Reviewed, UniProtKB/Swiss-Prot P84719 (LGUL_PINST)

Names and origin

Protein names	Recommended name:     Putative lactoylglutathione lyase     EC=4.4.1.5 Alternative name(s):     Methylglyoxalase     Aldoketomutase     Glyoxalase I       Short name=Glx I     Ketone-aldehyde mutase     S-D-lactoylglutathione methylglyoxal lyase     PS3
Organism	Pinus strobus (Eastern white pine)
Taxonomic identifier	3348 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Pinaceae › Pinus › Strobus

Protein attributes

Sequence length	22 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	lactoylglutathione lyase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›22	›22	Putative lactoylglutathione lyase		PRO_0000240626
Experimental info
	Non-adjacent residues	11 – 12	2
	Non-terminal residue	1	1
	Non-terminal residue	22	1

Sequences

	Sequence		Length	Mass (Da)
	P84719-1 [UniParc]. Last modified June 27, 2006. Version 1. Checksum: 5E312E7F47F4B4D6	FASTA	22	2,296
	10 20 ITACLDPDGW KEPGPLPGIS TK

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
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.4.1.5. 228853.
Family and domain databases
InterPro	IPR018146. Glyoxalase_1_CS. [Graphical view]
PROSITE	PS00934. GLYOXALASE_I_1. Partial match. PS00935. GLYOXALASE_I_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LGUL_PINST

Accession

Primary (citable) accession number: P84719

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	June 27, 2006
Last modified:	October 13, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)