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Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Mus musculus (Mouse)
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. 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

  • carbohydrate metabolic process Source: Ensembl
  • glutathione metabolic process Source: Ensembl
  • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: MGI
  • negative regulation of apoptotic process Source: UniProtKB
  • osteoclast differentiation Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: MGI

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.
MINTiMINT-2513171.
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.
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: August 30, 2017
This is version 146 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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families