P0AC84 (GLO2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	yafR
Ordered Locus Names:	b0212, JW0202

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. HAMAP-Rule MF_01374
Catalytic activity	S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP-Rule MF_01374
Cofactor	Binds 2 zinc ions per subunit. Ref.5
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP-Rule MF_01374
Subunit structure	Monomer. Ref.5
Miscellaneous	Mn2+ and Co2+ can substitute for zinc in reconstitution experiments. HAMAP-Rule MF_01374
Sequence similarities	Belongs to the metallo-beta-lactamase superfamily. Glyoxalase II family.
Biophysicochemical properties	Kinetic parameters: KM=184 µM for S-D-lactoyl-glutathione Vmax=122 µmol/min/mg enzyme
Mass spectrometry	Molecular mass is 28432 Da from positions 1 - 251. Determined by ESI. Ref.5

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione biosynthetic process Inferred from electronic annotation. Source: InterPro methylglyoxal catabolic process to D-lactate Inferred from direct assay Ref.5. Source: EcoCyc
Molecular_function	hydroxyacylglutathione hydrolase activity Inferred from direct assay Ref.5. Source: EcoCyc zinc ion binding Inferred from direct assay Ref.5. Source: EcoCyc
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-Rule MF_01374		PRO_0000192351
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)
	P0AC84 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: D59948B6E12809F5	FASTA	251	28,434
	10 20 30 40 50 60 MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIA ANNWQPEAIF LTHHHHDHVG 70 80 90 100 110 120 GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK 130 140 150 160 170 180 PYLFCGDTLF SGGCGRLFEG TASQMYQSLK KLSALPDDTL VCCAHEYTLS NMKFALSILP 190 200 210 220 230 240 HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER 250 FAWLRSKKDR F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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]	"Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme." O'Young J., Sukdeo N., Honek J.F. Arch. Biochem. Biophys. 459:20-26(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, COFACTOR, SUBUNIT, MASS SPECTROMETRY. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U70214 Genomic DNA. Translation: AAB08634.1. U00096 Genomic DNA. Translation: AAC73317.1. AP009048 Genomic DNA. Translation: BAA77883.1.
PIR	F64745.
RefSeq	NP_414748.1. NC_000913.2. YP_488509.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AC84.
SMR	P0AC84. Positions 1-251.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48248N.
IntAct	P0AC84. 1 interaction.
MINT	MINT-1295781.
STRING	511145.b0212.
Proteomic databases
PaxDb	P0AC84.
PRIDE	P0AC84.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73317; AAC73317; b0212. BAA77883; BAA77883; BAA77883.
GeneID	12933011. 944902.
KEGG	ecj:Y75_p0203. eco:b0212.
PATRIC	32115537. VBIEscCol129921_0214.
Organism-specific databases
EchoBASE	EB3114.
EcoGene	EG13330. gloB.
Phylogenomic databases
eggNOG	COG0491.
HOGENOM	HOG000058041.
KO	K01069.
OMA	PFMRVHE.
ProtClustDB	PRK10241.
Enzyme and pathway databases
BioCyc	EcoCyc:GLYOXII-MONOMER. ECOL316407:JW0202-MONOMER. MetaCyc:GLYOXII-MONOMER.
SABIO-RK	P0AC84.
UniPathway	UPA00619; UER00676.
Gene expression databases
Genevestigator	P0AC84.
Family and domain databases
HAMAP	MF_01374. Glyoxalase_2.
InterPro	IPR001279. Beta-lactamas-like. IPR017782. Hydroxyacylglutathione_Hdrlase. [Graphical view]
PANTHER	PTHR11935:SF7. PTHR11935:SF7. 1 hit.
Pfam	PF00753. Lactamase_B. 1 hit. [Graphical view]
PIRSF	PIRSF005457. Glx. 1 hit.
SMART	SM00849. Lactamase_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR03413. GSH_gloB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GLO2_ECOLI

Accession

Primary (citable) accession number: P0AC84
Secondary accession number(s): Q47677

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program