Q09751 (LGUL_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Domain	Repeat
Ligand	Cobalt Manganese Metal-binding Nickel Zinc
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular 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 component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	lactoylglutathione 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Lactoylglutathione lyase		PRO_0000168086
Sites
	Metal binding	223	1	Zinc Potential
	Metal binding	226	1	Zinc Potential
	Metal binding	239	1	Zinc Potential
	Metal binding	251	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q09751 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D5F916F51BA2A0F5	FASTA	302	34,410
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	T11675.
RefSeq	NP_596010.1. NM_001021918.1.
3D structure databases
ProteinModelPortal	Q09751.
ModBase	Search...
Protein-protein interaction databases
STRING	Q09751.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
GeneID	2539736.
GenomeReviews	Gene locus glo1 in contig CU329671_GR.
KEGG	spo:SPBC12C2.12c.
NMPDR	fig|4896.1.peg.1876.
Organism-specific databases
GeneDB_Spombe	SPBC12C2.12c.
Phylogenomic databases
eggNOG	fuNOG05381.
GeneTree	EFGT00050000004759.
HOGENOM	HBG325985.
OMA	NHTMVRV.
OrthoDB	EOG4GXJWH.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003750-MONOMER.
Gene expression databases
ArrayExpress	Q09751.
Family and domain databases
InterPro	IPR004360. Glyas_Fos-R_dOase. IPR004361. Glyoxalase_1. IPR018146. Glyoxalase_1_CS. [Graphical view]
KO	K01759.
Pfam	PF00903. Glyoxalase. 2 hits. [Graphical view]
TIGRFAMs	TIGR00068. Glyox_I. 2 hits.
PROSITE	PS00934. GLYOXALASE_I_1. 2 hits. PS00935. GLYOXALASE_I_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LGUL_SCHPO

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program