Reviewed, UniProtKB/Swiss-Prot P0AC81 (LGUL_ECOLI)

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:	b1651, JW1643

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [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	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic activity	(R)-S-lactoylglutathione = glutathione + methylglyoxal.
Cofactor	Binds 1 nickel ion per subunit.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the glyoxalase I family.
Mass spectrometry	Molecular mass is 14919 Da from positions 1 - 135. Determined by ESI. Ref.2

Ontologies

Keywords
Ligand	Metal-binding Nickel
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Molecular function	lactoylglutathione lyase activity Inferred from electronic annotation. Source: EC nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-551143,EBI-542092
rhaM	P32156	1	EBI-551143,EBI-1134000

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 135

135

Lactoylglutathione lyase

PRO_0000168088

Sites

Metal binding

5

1

Nickel

Metal binding

56

1

Nickel

Metal binding

74

1

Nickel

Metal binding

122

1

Nickel

Secondary structure

1

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135

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

13 – 22

10

Beta strand

27 – 34

8

Turn

35 – 38

4

Beta strand

39 – 47

9

Turn

49 – 51

3

Beta strand

54 – 60

7

Beta strand

70 – 78

9

Helix

82 – 91

10

Beta strand

95 – 102

8

Beta strand

109 – 114

6

Beta strand

120 – 125

6

Sequences

	Sequence		Length	Mass (Da)
	P0AC81-1 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences." Clugston S.L., Daub E., Kinach R., Miedema D., Barnard J.F.J., Honek J.F. Gene 186:103-111(1997) [PubMed: 9047352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions." Clugston S.L., Barnard J.F.J., Kinach R., Miedema D., Ruman R., Daub E., Honek J.F. Biochemistry 37:8754-8763(1998) [PubMed: 9628737] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, CHARACTERIZATION, MASS SPECTROMETRY.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Mizugaki M., Miura K., Yonezawa M., Hishinuma T., Tomioka Y. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation." He M.M., Clugston S.L., Honek J.F., Matthews B.W. Biochemistry 39:8719-8727(2000) [PubMed: 10913283] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U57363 Genomic DNA. Translation: AAC27133.1.
U00096 Genomic DNA. Translation: AAC74723.1.
AP009048 Genomic DNA. Translation: BAE76494.1.
D86931 Genomic DNA. Translation: BAA13187.1.

PIR

E64922.

RefSeq

AP_002273.1.
NP_416168.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F9Z	X-ray	1.50	A/B	1-135	[»]
1FA5	X-ray	1.80	A/B	1-135	[»]
1FA6	X-ray	1.90	A/B	1-135	[»]
1FA7	X-ray	1.90	A/B	1-135	[»]
1FA8	X-ray	1.70	A/B	1-135	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AC81. 5 interactions.

STRING

P0AC81.

Genome annotation databases

GeneID

946161.

GenomeReviews

Gene locus JW1643 in contig AP009048_GR.
Gene locus b1651 in contig U00096_GR.

KEGG

ecj:JW1643.
eco:b1651.

Organism-specific databases

EchoBASE

EB3197.

EcoGene

EG13421. gloA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AC81.

OMA

PGPMKHG

Enzyme and pathway databases

BioCyc

EcoCyc:GLYOXI-MON.
ECOL168927:B1651-MON.
MetaCyc:GLYOXI-MON.

Gene expression databases

Genevestigator

P0AC81.

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_ECOLI

Accession

Primary (citable) accession number: P0AC81
Secondary accession number(s): P77036, Q2MB62, Q59384

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	November 24, 2009
This is version 40 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)