Lactoylglutathione lyase - Escherichia coli (strain K12)

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P0AC81 (LGUL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	gloA
Ordered Locus Names:	b1651, JW1643

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	135 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.
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 Reference proteome
Gene Ontology (GO)
Biological_process	methylglyoxal catabolic process to D-lactate Inferred from mutant phenotype PubMed 9489668. Source: EcoCyc
Molecular_function	lactoylglutathione lyase activity Inferred from direct assay Ref.2. Source: EcoCyc nickel cation binding Inferred from direct assay Ref.2. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	2	EBI-551143,EBI-542092

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

Nickel

Metal binding

Nickel

Metal binding

Nickel

Metal binding

122

Nickel

Secondary structure

135

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AC81 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: A53FC5412B9A6CE3
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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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_416168.1. NC_000913.2.
YP_489915.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AC81.

SMR

P0AC81. Positions 1-126.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47995N.

IntAct

P0AC81. 5 interactions.

MINT

MINT-1255986.

STRING

511145.b1651.

Proteomic databases

PaxDb

P0AC81.

PRIDE

P0AC81.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74723; AAC74723; b1651.
BAE76494; BAE76494; BAE76494.

GeneID

12930393.
946161.

KEGG

ecj:Y75_p1628.
eco:b1651.

PATRIC

32118604. VBIEscCol129921_1722.

Organism-specific databases

EchoBASE

EB3197.

EcoGene

EG13421. gloA.

Phylogenomic databases

eggNOG

COG0346.

HOGENOM

HOG000232011.

K01759.

OMA

VREPGPM.

ProtClustDB

PRK10291.

Enzyme and pathway databases

BioCyc

EcoCyc:GLYOXI-MONOMER.
ECOL316407:JW1643-MONOMER.
MetaCyc:GLYOXI-MONOMER.

SABIO-RK

P0AC81.

UniPathway

UPA00619; UER00675.

Gene expression databases

Genevestigator

P0AC81.

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...

Other

EvolutionaryTrace

P0AC81.

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:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents