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Reviewed, UniProtKB/Swiss-Prot B7LW87 (GLO2_ESCF3)

Last modified February 9, 2010. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Ordered Locus Names: EFER_0241
OrganismEscherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]
Taxonomic identifier585054 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceInferred 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
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionhydroxyacylglutathione 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_1000144767

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

Sequences

Sequence LengthMass (Da)Tools
B7LW87-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: B8DAF8581C6258AA

FASTA25128,459
        10         20         30         40         50         60 
MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIA ANNWQPEAIF LTHHHHDHVG 

        70         80         90        100        110        120 
GVKELVKKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH EFSVIATPGH TLGHICYFSK 

       130        140        150        160        170        180 
PYLFCGDTLF SGGCGRLFEG TPSQMYQSLK KLSALPDDTL VCCAHEYTLS NMKFALSILP 

       190        200        210        220        230        240 
HDLSINDYYR KVKELRAKNQ ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER 

       250 
FAWLRSKKDR F 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928158 Genomic DNA. Translation: CAQ87810.1.
RefSeqYP_002381453.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7120940.
GenomeReviewsGene locus EFER_0241 in contig CU928158_GR.
KEGGefe:EFER_0241.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753931.

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...

Entry information

Entry nameGLO2_ESCF3
AccessionPrimary (citable) accession number: B7LW87
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 9, 2010
This is version 12 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)

Relevant documents

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