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Reviewed, UniProtKB/Swiss-Prot A5UF43 (GLO2_HAEIG)

Last modified February 9, 2010. Version 21. 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

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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: CGSHiGG_01615
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_0000309649

Sites

Metal binding521Zinc 1 By similarity
Metal binding541Zinc 1 By similarity
Metal binding561Zinc 2 By similarity
Metal binding571Zinc 2 By similarity
Metal binding1081Zinc 1 By similarity
Metal binding1251Zinc 1 By similarity
Metal binding1251Zinc 2 By similarity
Metal binding1631Zinc 2 By similarity

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Sequences

Sequence LengthMass (Da)Tools
A5UF43-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 358B8F51657451B8

FASTA24327,336
        10         20         30         40         50         60 
MLFALPALND NYIWLYQREN LPLIIVDLPE TDKLFAWLDK QNATVEAVLL THEHDDHTQG 

        70         80         90        100        110        120 
VSAFKKRYPT VPIYGPQECE KKGATQIVNE GKILTANYQI DVIPTGGHTK QHVSFLVDNH 

       130        140        150        160        170        180 
LFCGDALFSA GCGRVFTGNY ALMFEGLQRL NTLPDETIVC PAHEYTLGNL AFAETVLVDK 

       190        200        210        220        230        240 
SAVEKSAVEK SAVEKQRIFV ETQRAENKPS LPTTLKLERE INPFLQAKTL EEFTALRKAK 


DIF

« Hide

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References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed: 17550610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000672 Genomic DNA. Translation: ABQ99398.1.
RefSeqYP_001291782.1.

3D structure databases

SMRA5UF43. Positions 3-243.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5UF43.

Genome annotation databases

GeneID5226872.
GenomeReviewsGene locus CGSHiGG_01615 in contig CP000672_GR.
KEGGhiq:CGSHiGG_01615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
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...

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Entry information

Entry nameGLO2_HAEIG
AccessionPrimary (citable) accession number: A5UF43
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 10, 2007
Last modified: February 9, 2010
This is version 21 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)

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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