Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AC83 (LGUL_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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:
Lactoylglutathione lyase

EC=4.4.1.5
Alternative name(s):
Aldoketomutase
Glyoxalase I
Short name=Glx I
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase
Gene names
Name:gloA
Ordered Locus Names:SF1678, S1810
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
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. In the homodimer, two nickel ions are bound between subunits By similarity.

Pathway

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

Subunit structure

Homodimer By similarity.

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: UniProtKB-EC

metal 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_0000168092

Sites

Active site1221Proton donor/acceptor By similarity
Metal binding51Nickel; via tele nitrogen; shared with dimeric partner By similarity
Metal binding561Nickel; shared with dimeric partner By similarity
Metal binding741Nickel; via tele nitrogen By similarity
Metal binding1221Nickel By similarity
Binding site91Substrate; shared with dimeric partner By similarity
Binding site601Substrate; shared with dimeric partner By similarity
Binding site741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AC83 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: A53FC5412B9A6CE3

FASTA13514,920
        10         20         30         40         50         60 
MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET EEAVIELTYN 

        70         80         90        100        110        120 
WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA GPVKGGTTVI AFVEDPDGYK 

       130 
IELIEEKDAG RGLGN 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43259.1.
AE014073 Genomic DNA. Translation: AAP17147.1.
RefSeqNP_707552.1. NC_004337.2.
NP_837338.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AC83.
SMRP0AC83. Positions 1-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF1678.

Proteomic databases

PaxDbP0AC83.
PRIDEP0AC83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43259; AAN43259; SF1678.
AAP17147; AAP17147; S1810.
GeneID1024857.
1078150.
KEGGsfl:SF1678.
sfx:S1810.
PATRIC18705008. VBIShiFle31049_2002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0346.
HOGENOMHOG000232011.
KOK01759.
OMATHNWDTP.
OrthoDBEOG6DVJXX.
ProtClustDBPRK10291.

Enzyme and pathway databases

UniPathwayUPA00619; UER00675.

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00068. glyox_I. 1 hit.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_SHIFL
AccessionPrimary (citable) accession number: P0AC83
Secondary accession number(s): P77036, Q59384
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways