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Reviewed, UniProtKB/Swiss-Prot P0A1Q3 (LGUL_SALTI)

Last modified November 3, 2009. Version 30. 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

Names and origin

Protein namesRecommended name:
    Lactoylglutathione lyase
    EC=4.4.1.5
Alternative name(s):
    Methylglyoxalase
    Aldoketomutase
    Glyoxalase I
      Short name=Glx I
    Ketone-aldehyde mutase
    S-D-lactoylglutathione methylglyoxal lyase
Gene names
Name: gloA
Ordered Locus Names: STY1687, t1303
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity.

Catalytic activity

(R)-S-lactoylglutathione = glutathione + methylglyoxal.

Cofactor

Binds 1 nickel ion per subunit By similarity.

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.

Sequence similarities

Belongs to the glyoxalase I family.

Ontologies

Keywords
   LigandMetal-binding
Nickel
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionlactoylglutathione lyase activity

Inferred from electronic annotation. Source: EC

nickel ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 135135Lactoylglutathione lyase
PRO_0000168090

Sites

Metal binding51Nickel By similarity
Metal binding561Nickel By similarity
Metal binding741Nickel By similarity
Metal binding1221Nickel By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A1Q3-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 35844EF34EAB5CDA

FASTA13514,822
        10         20         30         40         50         60 
MRLLHTMLRV GDLQRSIAFY TNVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN 

        70         80         90        100        110        120 
WGVESYDMGN AYGHIALSVD NAAEACERIR QNGGNVTREA GPVKGGSTII AFVEDPDGYK 

       130 
IELIEAKDAG RGLGN 

« Hide

References

Cross-references

Sequence databases

AL627271 Genomic DNA. Translation: CAD01932.1.
AE014613 Genomic DNA. Translation: AAO68953.1.
RefSeqNP_456095.1.
NP_805104.1.

3D structure databases

HSSPHSSP built from PDB template 1F9Z based on UniProtKB Q59384.
SMRP0A1Q3. Positions 1-125.
ModBaseSearch...

Proteomic databases

PRIDEP0A1Q3.

Genome annotation databases

GeneID1070728.
1248061.
GenomeReviewsGene locus t1303 in contig AE014613_GR.
Gene locus STY1687 in contig AL513382_GR.
KEGGstt:t1303.
sty:STY1687.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A1Q3.
OMAPGPMKHG.

Enzyme and pathway databases

BioCycSENT209261:T1303-MON.
SENT220341:STY1687-MON.
BRENDA4.4.1.5. 3716.

Family and domain databases

InterProIPR004360. Glyas_bleo-R_dOase.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
ProDomPD002334. Gly_diox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00068. glyox_I. 1 hit.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_SALTI
AccessionPrimary (citable) accession number: P0A1Q3
Secondary accession number(s): Q60003
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 3, 2009
This is version 30 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)

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