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Q09751 (LGUL_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. 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) [Reference proteome]
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Lactoylglutathione lyase
PRO_0000168086

Sites

Active site1491Proton donor/acceptor By similarity
Metal binding141Zinc; via tele nitrogen; shared with dimeric partner By similarity
Metal binding751Zinc; shared with dimeric partner By similarity
Metal binding1031Zinc; via tele nitrogen By similarity
Metal binding1491Zinc By similarity
Binding site181Substrate By similarity
Binding site791Substrate By similarity
Binding site991Substrate By similarity
Binding site1031Substrate By similarity

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] [Europe PMC] [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] [Europe PMC] [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_001021918.2.

3D structure databases

ProteinModelPortalQ09751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276288. 16 interactions.
MINTMINT-4694686.
STRING4896.SPBC12C2.12c-1.

Proteomic databases

MaxQBQ09751.
PaxDbQ09751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
GeneID2539736.
KEGGspo:SPBC12C2.12c.

Organism-specific databases

PomBaseSPBC12C2.12c.

Phylogenomic databases

eggNOGCOG0346.
HOGENOMHOG000215632.
KOK01759.
OMASTYRMNH.
OrthoDBEOG7HXD33.
PhylomeDBQ09751.

Enzyme and pathway databases

UniPathwayUPA00619; UER00675.

Family and domain databases

Gene3D3.10.180.10. 2 hits.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 2 hits.
[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

NextBio20800887.
PROQ09751.

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: June 11, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways