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P49295 (HEM12_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 2, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA2
OrganismCucumis sativus (Cucumber)
Taxonomic identifier3659 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Protein attributes

Sequence length542 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

Found in all tissues examined.

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? – 542Glutamyl-tRNA reductase 2, chloroplastic HAMAP-Rule MF_00087PRO_0000013310

Regions

Nucleotide binding284 – 2896NADP By similarity
Region142 – 1454Substrate binding By similarity
Region207 – 2093Substrate binding By similarity

Sites

Active site1431Nucleophile By similarity
Binding site2021Substrate By similarity
Binding site2131Substrate By similarity
Site1921Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P49295 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A576B3B96A0B6EEF

FASTA54259,707
        10         20         30         40         50         60 
MAAAVGGLTT CFARPTPEFI APSTSYSAPV RVFFKPFKVR DLCCAGEVVG VLSARSIPIS 

        70         80         90        100        110        120 
PRFELIRLVR MQPGLSALEL LKTSSVNRYT KERISIVVIG LNVHTAPVEL REKLAIPEAQ 

       130        140        150        160        170        180 
WPPGIGELCA LNHIEEAAVL STCNRIEIYV VALSQHRGVK EVTEWMSKRS GIPISELCKH 

       190        200        210        220        230        240 
RVLLYNTDAT QHLFEVSAGL DSLVLGEGQI LAQVKHVVKT GQGVAGFDRK ISGLFKHAIT 

       250        260        270        280        290        300 
VGKRVRTETN ISSGSFSVSS AAVELAQKKL PESSYATAKV MVVGAGKMGK LVIKHLVAKG 

       310        320        330        340        350        360 
CRKMVVVNRT QDSVDAVEEL KDVEIIYKPL SKILACASEA DVIFTCTASK TPLFTKEHVA 

       370        380        390        400        410        420 
MLPPAGTETG RRLFVDISVP RNVEQRVSDL ETVSVFNVDD LKEVVAANKE DRLKKVQEAQ 

       430        440        450        460        470        480 
SIIGEEINKF EAWRDSLETV PTIKKFRAYV ERIRAAELDK CLSKMGEDIP KKKKVAINDL 

       490        500        510        520        530        540 
SLGIANKLLH GPIQHLRCDG NDSRTLDEIL QNMHAINRMF DLETDLSVLE EKIRAKVERG 


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
D67088 mRNA. Translation: BAA11091.1.
PIRT10245.
RefSeqNP_001267616.1. NM_001280687.1.

3D structure databases

ProteinModelPortalP49295.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101208135.
KEGGcsv:101208135.

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 nameHEM12_CUCSA
AccessionPrimary (citable) accession number: P49295
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
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