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O65796 (HEM13_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA3
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087

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

Subcellular location

Plastidchloroplast HAMAP-Rule MF_00087.

Tissue specificity

Primarily expressed in roots.

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
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

   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 – ?Chloroplast Potential
Chain? – 535Glutamyl-tRNA reductase 3, chloroplastic HAMAP-Rule MF_00087PRO_0000013312

Regions

Nucleotide binding272 – 2776NADP By similarity
Region131 – 1333Substrate binding By similarity
Region195 – 1973Substrate binding By similarity

Sites

Active site1311Nucleophile By similarity
Binding site1901Substrate By similarity
Binding site2011Substrate By similarity
Site1801Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O65796 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: B2830889AE6A3224

FASTA53558,419
        10         20         30         40         50         60 
MASTSTASAT AMAGAFAAAG VNKPRGSAAC PRVPAGGRQR LSCVVRCDAG PGVPAQMAAM 

        70         80         90        100        110        120 
AASVAALEQF KISADRYMKE KSSIAVIGLS IHTAPVEMRE KLAVAEELWP RAVAELTNLN 

       130        140        150        160        170        180 
HIEKAAVLSP CNRMEIYVVA LSWNRGIREI VDWMSMKSGI PAVELREHLF MFRDSDATRH 

       190        200        210        220        230        240 
LFEVSSGLDS LVLGEGQILA QVKQVVRSGQ NSGGLGKNID RMFKDAITAG KRVRSETNIS 

       250        260        270        280        290        300 
CGAVSVSSAA VELALMKLPK SECLSARMLL IGAGKMGRLV AKHLAAKGCK KVVIVNRSVE 

       310        320        330        340        350        360 
RVDAIREEMQ GIEIVYRSLT EMYEAAADAD VVFTSTSSES PLFTKEHAEA LPPVSGALGG 

       370        380        390        400        410        420 
VRLFVDISVP RNVSACVSDV GHARVYNVDD LKEVVEANKE DRLRKAMEAQ TIISEELKRF 

       430        440        450        460        470        480 
EAWRDSMETV PTIKKLRSYA DRVRASELDK CLQKIGEDAL TKKMRRSIEQ LSTGIVNRLL 

       490        500        510        520        530 
HGPLQHLRCD GTDNRTLDET LENMHALNRM FGLDTEKAVM EQKIKTKVEK QKTQN 

« Hide

References

[1]"The third member of the hemA gene family encoding glutamyl-tRNA reductase is primarily expressed in roots in Hordeum vulgare."
Tanaka R., Yoshida K., Nakayashiki T., Tsuji H., Inokuchi H., Okada K., Tanaka A.
Photosyn. Res. 53:161-171(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Bonus.
Tissue: Root.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88383 mRNA. Translation: BAA25168.1.
PIRT04402.

3D structure databases

ProteinModelPortalO65796.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneO65796.

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.

Gene expression databases

GenevestigatorO65796.

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 nameHEM13_HORVU
AccessionPrimary (citable) accession number: O65796
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 88 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

PATHWAY comments

Index of metabolic and biosynthesis pathways