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Q57AW2 (GLO2_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BruAb1_1912
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length257 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: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_0000309631

Sites

Metal binding581Zinc 1 By similarity
Metal binding601Zinc 1 By similarity
Metal binding621Zinc 2 By similarity
Metal binding631Zinc 2 By similarity
Metal binding1161Zinc 1 By similarity
Metal binding1351Zinc 1 By similarity
Metal binding1351Zinc 2 By similarity
Metal binding1731Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57AW2 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: EE8B77529780D96B

FASTA25728,716
        10         20         30         40         50         60 
MEQRLEIEQF ICRSDNYGVL IHDPESALTA TIDAPDAYAI EAALERRGWT LDFIFTTHHH 

        70         80         90        100        110        120 
LDHVEGNEPL KEKFGVSIIG PEAEKAKIPG IDRTVKGGDE FTFGLFKVKV ISTPGHTAGG 

       130        140        150        160        170        180 
ISYYLPDAKV VFTGDTLFAL GCGRLFEGTP ATMFHSLEKL VALPGDTALY CGHEYTQNNA 

       190        200        210        220        230        240 
RFALTIDPDN SALKERAKEI ARLRAHERMT LPSTIALEMA TNPFLRWHDR TIRARLGLQD 

       250 
APDEAVFAEI RKRKDMF 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX75222.1.
RefSeqYP_222583.1. NC_006932.1.

3D structure databases

HSSPHSSP built from PDB template 1XM8 based on UniProtKB Q9SID3.
ProteinModelPortalQ57AW2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3340934.
GenomeReviewsGene locus BruAb1_1912 in contig AE017223_GR.
KEGGbmb:BruAb1_1912.
PATRIC17825650. VBIBruAbo15061_2018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753931.
OMAIGCGRVF.
PhylomeDBQ57AW2.
ProtClustDBCLSK898025.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_1912-MONOMER.

Family and domain databases

HAMAPMF_01374. Glyoxalase_2.
[Tree]
InterProIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
KOK01069.
PANTHERPTHR11935:SF7. PTHR11935:SF7. 1 hit.
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR03413. GSH_gloB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLO2_BRUAB
AccessionPrimary (citable) accession number: Q57AW2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 10, 2005
Last modified: January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families