Reviewed, UniProtKB/Swiss-Prot P0AC82 (LGUL_ECO57)

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:	gloA
Ordered Locus Names:	Z2669, ECs2360

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 nickel ion per subunit By similarity.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Ligand	Metal-binding Nickel
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	lactoylglutathione lyase activity Inferred from electronic annotation. Source: EC nickel 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 – 135	135	Lactoylglutathione lyase		PRO_0000168089
Sites
	Metal binding	5	1	Nickel By similarity
	Metal binding	56	1	Nickel By similarity
	Metal binding	74	1	Nickel By similarity
	Metal binding	122	1	Nickel By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AC82-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: A53FC5412B9A6CE3	FASTA	135	14,920
	10 20 30 40 50 60 MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN 70 80 90 100 110 120 WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA GPVKGGTTVI AFVEDPDGYK 130 IELIEEKDAG RGLGN

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG56640.1. BA000007 Genomic DNA. Translation: BAB35783.1.
PIR	D85772. H90923.
RefSeq	NP_288087.1. NP_310387.1.
3D structure databases
SMR	P0AC82. Positions 1-126.
ModBase	Search...
Genome annotation databases
GeneID	912789. 961613.
GenomeReviews	Gene locus Z2669 in contig AE005174_GR. Gene locus ECs2360 in contig BA000007_GR.
KEGG	ece:Z2669. ecs:ECs2360.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0AC82.
OMA	PGPMKHG.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2360-MON.
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]
ProDom	PD002334. Gly_diox. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_ECO57

Accession

Primary (citable) accession number: P0AC82
Secondary accession number(s): P77036, Q59384

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)