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Reviewed, UniProtKB/Swiss-Prot B7MBI8 (GLO2_ECO45)

Last modified February 9, 2010. Version 11. 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: ECS88_0227
OrganismEscherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP]
Taxonomic identifier585035 [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_1000144758

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
B7MBI8-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: F00DEE1926D38C5A

FASTA25128,476
        10         20         30         40         50         60 
MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIS ANNWQPEAIF LTHHHHDHVG 

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

       130        140        150        160        170        180 
PYLFCGDTLF SGGCGRLFEG TPSQMYQSIK 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
CU928161 Genomic DNA. Translation: CAR01582.1.
RefSeqYP_002390061.1.

3D structure databases

SMRB7MBI8. Positions 1-251.
ModBaseSearch...

Genome annotation databases

GeneID7128845.
GenomeReviewsGene locus ECS88_0227 in contig CU928161_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753931.
OMAWCAHEYT.

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_ECO45
AccessionPrimary (citable) accession number: B7MBI8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 9, 2010
This is version 11 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