Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q948T6 (LGUL_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Lactoylglutathione lyase

EC=4.4.1.5
Alternative name(s):
Aldoketomutase
Allergen Glb33
Glyoxalase I
Short name=Glx I
Ketone-aldehyde mutase
Methylglyoxalase
PP33
S-D-lactoylglutathione methylglyoxal lyase
Allergen=Ory s ?
Gene names
Name:GLX-I
Ordered Locus Names:Os08g0191700, LOC_Os08g09250
ORF Names:OSJNBa0056O06.9-1
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity.

Catalytic activity

(R)-S-lactoylglutathione = glutathione + methylglyoxal.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.

Tissue specificity

Expressed in callus, stem, leaves, panicles and maturing seeds (at protein level). Ref.1 Ref.4

Post-translational modification

Phosphorylated after gibberellin treatment. Ref.5

Allergenic properties

Causes an allergic reaction in human. Binds to IgE. Ref.1

Sequence similarities

Belongs to the glyoxalase I family.

Biophysicochemical properties

Kinetic parameters:

KM=7.6 mM for methylglyoxal Ref.1

Ontologies

Keywords
   DiseaseAllergen
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular functionlactoylglutathione lyase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Lactoylglutathione lyase
PRO_0000168085

Sites

Metal binding271Zinc By similarity
Metal binding781Zinc By similarity
Metal binding961Zinc By similarity
Metal binding1451Zinc By similarity

Experimental info

Sequence conflict251L → V in BAB71741. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q948T6 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 5CB9FEB32F2BC7ED

FASTA29132,553
        10         20         30         40         50         60 
MASGSEAEKS PEVVLEWPKK DKKRLLHAVY RVGDLDRTIK CYTECFGMKL LRKRDVPEEK 

        70         80         90        100        110        120 
YTNAFLGFGP EDTNFALELT YNYGVDKYDI GAGFGHFAIA TEDVYKLAEK IKSSCCCKIT 

       130        140        150        160        170        180 
REPGPVKGGS TVIAFAQDPD GYMFELIQRG PTPEPLCQVM LRVGDLDRSI KFYEKALGMK 

       190        200        210        220        230        240 
LLRKKDVPDY KYTIAMLGYA DEDKTTVIEL TYNYGVTEYT KGNAYAQVAI GTEDVYKSAE 

       250        260        270        280        290 
AVELVTKELG GKILRQPGPL PGLNTKIASF LDPDGWKVVL VDNADFLKEL Q 

« Hide

References

« Hide 'large scale' references
[1]"A 33-kDa allergen from rice (Oryza sativa L. Japonica). cDNA cloning, expression, and identification as a novel glyoxalase I."
Usui Y., Nakase M., Hotta H., Urisu A., Aoki N., Kitajima K., Matsuda T.
J. Biol. Chem. 276:11376-11381(2001) [PubMed: 11139585] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 222-236 AND 267-277, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, ALLERGEN.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed: 16100779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"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: 12869764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.
[4]"Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003."
Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.
Nucleic Acids Res. 32:D388-D392(2004) [PubMed: 14681440] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-37, TISSUE SPECIFICITY.
Strain: cv. Nipponbare.
Tissue: Callus and Panicle.
[5]"Identification of phosphoproteins regulated by gibberellin in rice leaf sheath."
Khan M.M.K., Jan A., Karibe H., Komatsu S.
Plant Mol. Biol. 58:27-40(2005) [PubMed: 16028114] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, PHOSPHORYLATION.
Strain: cv. Nipponbare.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017042 mRNA. Translation: BAA36759.1.
AB050986 Genomic DNA. Translation: BAB71741.1.
AP005441 Genomic DNA. Translation: BAD05593.1.
AK066092 mRNA. No translation available.
AK103694 mRNA. No translation available.
RefSeqNP_001061172.1. NM_001067707.1.
UniGeneOs.7835.

3D structure databases

ProteinModelPortalQ948T6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ948T6.

Protein family/group databases

Allergome1048. Ory s Glyoxalase I.

2D gel databases

ANU-2DPAGEQ948T6.

Proteomic databases

PRIDEQ948T6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsLOC_Os08g09250.2; LOC_Os08g09250.2; LOC_Os08g09250.
GeneID4344858.
KEGGosa:4344858.

Organism-specific databases

GrameneQ948T6.

Phylogenomic databases

GeneTreeEPGT00050000015867.
PhylomeDBQ948T6.
ProtClustDBPLN02300.

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
KOK01759.
PfamPF00903. Glyoxalase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00068. Glyox_I. 2 hits.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_ORYSJ
AccessionPrimary (citable) accession number: Q948T6
Secondary accession number(s): Q9ZWJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 16, 2011
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families