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A2Z928

- HEM1_ORYSI

UniProt

A2Z928 - HEM1_ORYSI

Protein

Glutamyl-tRNA reductase, chloroplastic

Gene

OsI_033071

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (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
    ORF Names:OsI_033071
    OrganismiOryza sativa subsp. indica (Rice)
    Taxonomic identifieri39946 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

    Organism-specific databases

    GrameneiA2Z928.

    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_0000295656Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliA2Z928.
    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.
    HOGENOMiHOG000109651.

    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.

    A2Z928-1 [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 EDSLTKKMRR SIEELSTGIV NKLLHGPLQH LRCDGSDSRT 500
    LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN 537
    Length:537
    Mass (Da):58,435
    Last modified:July 24, 2007 - v2
    Checksum:i51414A99FFF50A9A
    GO

    Sequence cautioni

    The sequence BAA25003.1 differs from that shown. Reason: Frameshift at positions 22 and 31.
    The sequence EAY79112.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511I → L in BAA25003. 1 PublicationCurated
    Sequence conflicti201 – 2011Q → E in BAA25003. 1 PublicationCurated
    Sequence conflicti463 – 4631S → A in BAA25003. 1 PublicationCurated
    Sequence conflicti468 – 4681M → T in BAA25003. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011416 mRNA. Translation: BAA25003.1. Frameshift.
    CM000135 Genomic DNA. Translation: EAY79112.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011416 mRNA. Translation: BAA25003.1 . Frameshift.
    CM000135 Genomic DNA. Translation: EAY79112.1 . Different initiation.

    3D structure databases

    ProteinModelPortali A2Z928.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei A2Z928.

    Phylogenomic databases

    eggNOGi COG0373.
    HOGENOMi HOG000109651.

    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. "Nucleotide sequence of a cDNA clone encoding glutamyl-tRNA reductase from rice."
      Nakayashiki T., Inokuchi H.
      Plant Gene Register PGR98-080
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. IR36.
    2. "The genomes of Oryza sativa: a history of duplications."
      Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
      , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
      PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. 93-11.

    Entry informationi

    Entry nameiHEM1_ORYSI
    AccessioniPrimary (citable) accession number: A2Z928
    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 57 of the entry and version 2 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

    Documents

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

    External Data

    Dasty 3