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P49295

- HEM12_CUCSA

UniProt

P49295 - HEM12_CUCSA

Protein

Glutamyl-tRNA reductase 2, chloroplastic

Gene

HEMA2

Organism
Cucumis sativus (Cucumber)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (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).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 sitei143 – 1431NucleophileBy similarity
    Sitei192 – 1921Important for activityBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Binding sitei213 – 2131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi284 – 2896NADPBy 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

    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 2, chloroplastic (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:HEMA2
    OrganismiCucumis sativus (Cucumber)
    Taxonomic identifieri3659 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

    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
    Chaini? – 542Glutamyl-tRNA reductase 2, chloroplasticPRO_0000013310
    Transit peptidei1 – ?ChloroplastSequence Analysis

    Expressioni

    Tissue specificityi

    Found in all tissues examined.

    Structurei

    3D structure databases

    ProteinModelPortaliP49295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni142 – 1454Substrate bindingBy similarity
    Regioni207 – 2093Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK02492.

    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.

    P49295-1 [UniParc]FASTAAdd to Basket

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    MAAAVGGLTT CFARPTPEFI APSTSYSAPV RVFFKPFKVR DLCCAGEVVG    50
    VLSARSIPIS PRFELIRLVR MQPGLSALEL LKTSSVNRYT KERISIVVIG 100
    LNVHTAPVEL REKLAIPEAQ WPPGIGELCA LNHIEEAAVL STCNRIEIYV 150
    VALSQHRGVK EVTEWMSKRS GIPISELCKH RVLLYNTDAT QHLFEVSAGL 200
    DSLVLGEGQI LAQVKHVVKT GQGVAGFDRK ISGLFKHAIT VGKRVRTETN 250
    ISSGSFSVSS AAVELAQKKL PESSYATAKV MVVGAGKMGK LVIKHLVAKG 300
    CRKMVVVNRT QDSVDAVEEL KDVEIIYKPL SKILACASEA DVIFTCTASK 350
    TPLFTKEHVA MLPPAGTETG RRLFVDISVP RNVEQRVSDL ETVSVFNVDD 400
    LKEVVAANKE DRLKKVQEAQ SIIGEEINKF EAWRDSLETV PTIKKFRAYV 450
    ERIRAAELDK CLSKMGEDIP KKKKVAINDL SLGIANKLLH GPIQHLRCDG 500
    NDSRTLDEIL QNMHAINRMF DLETDLSVLE EKIRAKVERG QK 542
    Length:542
    Mass (Da):59,707
    Last modified:February 1, 1996 - v1
    Checksum:iA576B3B96A0B6EEF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D67088 mRNA. Translation: BAA11091.1.
    PIRiT10245.
    RefSeqiNP_001267616.1. NM_001280687.1.

    Genome annotation databases

    GeneIDi101208135.
    KEGGicsv:101208135.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D67088 mRNA. Translation: BAA11091.1 .
    PIRi T10245.
    RefSeqi NP_001267616.1. NM_001280687.1.

    3D structure databases

    ProteinModelPortali P49295.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101208135.
    KEGGi csv:101208135.

    Phylogenomic databases

    KOi K02492.

    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. "Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase proteins in greening cucumber seedlings."
      Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H., Inokuchi H., Tanaka A.
      Plant Physiol. 110:1223-1230(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Aonagajibai.
      Tissue: Cotyledon.

    Entry informationi

    Entry nameiHEM12_CUCSA
    AccessioniPrimary (citable) accession number: P49295
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 92 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

    Documents

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

    External Data

    Dasty 3