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Q8ZRM2 (GLO2_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:STM0261
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid By similarity. Ref.2

Catalytic activity

S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate. HAMAP MF_01374

Cofactor

Binds 2 metal ions per subunit; upon overexpression in E.coli the enzyme purifies with various amounts of iron, zinc and manganese. Thus the endogenous metal is unknown. Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Hydroxyacylglutathione hydrolase HAMAP MF_01374
PRO_0000309704

Sites

Metal binding531Divalent metal cation 1
Metal binding551Divalent metal cation 1
Metal binding571Divalent metal cation 2
Metal binding581Divalent metal cation 2
Metal binding1101Divalent metal cation 1
Metal binding1271Divalent metal cation 1
Metal binding1271Divalent metal cation 2
Metal binding1651Divalent metal cation 2

Secondary structure

1 ................................................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZRM2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 5A8194A0C921C0E9

FASTA25128,633
        10         20         30         40         50         60 
MNLNSIPAFQ DNYIWVLTND EGRCVIVDPG EAAPVLKAIA EHKWMPEAIF LTHHHHDHVG 

        70         80         90        100        110        120 
GVKELLQHFP QMTVYGPAET QDKGATHLVG DGDTIRVLGE KFTLFATPGH TLGHVCYFSR 

       130        140        150        160        170        180 
PYLFCGDTLF SGGCGRLFEG TPSQMYQSLM KINSLPDDTL ICCAHEYTLA NIKFALSILP 

       190        200        210        220        230        240 
HDSFINEYYR KVKELRVKKQ MTLPVILKNE RKINLFLRTE DIDLINEINK ETILQQPEAR 

       250 
FAWLRSKKDT F

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity."
Campos-Bermudez V.A., Leite N.R., Krog R., Costa-Filho A.J., Soncini F.C., Oliva G., Vila A.J.
Biochemistry 46:11069-11079(2007) [PubMed: 17764159] [Abstract]
Cited for: FUNCTION, COFACTOR, STRUCTURE BY NMR, X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
Strain: ATCC 14028s / SGSG 2262.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006468 Genomic DNA. Translation: AAL19218.1.
RefSeqNP_459259.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QEDX-ray1.45A1-251[»]
ProteinModelPortalQ8ZRM2.
SMRQ8ZRM2. Positions 1-251.
ModBaseSearch...

Proteomic databases

PRIDEQ8ZRM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1251779.
GenomeReviewsGene locus STM0261 in contig AE006468_GR.
KEGGstm:STM0261.
NMPDRfig|99287.1.peg.252.
PATRIC32378813. VBISalEnt20916_0270.

Phylogenomic databases

HOGENOMHBG753931.
OMAITHHHRD.
ProtClustDBPRK10241.

Enzyme and pathway databases

BioCycSTYP99287:STM0261-MONOMER.
BRENDA3.1.2.6. 5542.

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_SALTY
AccessionPrimary (citable) accession number: Q8ZRM2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 53 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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