O04885 (LGUL_BRAJU) 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=Glx I
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase

Gene names

Name:

GLY I

Organism

Brassica juncea (Indian mustard) (Sinapis juncea)

Taxonomic identifier

3707 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica

Protein attributes

Sequence length	185 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
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_0000168082
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)
	O04885 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 19C161DFFCD5682E	FASTA	185	20,783
	10 20 30 40 50 60 MASEAKESPA NNPGLSTVRD EATKGYIMQQ TMFRVKDPKA SLDFYSRVLG MSLLKRLDFS 70 80 90 100 110 120 EMKFSLYFLG YEDTSTAPTD PTERTVWTFG RPATIELTHN WGTESDPEFK GYHNGNSEPR 130 140 150 160 170 180 GFGHIGVTVD DVHKACERFE QLGVEFVKKP HDGKMKNIAF IKDPDGYWIE IFDLKTIGTT AGNAA

References

[1]	Sopory S.K. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Pusa Bold. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13239 mRNA. Translation: CAA73691.1.
3D structure databases
ProteinModelPortal	O04885.
SMR	O04885. Positions 20-179.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	4.4.1.5. 941.
Family and domain databases
InterPro	IPR004360. Glyas_Fos-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_BRAJU

Accession

Primary (citable) accession number: O04885

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	September 21, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program