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Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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. Required for normal osteoclastogenesis.1 Publication

Miscellaneous

Expressed at higher levels in CD-1 mice which have been bred for low-anxiety-related behavior than in those which have been bred for high-anxiety-related behavior.

Catalytic activityi

(R)-S-lactoylglutathione = glutathione + methylglyoxal.1 Publication

Cofactori

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

Enzyme regulationi

Subject to competitive inhibition by methyl-gerfelin.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), 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 partnerCombined sources1
Binding sitei34Substrate; shared with dimeric partnerCombined sources1
Binding sitei38Substrate; shared with dimeric partnerCombined sources1
Metal bindingi100Zinc; shared with dimeric partnerCombined sources1
Binding sitei104Substrate; shared with dimeric partnerCombined sources1
Binding sitei123SubstrateCombined sources1
Metal bindingi127Zinc; via tele nitrogenCombined sources1
Binding sitei127SubstrateCombined sources1
Active sitei173Proton donor/acceptorBy similarity1
Metal bindingi173Zinc1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.4.1.5 3474
ReactomeiR-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95742 Glo1

Subcellular locationi

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2175

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001680782 – 184Lactoylglutathione lyaseAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Disulfide bondi19 ↔ 20By similarity
Modified residuei88N6-succinyllysineCombined sources1
Modified residuei107PhosphothreonineBy similarity1
Modified residuei139S-glutathionyl cysteineBy similarity1
Modified residuei148N6-acetyllysine; alternateBy similarity1
Modified residuei148N6-succinyllysine; alternateCombined sources1

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

EPDiQ9CPU0
MaxQBiQ9CPU0
PaxDbiQ9CPU0
PRIDEiQ9CPU0

2D gel databases

REPRODUCTION-2DPAGEiIPI00321734
Q9CPU0
UCD-2DPAGEiQ9CPU0

PTM databases

iPTMnetiQ9CPU0
PhosphoSitePlusiQ9CPU0
SwissPalmiQ9CPU0

Expressioni

Gene expression databases

BgeeiENSMUSG00000024026
CleanExiMM_GLO1
ExpressionAtlasiQ9CPU0 baseline and differential
GenevisibleiQ9CPU0 MM

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi225051, 1 interactor
IntActiQ9CPU0, 5 interactors
MINTiQ9CPU0
STRINGi10090.ENSMUSP00000024823

Structurei

Secondary structure

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Helixi13 – 18Combined sources6
Helixi25 – 27Combined sources3
Beta strandi31 – 38Combined sources8
Helixi42 – 51Combined sources10
Beta strandi56 – 63Combined sources8
Helixi64 – 66Combined sources3
Beta strandi68 – 75Combined sources8
Helixi78 – 80Combined sources3
Helixi85 – 92Combined sources8
Beta strandi95 – 104Combined sources10
Helixi107 – 109Combined sources3
Beta strandi118 – 122Combined sources5
Beta strandi125 – 131Combined sources7
Helixi135 – 144Combined sources10
Beta strandi149 – 151Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi162 – 165Combined sources4
Beta strandi171 – 175Combined sources5
Turni177 – 179Combined sources3
Helixi180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZA0X-ray1.70A/B1-184[»]
4KYHX-ray2.50A/B1-184[»]
4KYKX-ray2.00A/B1-184[»]
4OPNX-ray2.10A/B1-184[»]
4PV5X-ray2.30A/B2-184[»]
4X2AX-ray2.00A/B1-184[»]
ProteinModelPortaliQ9CPU0
SMRiQ9CPU0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CPU0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 177VOCPROSITE-ProRule annotationAdd BLAST147

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 158Substrate bindingCombined sources2

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

eggNOGiENOG410IU7X Eukaryota
ENOG4111FDV LUCA
GeneTreeiENSGT00390000009312
HOGENOMiHOG000232011
HOVERGENiHBG025852
InParanoidiQ9CPU0
KOiK01759
OMAiNWGTESY
OrthoDBiEOG091G0GMY
PhylomeDBiQ9CPU0
TreeFamiTF105011

Family and domain databases

Gene3Di3.10.180.10, 1 hit
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, 1 hit
SUPFAMiSSF54593 SSF54593, 1 hit
TIGRFAMsiTIGR00068 glyox_I, 1 hit
PROSITEiView protein in PROSITE
PS00934 GLYOXALASE_I_1, 1 hit
PS00935 GLYOXALASE_I_2, 1 hit
PS51819 VOC, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9CPU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT
60 70 80 90 100
RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE
110 120 130 140 150
LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV
160 170 180
KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATII
Length:184
Mass (Da):20,810
Last modified:January 23, 2007 - v3
Checksum:iF6B5667A65454D18
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti92T → M in AAH24663 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002386 mRNA Translation: BAB22060.1
AK003567 mRNA Translation: BAB22863.1
AK005055 mRNA Translation: BAB23781.1
AK031832 mRNA Translation: BAC27570.1
AK049703 mRNA Translation: BAC33882.1
BC024663 mRNA Translation: AAH24663.1
BC081432 mRNA Translation: AAH81432.1
CCDSiCCDS28600.1
RefSeqiNP_001107032.1, NM_001113560.1
NP_079650.3, NM_025374.3
UniGeneiMm.261984

Genome annotation databases

EnsembliENSMUST00000024823; ENSMUSP00000024823; ENSMUSG00000024026
ENSMUST00000167624; ENSMUSP00000126586; ENSMUSG00000024026
GeneIDi109801
KEGGimmu:109801
UCSCiuc012aos.1 mouse

Similar proteinsi

Entry informationi

Entry nameiLGUL_MOUSE
AccessioniPrimary (citable) accession number: Q9CPU0
Secondary accession number(s): Q543L3, Q8R3T1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 150 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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