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Q1H188 (GLO2_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Mfla_1481
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Methylophilales › Methylophilaceae › Methylobacillus ›

Protein attributes

Sequence length250 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 – 250250Hydroxyacylglutathione hydrolase HAMAP-Rule MF_01374
PRO_1000144772

Sites

Metal binding531Zinc 1 By similarity
Metal binding551Zinc 1 By similarity
Metal binding571Zinc 2 By similarity
Metal binding581Zinc 2 By similarity
Metal binding1111Zinc 1 By similarity
Metal binding1281Zinc 1 By similarity
Metal binding1281Zinc 2 By similarity
Metal binding1661Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1H188 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 5AE863CAB2E36003

FASTA25027,188
        10         20         30         40         50         60 
MFEIIPILAF EDNYIWLLHQ HGHALVVDPG DAHPVLEILD ARGLQLRAIL VTHHHQDHTG 

        70         80         90        100        110        120 
GVEELIQATS AQVFAPAKEQ FSFPHHPVTA GDRLDIPGIA LSLSVLDVPG HTVGHVAYYG 

       130        140        150        160        170        180 
DGMLFSGDTL FGAGCGRLFE GTPGQMYSSL QQLAQLPVNT RVYCGHEYTE RNLAFALSLE 

       190        200        210        220        230        240 
PHHEALLSRR EATAALRAQG LPSLPSSMAL ELATNPFLRC HEPGIIAASK SAATDPVSVF 

       250 
AAIREMRNHF

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000284 Genomic DNA. Translation: ABE49749.1.
RefSeqYP_545590.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H188.
ModBaseSearch...

Protein-protein interaction databases

STRING265072.Mfla_1481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE49749; ABE49749; Mfla_1481.
GeneID4000453.
KEGGmfa:Mfla_1481.
PATRIC32268693. VBIMetFla97085_1573.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0491.
HOGENOMHOG000058041.
KOK01069.
OMALTHHHQD.
ProtClustDBCLSK2529445.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-1543-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_METFK
AccessionPrimary (citable) accession number: Q1H188
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 27, 2006
Last modified: May 1, 2013
This is version 49 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

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