Q9ZS21 (LGUL_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lactoylglutathione lyase
EC=4.4.1.5

Alternative name(s):
Aldoketomutase
Glyoxalase I
Short name=GmGlyoxI
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase

Gene names

Name:

GLXI

Organism

Glycine max (Soybean) (Glycine hispida) [Reference proteome]

Taxonomic identifier

3847 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Active toward the hemithioacetal adducts formed by reacting methylglyoxal or phenylglyoxal with glutathione, homoglutathione or gamma-glutamylcysteine, showing no preference for homoglutathione adducts over glutathione adducts.
Catalytic activity	(R)-S-lactoylglutathione = glutathione + methylglyoxal. Ref.1
Cofactor	Binds 3 zinc ions per subunit, but unlike the enzyme from mammals, shows full activity in the absence of metal ions (Ref.1).
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Homodimer. Ref.1
Miscellaneous	Zinc ions may be required for the correct assembly of the enzyme but are not required for catalysis.
Sequence similarities	Belongs to the glyoxalase I family.
Biophysicochemical properties	Kinetic parameters: X. KM=24.83 µM for methylglyoxal-glutathione adduct Ref.1 KM=66.02 µM for methylglyoxal-homoglutathione adduct KM=201.78 µM for methylglyoxal-gamma-glutamylcysteine adduct KM=49.32 µM for phenylglyoxal-glutathione adduct KM=26.77 µM for phenylglyoxal-homoglutathione adduct KM=244.83 µM for phenylglyoxal-gamma-glutamylcysteine adduct Vmax=3.00 nmol/sec/mg enzyme toward methylglyoxal-glutathione adduct Vmax=5.70 nmol/sec/mg enzyme toward methylglyoxal-homoglutathione adduct Vmax=7.00 nmol/sec/mg enzyme toward methylglyoxal-gamma-glutamylcysteine adduct Vmax=24.38 nmol/sec/mg enzyme toward phenylglyoxal-glutathione adduct Vmax=21.10 nmol/sec/mg enzyme toward phenylglyoxal-homoglutathione adduct Vmax=83.64 nmol/sec/mg enzyme toward phenylglyoxal-gamma-glutamylcysteine adduct

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	lactoylglutathione 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	Lactoylglutathione lyase		PRO_0000391067
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)
	Q9ZS21 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 1A2C7BD375441915	FASTA	185	20,960
	10 20 30 40 50 60 MAAEPKESPS NNPGLHTTPD EATKGYIMQQ TMFRIKDPKV SLDFYSRVLG MSLLKRLDFP 70 80 90 100 110 120 EMKFSLYFMG YENTAEAPSN PIDKVVWTFS QKATIELTHN WGTESDPEFK GYHNGNSEPR 130 140 150 160 170 180 GFGHIGVTVD DTYKACERFQ NLGVEFVKKP EDGKMKGIAF IKDPDGYWIE IFDRKTIGNV TQTAA

References

[1]

"Cloning and characterization of glyoxalase I from soybean." Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R. Arch. Biochem. Biophys. 374:261-268(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Mandarin.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ010423 mRNA. Translation: CAA09177.1.
RefSeq	NP_001236152.1. NM_001249223.1.
UniGene	Gma.4045.
3D structure databases
ProteinModelPortal	Q9ZS21.
SMR	Q9ZS21. Positions 20-173.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	GLYMA11G20000.12; GLYMA11G20000.12; GLYMA11G20000. GLYMA11G20000.13; GLYMA11G20000.13; GLYMA11G20000.
GeneID	547667.
KEGG	gmx:547667.
Phylogenomic databases
KO	K01759.
Enzyme and pathway databases
BRENDA	4.4.1.5. 2483.
SABIO-RK	Q9ZS21.
UniPathway	UPA00619; UER00675.
Gene expression databases
Genevestigator	Q9ZS21.
Family and domain databases
InterPro	IPR004360. Glyas_Fos-R_dOase_dom. 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_SOYBN

Accession

Primary (citable) accession number: Q9ZS21

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 9, 2010
Last sequence update:	May 1, 1999
Last modified:	May 29, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program