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Q42843 (HEM11_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase 1, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA1
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Ref.3

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Subunit structure

Homodimer. Ref.3

Subcellular location

Plastidchloroplast HAMAP-Rule MF_00087.

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Sequence caution

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

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to oxidative stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Chloroplast Ref.2
Chain44 – 527484Glutamyl-tRNA reductase 1, chloroplastic HAMAP-Rule MF_00087
PRO_0000013311

Regions

Nucleotide binding266 – 2716NADP By similarity
Region124 – 1274Substrate binding By similarity
Region189 – 1913Substrate binding By similarity
Compositional bias286 – 2894Poly-Val HAMAP-Rule MF_00087

Sites

Active site1251Nucleophile By similarity
Binding site1841Substrate By similarity
Binding site1951Substrate By similarity
Site1741Important for activity By similarity

Secondary structure

................................................................. 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q42843 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: D329E56458BE1165

FASTA52757,653
        10         20         30         40         50         60 
MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ AASKAASITA 

        70         80         90        100        110        120 
LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL TSLNHIEEAA 

       130        140        150        160        170        180 
VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA 

       190        200        210        220        230        240 
GLDSLVLGEG QILAQVKQVV RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV 

       250        260        270        280        290        300 
SSAAVELAMM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR 

       310        320        330        340        350        360 
EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL AMGGVRLFVD 

       370        380        390        400        410        420 
ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA MEAQTIITQE LKRFEAWRDS 

       430        440        450        460        470        480 
LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDNLNKKMRR SIEELSTGIV NKLLHGPLQH 

       490        500        510        520 
LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAVLEQKIKA KVEKTQS 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92403 mRNA. Translation: CAA63140.1.
X86101 mRNA. Translation: CAA60054.1. Different initiation.
PIRT05732.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B29model-A76-460[»]
1B61model-A76-460[»]
ProteinModelPortalQ42843.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ42843.

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.

Gene expression databases

GenevestigatorQ42843.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM11_HORVU
AccessionPrimary (citable) accession number: Q42843
Secondary accession number(s): Q42844
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways