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P84719 (LGUL_PINST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative lactoylglutathione lyase

EC=4.4.1.5
Alternative name(s):
Aldoketomutase
Glyoxalase I
Short name=Glx I
Ketone-aldehyde mutase
Methylglyoxalase
PS3
S-D-lactoylglutathione methylglyoxal lyase
OrganismPinus strobus (Eastern white pine)
Taxonomic identifier3348 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaConiferopsidaConiferalesPinaceaePinusStrobus

Protein attributes

Sequence length22 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity. UniProtKB Q09751

Catalytic activity

(R)-S-lactoylglutathione = glutathione + methylglyoxal. UniProtKB Q09751

Cofactor

Binds 1 zinc ion per subunit By similarity. UniProtKB Q09751

Pathway

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

Miscellaneous

On the 2D-gel the determined pI of this protein is: 5.7, its MW is: 35.1 kDa. Ref.1

Sequence similarities

Belongs to the glyoxalase I family.

Caution

The order of the peptides shown is unknown. Ref.1

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionLyase
   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

Chain‹1 – ›22›22Putative lactoylglutathione lyase
PRO_0000240626

Experimental info

Non-adjacent residues11 – 122
Non-terminal residue11
Non-terminal residue221

Sequences

Sequence LengthMass (Da)Tools
P84719 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 5E312E7F47F4B4D6

FASTA222,296
        10         20 
ITACLDPDGW KEPGPLPGIS TK 

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References

[1]"Proteomic comparison of needles from blister rust-resistant and susceptible Pinus strobus seedlings reveals upregulation of putative disease resistance proteins."
Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L., Witthuhn B.A., David A.J., Gillman J.H.
Mol. Plant Microbe Interact. 19:150-160(2006) [PubMed: 16529377] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Leaf.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

PROSITEPS00934. GLYOXALASE_I_1. Partial match.
PS00935. GLYOXALASE_I_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_PINST
AccessionPrimary (citable) accession number: P84719
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: May 31, 2011
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families