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Q42843

- HEM11_HORVU

UniProt

Q42843 - HEM11_HORVU

Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei125 – 1251NucleophileBy similarity
    Sitei174 – 1741Important for activityBy similarity
    Binding sitei184 – 1841SubstrateBy similarity
    Binding sitei195 – 1951SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi266 – 2716NADPBy 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 1, chloroplastic (EC:1.2.1.70)
    Short name:
    GluTR
    Gene namesi
    Name:HEMA1
    OrganismiHordeum vulgare (Barley)
    Taxonomic identifieri4513 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiQ42843.

    Subcellular locationi

    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 – 4343Chloroplast1 PublicationAdd
    BLAST
    Chaini44 – 527484Glutamyl-tRNA reductase 1, chloroplasticPRO_0000013311Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriQ42843.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    527
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi79 – 813
    Beta strandi96 – 994
    Helixi104 – 12522
    Beta strandi133 – 1375
    Turni150 – 1523
    Helixi155 – 1595
    Helixi170 – 18213
    Helixi193 – 1975
    Helixi209 – 2135
    Beta strandi215 – 2228
    Helixi225 – 2306
    Helixi233 – 25119
    Beta strandi262 – 2654
    Helixi269 – 28113
    Beta strandi285 – 2884
    Helixi293 – 30210
    Helixi313 – 3153
    Turni316 – 3183
    Helixi319 – 3213
    Beta strandi324 – 3274
    Beta strandi334 – 3363
    Helixi347 – 3504
    Beta strandi356 – 3583
    Beta strandi361 – 3633
    Beta strandi365 – 3673
    Helixi368 – 3769
    Beta strandi380 – 3834
    Helixi386 – 3894
    Beta strandi392 – 3976
    Helixi398 – 4047
    Beta strandi406 – 4105
    Helixi413 – 4219
    Helixi423 – 43614
    Helixi443 – 45715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B29model-A76-460[»]
    1B61model-A76-460[»]
    ProteinModelPortaliQ42843.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni124 – 1274Substrate bindingBy similarity
    Regioni189 – 1913Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi286 – 2894Poly-Val

    Sequence similaritiesi

    Belongs to the glutamyl-tRNA reductase family.Curated

    Keywords - Domaini

    Transit peptide

    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.

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

    Q42843-1 [UniParc]FASTAAdd to Basket

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    MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ    50
    AASKAASITA LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE 100
    ELWPRAISEL TSLNHIEEAA VLSTCNRMEI YVVALSWNRG IREVVDWMSK 150
    KSGIPASELR EHLFMLRDSD ATRHLFEVSA GLDSLVLGEG QILAQVKQVV 200
    RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV SSAAVELAMM 250
    KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR 300
    EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL 350
    AMGGVRLFVD ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA 400
    MEAQTIITQE LKRFEAWRDS LETVPTIKKL RSYADRIRAS ELEKCLQKIG 450
    EDNLNKKMRR SIEELSTGIV NKLLHGPLQH LRCDGSDSRT LDETLENMHA 500
    LNRMFSLDTE KAVLEQKIKA KVEKTQS 527
    Length:527
    Mass (Da):57,653
    Last modified:November 1, 1997 - v1
    Checksum:iD329E56458BE1165
    GO

    Sequence cautioni

    The sequence CAA60054.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92403 mRNA. Translation: CAA63140.1.
    X86101 mRNA. Translation: CAA60054.1. Different initiation.
    PIRiT05732.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92403 mRNA. Translation: CAA63140.1 .
    X86101 mRNA. Translation: CAA60054.1 . Different initiation.
    PIRi T05732.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B29 model - A 76-460 [» ]
    1B61 model - A 76-460 [» ]
    ProteinModelPortali Q42843.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei Q42843.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00316 .

    Gene expression databases

    Genevestigatori Q42843.

    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. "Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley."
      Bougri O., Grimm B.
      Plant J. 9:867-878(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Klages.
    2. "Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis."
      Pontoppidan B., Kannangara C.G.
      Eur. J. Biochem. 225:529-537(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 44-65, CHARACTERIZATION.
    3. "Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase."
      Vothknecht U.C., Kannangara C.G., von Wettstein D.
      Proc. Natl. Acad. Sci. U.S.A. 93:9287-9291(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION, HEME BINDING, SUBUNIT.
    4. "Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins."
      Brody S.S., Gough S.P., Kannangara C.G.
      Proteins 37:485-493(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 76-460.

    Entry informationi

    Entry nameiHEM11_HORVU
    AccessioniPrimary (citable) accession number: Q42843
    Secondary accession number(s): Q42844
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Was shown to bind heme, but the precise role of heme is unclear.
    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

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3