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P93111 (HEM11_CUCSA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. 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 1, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA1
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Protein attributes

Sequence length552 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 By similarity HAMAP-Rule MF_00087.

Tissue specificity

Primarily in cotyledons and hypocotyls of greening cucumber seedlings.

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? – 552Glutamyl-tRNA reductase 1, chloroplastic HAMAP-Rule MF_00087PRO_0000013309

Regions

Nucleotide binding292 – 2976NADP By similarity
Region150 – 1534Substrate binding By similarity
Region215 – 2173Substrate binding By similarity

Sites

Active site1511Nucleophile By similarity
Binding site2101Substrate By similarity
Binding site2211Substrate By similarity
Site2001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P93111 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 9C7A72AF24FF00F5

FASTA55260,895
        10         20         30         40         50         60 
MAVSTSFSGA KLEALLFKSA SNSSSTRNLS SSHLPGFCKS IRTRRILFQR TGVSSFTPFK 

        70         80         90        100        110        120 
CELASSDVLV QNDEIDPPKS SNLSALEQLK TSAVDRYTKE RSSIVVIGLS IHTTPVEMRE 

       130        140        150        160        170        180 
KLAIPEAEWP RAIGELCGLN HIEEAAVLST CNRMEIYVVA LSQHRGVKEV TEWMSKTSGI 

       190        200        210        220        230        240 
PVSEICQHRF LLYNNDATQH IFEVSAGLDS LVLGEGQILA QVKQVVKVGQ GVAGFGRNIS 

       250        260        270        280        290        300 
GLFKHAITVG KRVRTETNIA AGAVSVSSAA VELALMKLPE PSHATARMLV IGAGKMGKLV 

       310        320        330        340        350        360 
IKHLVAKGCT KMVVVNRSEE RVTAIREEMK DVEIIYKPLT EMLSCTAEAD VIFTSTASES 

       370        380        390        400        410        420 
LLFTKEQVKD LPPVGHDVGG LRLFIDISVP RNVGACINNL EDVRVYNVDD LKEVVAANKE 

       430        440        450        460        470        480 
DRLRKAMEAQ SIITEESKQF EAWRDSLETV PTIKKLRAYA ERIRTAELEK CLSKMGDDIP 

       490        500        510        520        530        540 
KKTRRAVDDL SRGIVNKLLH GPMQHLRCDG SDSRTLSETL ENMHALNRMF SLETEIAVLE 

       550 
QKIRAKVEQN QK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50407 mRNA. Translation: BAA08910.1.
PIRT10186.
RefSeqNP_001267503.1. NM_001280574.1.

3D structure databases

ProteinModelPortalP93111.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101220615.
KEGGcsv:101220615.

Phylogenomic databases

KOK02492.

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.

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]
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM11_CUCSA
AccessionPrimary (citable) accession number: P93111
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 90 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