 10

    Organism-specific databases

    GrameneiP0C587.

    Subcellular locationi

    Plastidchloroplast By similarity

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848ChloroplastSequence AnalysisAdd
    BLAST
    Chaini49 – 537489Glutamyl-tRNA reductase, chloroplasticPRO_0000013313Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP0C587.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 1374Substrate bindingBy similarity
    Regioni199 – 2013Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0373.
    KOiK02492.
    OMAiGLSIHTT.

    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]
    SUPFAMiSSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsiTIGR01035. hemA. 1 hit.
    PROSITEiPS00747. GLUTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0C587-1 [UniParc]FASTAAdd to Basket

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    MMASTTSATA AGGAFAAAKT RAGSSAAGGG ACARVAAGGR RRSGVVVRCD    50
    AGVEAQAQAQ AVAKAASVAA LEQFKISADR YMKERSSIAV IGLSVHTAPV 100
    EMREKLAVAE ELWPRAISEL TSLNHIEEAA VLSTCNRMEI YVVALSWNRG 150
    IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA GLDSLVLGEG 200
    QILAQVKQVV RSGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISSGAVSV 250
    SSAAVELALM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN 300
    RSVERVDAIR EEMKDIEIVY RPLTEMYEAA AEADVVFTST ASETPLFTKE 350
    HAEALPAISD AMGGVRLFVD ISVPRNVSAC VSEVGHARVY NVDDLKEVVE 400
    ANKEDRLRKA MEAQTIITQE LKRFEAWRDS LETVPTIKKL RSYADRIRAS 450
    ELEKCLQKIG EDALTKKMRR SIEELSTGIV NKLLHGPLQH LRCDGSDSRT 500
    LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN 537
    Length:537
    Mass (Da):58,419
    Last modified:July 24, 2007 - v1
    Checksum:i51415C5525E3C640
    GO

    Sequence cautioni

    The sequence AAG13620.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti346 – 3461L → F in AK099393. (PubMed:12869764)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC078840 Genomic DNA. Translation: AAG13620.1. Different initiation.
    AC079888 Genomic DNA. Translation: AAM93670.1.
    DP000086 Genomic DNA. Translation: ABB47844.1.
    AP008216 Genomic DNA. Translation: BAF26905.1.
    AK099393 mRNA. No translation available.
    RefSeqiNP_001064991.1. NM_001071526.1.
    UniGeneiOs.11129.

    Genome annotation databases

    EnsemblPlantsiOS10T0502400-01; OS10T0502400-01; OS10G0502400.
    GeneIDi4349044.
    KEGGiosa:4349044.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC078840 Genomic DNA. Translation: AAG13620.1 . Different initiation.
    AC079888 Genomic DNA. Translation: AAM93670.1 .
    DP000086 Genomic DNA. Translation: ABB47844.1 .
    AP008216 Genomic DNA. Translation: BAF26905.1 .
    AK099393 mRNA. No translation available.
    RefSeqi NP_001064991.1. NM_001071526.1.
    UniGenei Os.11129.

    3D structure databases

    ProteinModelPortali P0C587.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi OS10T0502400-01 ; OS10T0502400-01 ; OS10G0502400 .
    GeneIDi 4349044.
    KEGGi osa:4349044.

    Organism-specific databases

    Gramenei P0C587.

    Phylogenomic databases

    eggNOGi COG0373.
    KOi K02492.
    OMAi GLSIHTT.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    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 SSF69075. SSF69075. 1 hit.
    SSF69742. SSF69742. 1 hit.
    TIGRFAMsi TIGR01035. hemA. 1 hit.
    PROSITEi PS00747. GLUTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "In-depth view of structure, activity, and evolution of rice chromosome 10."
      Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.
      , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
      Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    3. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    4. "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
      The rice full-length cDNA consortium
      Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Nipponbare.

    Entry informationi

    Entry nameiHEM1_ORYSJ
    AccessioniPrimary (citable) accession number: P0C587
    Secondary accession number(s): O48674
    , Q0IWL0, Q337F6, Q8LNE9, Q9FW00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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 By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3