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

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Cobalt, Manganese, Metal-binding, Nickel, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-70268. Pyruvate metabolism.
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

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ09751.
PRIDEiQ09751.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi276288. 19 interactors.
MINTiMINT-4694686.

Structurei

3D structure databases

ProteinModelPortaliQ09751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000215632.
InParanoidiQ09751.
KOiK01759.
OMAiCNWKKRL.
OrthoDBiEOG092C5AJ6.
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 interactors.
MINTiMINT-4694686.

Proteomic databases

MaxQBiQ09751.
PRIDEiQ09751.

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. glo1.

Phylogenomic databases

HOGENOMiHOG000215632.
InParanoidiQ09751.
KOiK01759.
OMAiCNWKKRL.
OrthoDBiEOG092C5AJ6.
PhylomeDBiQ09751.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.
ReactomeiR-SPO-70268. Pyruvate metabolism.

Miscellaneous databases

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...

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: November 30, 2016
This is version 126 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

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 one 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.