Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q09751 (LGUL_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:SPBC12C2.12c, SPBC21D10.03c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length302 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.2

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions can also function as cofactors. Ref.2

Pathway

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

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the glyoxalase I family.

Ontologies

Keywords
   DomainRepeat
   LigandCobalt
Manganese
Metal-binding
Nickel
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular response to osmotic stress

Traceable author statement. Source: GeneDB_Spombe

glutathione metabolic process

Inferred from direct assay. Source: GeneDB_Spombe

methylglyoxal catabolic process to D-lactate

Inferred from mutant phenotype. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionlactoylglutathione lyase activity

Inferred from direct assay. Source: GeneDB_Spombe

zinc ion binding

Inferred from direct assay. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Lactoylglutathione lyase
PRO_0000168086

Sites

Metal binding2231Zinc Potential
Metal binding2261Zinc Potential
Metal binding2391Zinc Potential
Metal binding2511Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q09751 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D5F916F51BA2A0F5

FASTA30234,410
        10         20         30         40         50         60 
MASTTDMSTY KLNHTMIRVK DLDKSLKFYT EVFGMKLIDQ WVFEENEFSL SFLAFDGPGA 

        70         80         90        100        110        120 
LNHGVERSKR EGILELTYNF GTEKKEGPVY INGNTEPKRG FGHICFTVDN IESACAYLES 

       130        140        150        160        170        180 
KGVSFKKKLS DGKMKHIAFA LDPDNYWIEL VSQSETKPKA NISNFRFNHT MVRVKDPEPS 

       190        200        210        220        230        240 
IAFYEKLGMK VIDKADHPNG KFTNYFLAYP SDLPRHDREG LLELTHNWGT EKESGPVYHN 

       250        260        270        280        290        300 
GNDGDEKGYG HVCISVDNIN AACSKFEAEG LPFKKKLTDG RMKDIAFLLD PDNYWVEVIE 


QK 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe."
Takatsume Y., Izawa S., Inoue Y.
Arch. Microbiol. 181:371-377(2004) [PubMed: 15042280] [Abstract]
Cited for: FUNCTION, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA20759.1.
PIRT11675.
RefSeqNP_596010.1. NM_001021918.1.

3D structure databases

ProteinModelPortalQ09751.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ09751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
GeneID2539736.
GenomeReviewsGene locus glo1 in contig CU329671_GR.
KEGGspo:SPBC12C2.12c.
NMPDRfig|4896.1.peg.1876.

Organism-specific databases

GeneDB_SpombeSPBC12C2.12c.

Phylogenomic databases

eggNOGfuNOG05381.
GeneTreeEFGT00050000004759.
HOGENOMHBG325985.
OMANHTMVRV.
OrthoDBEOG4GXJWH.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-003750-MONOMER.

Gene expression databases

ArrayExpressQ09751.

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
KOK01759.
PfamPF00903. Glyoxalase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00068. Glyox_I. 2 hits.
PROSITEPS00934. GLYOXALASE_I_1. 2 hits.
PS00935. GLYOXALASE_I_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_SCHPO
AccessionPrimary (citable) accession number: Q09751
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 14, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families