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Q6FYC3 (GLO2_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:BQ13520
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length253 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 – 253253Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_1000068209

Sites

Metal binding541Zinc 1 By similarity
Metal binding561Zinc 1 By similarity
Metal binding581Zinc 2 By similarity
Metal binding591Zinc 2 By similarity
Metal binding1121Zinc 1 By similarity
Metal binding1311Zinc 1 By similarity
Metal binding1311Zinc 2 By similarity
Metal binding1691Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FYC3 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 2E5A18012C5451B4

FASTA25328,958
        10         20         30         40         50         60 
MLIEQFICRE DNFGVLIHDE RSGYTAAIDA PESKAICSAL KRRNWTLQTI FVTHHHHDHI 

        70         80         90        100        110        120 
EALAELKQIY KAVVIGPEAE KEKIGHLDQA LQPDESLFFG THTLLALSTP GHTLGSLSYY 

       130        140        150        160        170        180 
FPQENLLFSG DTLFSLGCGR LFEGTPAQML NSFKKLRQLP DETLLYCGHE YTKTNALFAL 

       190        200        210        220        230        240 
TLDSHNQKLH QRVEDVFLLR AKNAMTLPVT LGQEKATNPF LRWDDRTLRK NLAMEKETDE 

       250 
EVFAEIRKRK DNF 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26810.1.
RefSeqYP_032866.1. NC_005955.1.

3D structure databases

HSSPHSSP built from PDB template 1XM8 based on UniProtKB Q9SID3.
ProteinModelPortalQ6FYC3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2867173.
GenomeReviewsGene locus BQ13520 in contig BX897700_GR.
KEGGbqu:BQ13520.
NMPDRfig|283165.1.peg.1136.
PATRIC31954181. VBIBarQui58630_1487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753931.
OMAIGCGRVF.
PhylomeDBQ6FYC3.
ProtClustDBCLSK927387.

Enzyme and pathway databases

BioCycBQUI283165:BQ13520-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_BARQU
AccessionPrimary (citable) accession number: Q6FYC3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 42 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