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Reviewed, UniProtKB/Swiss-Prot P0AC84 (GLO2_ECOLI)

Last modified February 9, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. 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. Ref.5

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2. HAMAP MF_01374

Subunit structure

Monomer. Ref.5

Miscellaneous

Mn2+ and Co2+ can substitute for zinc in reconstitution experiments. HAMAP 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 HAMAP MF_01374

Vmax=122 µmol/min/mg enzyme

Mass spectrometry

Molecular mass is 28432 Da from positions 1 - 251. Determined by ESI. Ref.5

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Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmethylglyoxal catabolic process to D-lactate Ref.5

Inferred from direct assay. Source: UniProtKB

   Molecular functionhydroxyacylglutathione hydrolase activity Ref.5

Inferred from direct assay. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_0000192351

Sites

Metal binding531Zinc 1 By similarity
Metal binding551Zinc 1 By similarity
Metal binding571Zinc 2 By similarity
Metal binding581Zinc 2 By similarity
Metal binding1101Zinc 1 By similarity
Metal binding1271Zinc 1 By similarity
Metal binding1271Zinc 2 By similarity
Metal binding1651Zinc 2 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P0AC84-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: D59948B6E12809F5

FASTA25128,434
        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

« Hide

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References

« Hide '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: 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]"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: 17196158] [Abstract]
Cited for: CHARACTERIZATION, COFACTOR, SUBUNIT, MASS SPECTROMETRY.
Strain: K12 / MG1655 / ATCC 47076.

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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.
PIRF64745.
RefSeqAP_000867.1.
NP_414748.1.

3D structure databases

SMRP0AC84. Positions 1-251.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0AC84.

Genome annotation databases

GeneID944902.
GenomeReviewsGene locus JW0202 in contig AP009048_GR.
Gene locus b0212 in contig U00096_GR.
KEGGecj:JW0202.
eco:b0212.

Organism-specific databases

EchoBASEEB3114.
EcoGeneEG13330. gloB.
CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
HOGENOMHBG753931.
OMAWCAHEYT.

Enzyme and pathway databases

BioCycEcoCyc:GLYOXII-MONOMER.
ECOL168927:B0212-MONOMER.
MetaCyc:GLYOXII-MONOMER.

Gene expression databases

GenevestigatorP0AC84.

Family and domain databases

HAMAPMF_01374. Glyoxalase_2.
[Tree]
InterProIPR001279. Blactmase-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR03413. GSH_gloB. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameGLO2_ECOLI
AccessionPrimary (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: February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents