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B0CIU0 (GLO2_BRUSI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:BSUIS_A1776
OrganismBrucella suis (strain ATCC 23445 / NCTC 10510) [Complete proteome] [HAMAP]
Taxonomic identifier470137 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length260 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 – 260260Hydroxyacylglutathione hydrolase HAMAP-Rule MF_01374
PRO_1000087278

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding651Zinc 2 By similarity
Metal binding661Zinc 2 By similarity
Metal binding1191Zinc 1 By similarity
Metal binding1381Zinc 1 By similarity
Metal binding1381Zinc 2 By similarity
Metal binding1761Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CIU0 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 56A7D32D568319BA

FASTA26029,140
        10         20         30         40         50         60 
MHRMEQRLEI EQFICRSDNY GVLIHDPESA LTATIDAPDA YAIEAALERR GWTLDFIFTT 

        70         80         90        100        110        120 
HHHLDHVEGN EPLKEKFGVS IIGPEAEKAK IPGIDRTVKG GDEFTFGLFK VKVISTPGHT 

       130        140        150        160        170        180 
AGGISYYLPD AKVVFTGDTL FALGCGRLFE GTPATMFHSL EKLVALPGDT ALYCGHEYTQ 

       190        200        210        220        230        240 
NNARFALTID PDNSALKERA KEIARLRAHE RMTLPSTIAL EMATNPFLRW HDRTIRARLG 

       250        260 
LQDAPDEAVF AEIRKRKDMF 

« Hide

References

[1]"Brucella suis ATCC 23445 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23445 / NCTC 10510.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000911 Genomic DNA. Translation: ABY38793.1.
RefSeqYP_001628363.1. NC_010169.1.

3D structure databases

ProteinModelPortalB0CIU0.
ModBaseSearch...

Protein-protein interaction databases

STRING470137.BSUIS_A1776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY38793; ABY38793; BSUIS_A1776.
GeneID5837838.
KEGGbmt:BSUIS_A1776.
PATRIC17871166. VBIBruSui83806_3363.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
HOGENOMHOG000058041.
KOK01069.
OMALTHHHQD.
ProtClustDBCLSK898025.

Enzyme and pathway databases

BioCycBSUI470137:GJIC-1767-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_BRUSI
AccessionPrimary (citable) accession number: B0CIU0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families