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Q2YLU8 (GLO2_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. 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:BAB1_1936
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [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-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 By similarity.

Pathway

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

Subunit structure

Monomer By similarity.

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)
   Biological_processglutathione biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionhydroxyacylglutathione hydrolase activity

Inferred from electronic annotation. Source: HAMAP

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-Rule MF_01374
PRO_0000309632

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
Q2YLU8 [UniParc].

Last modified February 7, 2006. 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]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ11892.1.
RefSeqYP_415275.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YLU8.
ModBaseSearch...

Protein-protein interaction databases

STRING359391.BAB1_1936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ11892; CAJ11892; BAB1_1936.
GeneID3788401.
KEGGbmf:BAB1_1936.
PATRIC17846949. VBIBruMel86222_2015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
HOGENOMHOG000058041.
KOK01069.
OMALTHHHQD.
ProtClustDBCLSK898025.

Enzyme and pathway databases

BioCycBMEL359391:GJOQ-1987-MONOMER.
UniPathwayUPA00619; UER00676.

Family and domain databases

HAMAPMF_01374. Glyoxalase_2.
InterProIPR001279. Beta-lactamas-like.
IPR017782. Hydroxyacylglutathione_Hdrlase.
[Graphical view]
PANTHERPTHR11935:SF7. PTHR11935:SF7. 1 hit.
PfamPF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFPIRSF005457. Glx. 1 hit.
SMARTSM00849. Lactamase_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR03413. GSH_gloB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLO2_BRUA2
AccessionPrimary (citable) accession number: Q2YLU8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 44 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 2308

Brucella abortus (strain 2308): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families