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Protein

Lactoylglutathione lyase

Gene

GLO1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (By similarity).By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.By similarity

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 (EGM_13562), Lactoylglutathione lyase (GLO1)
  2. Hydroxyacylglutathione hydrolase, mitochondrial (HAGH)
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 bindingi34Zinc; shared with dimeric partnerBy similarity1
Binding sitei34Substrate; shared with dimeric partnerBy similarity1
Binding sitei38Substrate; shared with dimeric partnerBy similarity1
Metal bindingi100Zinc; shared with dimeric partnerBy similarity1
Binding sitei104Substrate; shared with dimeric partnerBy similarity1
Binding sitei123SubstrateBy similarity1
Metal bindingi127Zinc; via tele nitrogenBy similarity1
Binding sitei127SubstrateBy similarity1
Active sitei173Proton donor/acceptorBy similarity1
Metal bindingi173ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, 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:QnpA-15219
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001680772 – 184Lactoylglutathione lyaseAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Disulfide bondi19 ↔ 20By similarity
Disulfide bondi61 ↔ 139AlternateBy similarity
Modified residuei88N6-succinyllysineBy similarity1
Modified residuei107PhosphothreonineBy similarity1
Modified residuei139S-glutathionyl cysteine; alternateBy similarity1
Modified residuei148N6-acetyllysine; alternateBy similarity1
Modified residuei148N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Glutathionylation at Cys-139 inhibits enzyme activity.By similarity
Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity).By similarity
Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B (By similarity).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

Proteomic databases

PRIDEiQ4R5F2.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ4R5F2.
SMRiQ4R5F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 158Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

HOVERGENiHBG025852.
KOiK01759.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR00068. glyox_I. 1 hit.
PROSITEiPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4R5F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT
60 70 80 90 100
RVLGMTLIQK CDFPAMKFSL YFLAYEDKND IPKDKEEKIA WALSRKATLE
110 120 130 140 150
LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVHSACK RFEELGVKFV
160 170 180
KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM
Length:184
Mass (Da):20,710
Last modified:January 23, 2007 - v3
Checksum:i8E8B276CB80EAB34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169591 mRNA. Translation: BAE01673.1.
RefSeqiNP_001271981.1. NM_001285052.1.
UniGeneiMfa.8289.

Genome annotation databases

GeneIDi101926610.
KEGGimcf:101926610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169591 mRNA. Translation: BAE01673.1.
RefSeqiNP_001271981.1. NM_001285052.1.
UniGeneiMfa.8289.

3D structure databases

ProteinModelPortaliQ4R5F2.
SMRiQ4R5F2.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ4R5F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101926610.
KEGGimcf:101926610.

Organism-specific databases

CTDi2739.

Phylogenomic databases

HOVERGENiHBG025852.
KOiK01759.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.

Family and domain databases

Gene3Di3.10.180.10. 1 hit.
InterProiIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamiPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMiSSF54593. SSF54593. 1 hit.
TIGRFAMsiTIGR00068. glyox_I. 1 hit.
PROSITEiPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLGUL_MACFA
AccessioniPrimary (citable) accession number: Q4R5F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.