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P0C587 (HEM1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Ordered Locus Names:Os10g0502400, LOC_Os10g35840
ORF Names:OSJNBa0078O01.14, OSJNBb0073N24.1
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length537 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.

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.

Sequence caution

The sequence AAG13620.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
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 – 4848Chloroplast Potential
Chain49 – 537489Glutamyl-tRNA reductase, chloroplastic HAMAP-Rule MF_00087
PRO_0000013313

Regions

Nucleotide binding276 – 2816NADP By similarity
Region134 – 1374Substrate binding By similarity
Region199 – 2013Substrate binding By similarity

Sites

Active site1351Nucleophile By similarity
Binding site1941Substrate By similarity
Binding site2051Substrate By similarity
Site1841Important for activity By similarity

Experimental info

Sequence conflict3461L → F in AK099393. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P0C587 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 51415C5525E3C640

FASTA53758,419
        10         20         30         40         50         60 
MMASTTSATA AGGAFAAAKT RAGSSAAGGG ACARVAAGGR RRSGVVVRCD AGVEAQAQAQ 

        70         80         90        100        110        120 
AVAKAASVAA LEQFKISADR YMKERSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL 

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

       190        200        210        220        230        240 
ATRHLFEVSA GLDSLVLGEG QILAQVKQVV RSGQNSGGLG KNIDRMFKDA ITAGKRVRCE 

       250        260        270        280        290        300 
TNISSGAVSV SSAAVELALM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN 

       310        320        330        340        350        360 
RSVERVDAIR EEMKDIEIVY RPLTEMYEAA AEADVVFTST ASETPLFTKE HAEALPAISD 

       370        380        390        400        410        420 
AMGGVRLFVD ISVPRNVSAC VSEVGHARVY NVDDLKEVVE ANKEDRLRKA MEAQTIITQE 

       430        440        450        460        470        480 
LKRFEAWRDS LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDALTKKMRR SIEELSTGIV 

       490        500        510        520        530 
NKLLHGPLQH LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN 

« Hide

References

« Hide 'large scale' references
[1]"In-depth view of structure, activity, and evolution of rice chromosome 10."
Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. expand/collapse author list , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC078840 Genomic DNA. Translation: AAG13620.1. Different initiation.
AC079888 Genomic DNA. Translation: AAM93670.1.
DP000086 Genomic DNA. Translation: ABB47844.1.
AP008216 Genomic DNA. Translation: BAF26905.1.
AK099393 mRNA. No translation available.
RefSeqNP_001064991.1. NM_001071526.1.
UniGeneOs.11129.

3D structure databases

ProteinModelPortalP0C587.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS10T0502400-01; OS10T0502400-01; OS10G0502400.
GeneID4349044.
KEGGosa:4349044.

Organism-specific databases

GrameneP0C587.

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMAGLSIHTT.

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 nameHEM1_ORYSJ
AccessionPrimary (citable) accession number: P0C587
Secondary accession number(s): O48674 expand/collapse secondary AC list , Q0IWL0, Q337F6, Q8LNE9, Q9FW00
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: May 14, 2014
This is version 57 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

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways