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Protein

Lactoylglutathione lyase

Gene

glo1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -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: methylglyoxal degradation

This protein is involved in step 1 of the subpathway that synthesizes (R)-lactate from methylglyoxal.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lactoylglutathione lyase (glo1)
  2. Probable hydroxyacylglutathione hydrolase C824.07 (SPAC824.07), Probable hydroxyacylglutathione hydrolase C13B11.03c (SPCC13B11.03c)
This subpathway is part of the pathway methylglyoxal degradation, which is itself part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-lactate from methylglyoxal, the pathway methylglyoxal degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi14Zinc; via tele nitrogen; shared with dimeric partnerBy similarity1
Binding sitei18SubstrateBy similarity1
Metal bindingi75Zinc; shared with dimeric partnerBy similarity1
Binding sitei79SubstrateBy similarity1
Binding sitei99SubstrateBy similarity1
Metal bindingi103Zinc; via tele nitrogenBy similarity1
Binding sitei103SubstrateBy similarity1
Active sitei149Proton donor/acceptorBy similarity1
Metal bindingi149ZincBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • cellular detoxification Source: PomBase
  • cellular response to osmotic stress Source: PomBase
  • glutathione metabolic process Source: PomBase
  • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: PomBase

Keywordsi

Molecular functionLyase
LigandCobalt, Manganese, Metal-binding, Nickel, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-70268 Pyruvate metabolism
SABIO-RKiQ09751
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
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC12C2.12c
PomBaseiSPBC12C2.12c glo1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001680861 – 302Lactoylglutathione lyaseAdd BLAST302

Proteomic databases

MaxQBiQ09751
PaxDbiQ09751
PRIDEiQ09751

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi276288, 19 interactors
STRINGi4896.SPBC12C2.12c.1

Structurei

3D structure databases

ProteinModelPortaliQ09751
SMRiQ09751
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 153VOC 1PROSITE-ProRule annotationAdd BLAST143
Domaini166 – 301VOC 2PROSITE-ProRule annotationAdd BLAST136

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000215632
InParanoidiQ09751
KOiK01759
OMAiMGDAWGH
OrthoDBiEOG092C5AJ6
PhylomeDBiQ09751

Family and domain databases

Gene3Di3.10.180.10, 2 hits
InterProiView protein in InterPro
IPR029068 Glyas_Bleomycin-R_OHBP_Dase
IPR004360 Glyas_Fos-R_dOase_dom
IPR004361 Glyoxalase_1
IPR018146 Glyoxalase_1_CS
IPR037523 VOC
PfamiView protein in Pfam
PF00903 Glyoxalase, 2 hits
SUPFAMiSSF54593 SSF54593, 2 hits
TIGRFAMsiTIGR00068 glyox_I, 2 hits
PROSITEiView protein in PROSITE
PS00934 GLYOXALASE_I_1, 2 hits
PS00935 GLYOXALASE_I_2, 2 hits
PS51819 VOC, 2 hits

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

Entry informationi

Entry nameiLGUL_SCHPO
AccessioniPrimary (citable) accession number: Q09751
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health