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Protein

Lactoylglutathione lyase

Gene

glo1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+1 Publication, Cu2+1 Publication, Ni2+1 Publication, Mn2+1 PublicationNote: Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions can also function as cofactors.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Zinc; via tele nitrogen; shared with dimeric partnerBy similarity
Binding sitei18 – 181SubstrateBy similarity
Metal bindingi75 – 751Zinc; shared with dimeric partnerBy similarity
Binding sitei79 – 791SubstrateBy similarity
Binding sitei99 – 991SubstrateBy similarity
Metal bindingi103 – 1031Zinc; via tele nitrogenBy similarity
Binding sitei103 – 1031SubstrateBy similarity
Active sitei149 – 1491Proton donor/acceptorBy similarity
Metal bindingi149 – 1491ZincBy similarity

GO - Molecular functioni

  • lactoylglutathione lyase activity Source: PomBase
  • zinc ion binding Source: PomBase

GO - Biological processi

  • cellular response to osmotic stress Source: PomBase
  • glutathione metabolic process Source: PomBase
  • methylglyoxal catabolic process to D-lactate Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Cobalt, Manganese, Metal-binding, Nickel, Zinc

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.

Names & Taxonomyi

Protein namesi
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 namesi
Name:glo1
ORF Names:SPBC12C2.12c, SPBC21D10.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.12c.
PomBaseiSPBC12C2.12c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Lactoylglutathione lyasePRO_0000168086Add
BLAST

Proteomic databases

MaxQBiQ09751.
PaxDbiQ09751.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi276288. 19 interactions.
MINTiMINT-4694686.
STRINGi4896.SPBC12C2.12c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000215632.
InParanoidiQ09751.
KOiK01759.
OMAiACDRFES.
OrthoDBiEOG7HXD33.
PhylomeDBiQ09751.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamiPF00903. Glyoxalase. 2 hits.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
TIGRFAMsiTIGR00068. glyox_I. 2 hits.
PROSITEiPS00934. GLYOXALASE_I_1. 2 hits.
PS00935. GLYOXALASE_I_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTTDMSTY KLNHTMIRVK DLDKSLKFYT EVFGMKLIDQ WVFEENEFSL
60 70 80 90 100
SFLAFDGPGA LNHGVERSKR EGILELTYNF GTEKKEGPVY INGNTEPKRG
110 120 130 140 150
FGHICFTVDN IESACAYLES KGVSFKKKLS DGKMKHIAFA LDPDNYWIEL
160 170 180 190 200
VSQSETKPKA NISNFRFNHT MVRVKDPEPS IAFYEKLGMK VIDKADHPNG
210 220 230 240 250
KFTNYFLAYP SDLPRHDREG LLELTHNWGT EKESGPVYHN GNDGDEKGYG
260 270 280 290 300
HVCISVDNIN AACSKFEAEG LPFKKKLTDG RMKDIAFLLD PDNYWVEVIE

QK
Length:302
Mass (Da):34,410
Last modified:November 1, 1995 - v1
Checksum:iD5F916F51BA2A0F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20759.1.
PIRiT11675.
RefSeqiNP_596010.1. NM_001021918.2.

Genome annotation databases

EnsemblFungiiSPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
GeneIDi2539736.
KEGGispo:SPBC12C2.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20759.1.
PIRiT11675.
RefSeqiNP_596010.1. NM_001021918.2.

3D structure databases

ProteinModelPortaliQ09751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276288. 19 interactions.
MINTiMINT-4694686.
STRINGi4896.SPBC12C2.12c-1.

Proteomic databases

MaxQBiQ09751.
PaxDbiQ09751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC12C2.12c.1; SPBC12C2.12c.1:pep; SPBC12C2.12c.
GeneIDi2539736.
KEGGispo:SPBC12C2.12c.

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.12c.
PomBaseiSPBC12C2.12c.

Phylogenomic databases

eggNOGiCOG0346.
HOGENOMiHOG000215632.
InParanoidiQ09751.
KOiK01759.
OMAiACDRFES.
OrthoDBiEOG7HXD33.
PhylomeDBiQ09751.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.

Miscellaneous databases

NextBioi20800887.
PROiQ09751.

Family and domain databases

Gene3Di3.10.180.10. 2 hits.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamiPF00903. Glyoxalase. 2 hits.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 2 hits.
TIGRFAMsiTIGR00068. glyox_I. 2 hits.
PROSITEiPS00934. GLYOXALASE_I_1. 2 hits.
PS00935. GLYOXALASE_I_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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.

Entry informationi

Entry nameiLGUL_SCHPO
AccessioniPrimary (citable) accession number: Q09751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 29, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.