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P50107 (LGUL_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:GLO1
Ordered Locus Names:YML004C
ORF Names:YM9571.15C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Ref.1 Ref.2

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

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

Subunit structure

Monomer.

Miscellaneous

Present with 2570 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glyoxalase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Lactoylglutathione lyase
PRO_0000168087

Sites

Active site1631Proton donor/acceptor By similarity
Metal binding251Zinc; via tele nitrogen; shared with dimeric partner By similarity
Metal binding891Zinc; shared with dimeric partner By similarity
Metal binding1171Zinc; via tele nitrogen By similarity
Metal binding1631Zinc By similarity
Binding site291Substrate By similarity
Binding site931Substrate By similarity
Binding site1131Substrate By similarity
Binding site1171Substrate By similarity

Experimental info

Sequence conflict361T → A in CAC16163. Ref.2
Sequence conflict1561G → D in CAC16163. Ref.2
Sequence conflict1561G → D AA sequence Ref.5
Sequence conflict3221H → Y in CAC16163. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P50107 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9726A8253F53FB2B

FASTA32637,209
        10         20         30         40         50         60 
MSTDSTRYPI QIEKASNDPT LLLNHTCLRV KDPARTVKFY TEHFGMKLLS RKDFEEAKFS 

        70         80         90        100        110        120 
LYFLSFPKDD IPKNKNGEPD VFSAHGVLEL THNWGTEKNP DYKINNGNEE PHRGFGHICF 

       130        140        150        160        170        180 
SVSDINKTCE ELESQGVKFK KRLSEGRQKD IAFALGPDGY WIELITYSRE GQEYPKGSVG 

       190        200        210        220        230        240 
NKFNHTMIRI KNPTRSLEFY QNVLGMKLLR TSEHESAKFT LYFLGYGVPK TDSVFSCESV 

       250        260        270        280        290        300 
LELTHNWGTE NDPNFHYHNG NSEPQGYGHI CISCDDAGAL CKEIEVKYGD KIQWSPKFNQ 

       310        320 
GRMKNIAFLK DPDGYSIEVV PHGLIA 

« Hide

References

« Hide 'large scale' references
[1]"Identification of the structural gene for glyoxalase I from Saccharomyces cerevisiae."
Inoue Y., Kimura A.
J. Biol. Chem. 271:25958-25965(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 204508 / S288c.
[2]"Yeast glyoxalase I is a monomeric enzyme with two active sites."
Frickel E.M., Jemth P., Widersten M., Mannervik B.
J. Biol. Chem. 276:1845-1849(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Positive effect of GAC gene product on the mRNA level of glyoxalase I gene in Saccharomyces cerevisiae."
Inoue Y., Yano H., Ginya H., Tsuchiyama H., Murata K., Kimura A.
Biotechnol. Appl. Biochem. 14:391-394(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 310-326, PROTEIN SEQUENCE OF 39-45; 150-165 AND 311-323.
Strain: ATCC 26109 / X2180.
[6]"The primary structure of monomeric yeast glyoxalase I indicates a gene duplication resulting in two similar segments homologous with the subunit of dimeric human glyoxalase I."
Ridderstroem M., Mannervik B.
Biochem. J. 316:1005-1006(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99240 Genomic DNA. Translation: CAA67622.1.
AJ297938 Genomic DNA. Translation: CAC16163.1.
Z49810 Genomic DNA. Translation: CAA89948.1.
S80483 Genomic DNA. Translation: AAB21302.1.
BK006946 Genomic DNA. Translation: DAA09895.1.
PIRS55115.
RefSeqNP_013710.1. NM_001182359.1.

3D structure databases

ProteinModelPortalP50107.
SMRP50107. Positions 18-165, 183-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35167. 11 interactions.
MINTMINT-4496565.

Chemistry

BindingDBP50107.
ChEMBLCHEMBL6057.

Proteomic databases

MaxQBP50107.
PaxDbP50107.
PeptideAtlasP50107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYML004C; YML004C; YML004C.
GeneID855009.
KEGGsce:YML004C.

Organism-specific databases

CYGDYML004c.
SGDS000004463. GLO1.

Phylogenomic databases

eggNOGCOG0346.
GeneTreeENSGT00390000009312.
HOGENOMHOG000215632.
KOK01759.
OMATEGRMKN.
OrthoDBEOG7HXD33.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-624.
YEAST:YML004C-MONOMER.
SABIO-RKP50107.
UniPathwayUPA00619; UER00675.

Gene expression databases

GenevestigatorP50107.

Family and domain databases

Gene3D3.10.180.10. 2 hits.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR025870. Glyoxalase-like_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
PF12681. Glyoxalase_2. 1 hit.
[Graphical view]
SUPFAMSSF54593. SSF54593. 2 hits.
TIGRFAMsTIGR00068. glyox_I. 2 hits.
PROSITEPS00934. GLYOXALASE_I_1. 2 hits.
PS00935. GLYOXALASE_I_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio978174.
PROP50107.

Entry information

Entry nameLGUL_YEAST
AccessionPrimary (citable) accession number: P50107
Secondary accession number(s): D6VZH1, Q9HFG0, Q9URB5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways