Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Rattus norvegicus (Rat)
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 (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 (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

  • lactoylglutathione lyase activity Source: RGD
  • zinc ion binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-70268 Pyruvate metabolism
SABIO-RKiQ6P7Q4
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2702 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

ChEMBLiCHEMBL2306

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001680792 – 184Lactoylglutathione lyaseAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Disulfide bondi19 ↔ 20By similarity
Modified residuei107PhosphothreonineBy similarity1
Modified residuei139S-glutathionyl cysteineBy 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

PaxDbiQ6P7Q4
PRIDEiQ6P7Q4

PTM databases

iPTMnetiQ6P7Q4
PhosphoSitePlusiQ6P7Q4
SwissPalmiQ6P7Q4

Expressioni

Gene expression databases

BgeeiENSRNOG00000000541
GenevisibleiQ6P7Q4 RN

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000650

Structurei

3D structure databases

ProteinModelPortaliQ6P7Q4
SMRiQ6P7Q4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

eggNOGiENOG410IU7X Eukaryota
ENOG4111FDV LUCA
GeneTreeiENSGT00390000009312
HOGENOMiHOG000232011
HOVERGENiHBG025852
InParanoidiQ6P7Q4
KOiK01759
OMAiNWGTESY
OrthoDBiEOG091G0GMY
PhylomeDBiQ6P7Q4
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.

Q6P7Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPQPASSG LTDEAALSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT
60 70 80 90 100
RVLGLTLLQK LDFPSMKFSL YFLAYEDKND IPKDKTERTA WAFSRKATLE
110 120 130 140 150
LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYEACK RFEELGVKFV
160 170 180
KKPDDGKMKG LAFVQDPDGY WIEILNPNKM ATII
Length:184
Mass (Da):20,820
Last modified:January 23, 2007 - v3
Checksum:i1834FA5E9871A1C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061570 mRNA Translation: AAH61570.1
RefSeqiNP_997477.1, NM_207594.2
UniGeneiRn.108014

Genome annotation databases

EnsembliENSRNOT00000000650; ENSRNOP00000000650; ENSRNOG00000000541
GeneIDi294320
KEGGirno:294320
UCSCiRGD:2702 rat

Similar proteinsi

Entry informationi

Entry nameiLGUL_RAT
AccessioniPrimary (citable) accession number: Q6P7Q4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 115 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health