Reviewed, UniProtKB/Swiss-Prot B7M211 (GLO2_ECO8A)

Names and origin

Protein names

Recommended name:
    Hydroxyacylglutathione hydrolase
    EC=3.1.2.6
Alternative name(s):
    Glyoxalase II
      Short name=Glx II

Gene names

Name:	gloB
Ordered Locus Names:	ECIAI1_0220

Organism

Escherichia coli O8 (strain IAI1) [Complete proteome] [HAMAP]

Taxonomic identifier

585034 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid By similarity. HAMAP MF_01374
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP MF_01374
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_01374
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP MF_01374
Subunit structure	Monomer By similarity. HAMAP MF_01374
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	hydroxyacylglutathione hydrolase activity Inferred from electronic annotation. Source: HAMAP zinc 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 – 251	251	Hydroxyacylglutathione hydrolase HAMAP MF_01374		PRO_1000144761
Sites
	Metal binding	53	1	Zinc 1 By similarity
	Metal binding	55	1	Zinc 1 By similarity
	Metal binding	57	1	Zinc 2 By similarity
	Metal binding	58	1	Zinc 2 By similarity
	Metal binding	110	1	Zinc 1 By similarity
	Metal binding	127	1	Zinc 1 By similarity
	Metal binding	127	1	Zinc 2 By similarity
	Metal binding	165	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7M211-1 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: D9772CF8AED4FD29	FASTA	251	28,450
	10 20 30 40 50 60 MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIT ANNWQPEAIF LTHHHHDHVG 70 80 90 100 110 120 GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK 130 140 150 160 170 180 PYLFCGDTLF SGGCGRLFEG TASQMYQSLN KLSALPDDTL VCCAHEYTLS NMKFALSILP 190 200 210 220 230 240 HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER 250 FAWLRSKKDR F

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928160 Genomic DNA. Translation: CAQ97095.1.
RefSeq	YP_002385700.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7124284.
GenomeReviews	Gene locus ECIAI1_0220 in contig CU928160_GR.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01374. Glyoxalase_2. [Tree]
InterPro	IPR001279. Blactmase-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR03413. GSH_gloB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLO2_ECO8A

Accession

Primary (citable) accession number: B7M211

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 24, 2009
Last modified:	February 9, 2010
This is version 10 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)