Reviewed, UniProtKB/Swiss-Prot Q42891 (LGUL_SOLLC)

Names and origin

Protein names

Recommended name:
    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

Gene names

Name:

GLX1

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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	Ubiquitous.
Induction	By stress conditions such as salt stress, water deficit, or treatment with abscisic acid.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Biological process	Stress response
Ligand	Metal-binding Zinc
Molecular function	Lyase
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: UniProtKB-KW
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 – 185	185	Lactoylglutathione lyase		PRO_0000168084
Sites
	Metal binding	96	1	Zinc Potential
	Metal binding	99	1	Zinc Potential
	Metal binding	113	1	Zinc Potential
	Metal binding	124	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q42891-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0D16247209138CA1	FASTA	185	20,717
	10 20 30 40 50 60 MASESKDSPS NNPGLHATPD EATKGYFLQQ TMFRIKDPKV SLEFYSKVLG MSLLKRLDFP 70 80 90 100 110 120 EMKFSLYFMG YEDTASAPSD PVERTAWTFS QKSTLELTHN WGTESDPNFT GYHNGNSEPR 130 140 150 160 170 180 GFGHIGVTVD DVYKACERFE SLGVEFVKKP LDGKMKGIAF IKDPDGYWIE IFDTKIIKDA AGSAS

References

[1]	"Molecular characterization of glyoxalase-I from a higher plant; upregulation by stress." Espartero J., Sanchez-Aguayo I., Pardo J.M. Plant Mol. Biol. 29:1223-1233(1995) [PubMed: 8616220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Rutgers.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z48183 mRNA. Translation: CAA88233.1.
PIR	S62723.
UniGene	Les.40
3D structure databases
HSSP	HSSP built from PDB template 1QIP based on UniProtKB Q04760.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.4.1.5. 281054.
Family and domain databases
InterPro	IPR004360. Glyas_bleo-R_dOase. IPR004361. Glyoxalase_1. IPR018146. Glyoxalase_1_CS. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00068. glyox_I. 1 hit.
PROSITE	PS00934. GLYOXALASE_I_1. 1 hit. PS00935. GLYOXALASE_I_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LGUL_SOLLC

Accession

Primary (citable) accession number: Q42891

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	September 22, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)