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Q42843

- HEM11_HORVU

UniProt

Q42843 - HEM11_HORVU

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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

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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251Nucleophile By similarity
Sitei174 – 1741Important for activity By similarity
Binding sitei184 – 1841Substrate By similarity
Binding sitei195 – 1951Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2716NADP By similarity

GO - Molecular functioni

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

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Chloroplast1 Publication
Add
BLAST
Chaini44 – 527484Glutamyl-tRNA reductase 1, chloroplasticUniRule annotation
PRO_0000013311Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriQ42843.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

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.

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

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

« Hide

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: September 3, 2014
This is version 99 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.

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

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