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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

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

Pathway:imethylglyoxal 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Zinc; shared with dimeric partner
Binding sitei34 – 341Substrate; shared with dimeric partner
Binding sitei38 – 381Substrate; shared with dimeric partner
Metal bindingi100 – 1001Zinc; shared with dimeric partner
Binding sitei104 – 1041Substrate; shared with dimeric partner
Binding sitei123 – 1231SubstrateBy similarity
Metal bindingi127 – 1271Zinc; via tele nitrogen
Binding sitei127 – 1271SubstrateBy similarity
Active sitei173 – 1731Proton donor/acceptorBy similarity
Metal bindingi173 – 1731Zinc

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.4.1.5. 3474.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:95742. Glo1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 184183Lactoylglutathione lyasePRO_0000168078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Disulfide bondi19 ↔ 20By similarity
Modified residuei88 – 881N6-succinyllysine1 Publication
Modified residuei107 – 1071PhosphothreonineBy similarity
Modified residuei139 – 1391S-glutathionyl cysteineBy similarity
Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
Modified residuei148 – 1481N6-succinyllysine; alternate1 Publication

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

MaxQBiQ9CPU0.
PaxDbiQ9CPU0.
PRIDEiQ9CPU0.

2D gel databases

REPRODUCTION-2DPAGEIPI00321734.
Q9CPU0.
UCD-2DPAGEQ9CPU0.

PTM databases

PhosphoSiteiQ9CPU0.

Expressioni

Gene expression databases

BgeeiQ9CPU0.
CleanExiMM_GLO1.
ExpressionAtlasiQ9CPU0. baseline and differential.
GenevisibleiQ9CPU0. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi225051. 1 interaction.
IntActiQ9CPU0. 5 interactions.
MINTiMINT-2513171.
STRINGi10090.ENSMUSP00000024823.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi13 – 186Combined sources
Helixi25 – 273Combined sources
Beta strandi31 – 388Combined sources
Helixi42 – 5110Combined sources
Beta strandi56 – 638Combined sources
Helixi64 – 663Combined sources
Beta strandi68 – 758Combined sources
Helixi78 – 803Combined sources
Helixi85 – 928Combined sources
Beta strandi95 – 10410Combined sources
Helixi107 – 1093Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi125 – 1317Combined sources
Helixi135 – 14410Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi171 – 1755Combined sources
Turni177 – 1793Combined sources
Helixi180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9CPU0.
SMRiQ9CPU0. Positions 4-183.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CPU0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1582Substrate binding

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

eggNOGiCOG0346.
GeneTreeiENSGT00390000009312.
HOGENOMiHOG000232011.
HOVERGENiHBG025852.
InParanoidiQ9CPU0.
KOiK01759.
OMAiWMKSIPG.
OrthoDBiEOG7XPZ6W.
PhylomeDBiQ9CPU0.
TreeFamiTF105011.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921T → M in AAH24663 (PubMed:15489334).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9CPU0.
SMRiQ9CPU0. Positions 4-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi225051. 1 interaction.
IntActiQ9CPU0. 5 interactions.
MINTiMINT-2513171.
STRINGi10090.ENSMUSP00000024823.

Chemistry

ChEMBLiCHEMBL2175.

PTM databases

PhosphoSiteiQ9CPU0.

2D gel databases

REPRODUCTION-2DPAGEIPI00321734.
Q9CPU0.
UCD-2DPAGEQ9CPU0.

Proteomic databases

MaxQBiQ9CPU0.
PaxDbiQ9CPU0.
PRIDEiQ9CPU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2739.
MGIiMGI:95742. Glo1.

Phylogenomic databases

eggNOGiCOG0346.
GeneTreeiENSGT00390000009312.
HOGENOMiHOG000232011.
HOVERGENiHBG025852.
InParanoidiQ9CPU0.
KOiK01759.
OMAiWMKSIPG.
OrthoDBiEOG7XPZ6W.
PhylomeDBiQ9CPU0.
TreeFamiTF105011.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.
BRENDAi4.4.1.5. 3474.

Miscellaneous databases

ChiTaRSiGlo1. mouse.
EvolutionaryTraceiQ9CPU0.
NextBioi362781.
PROiQ9CPU0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPU0.
CleanExiMM_GLO1.
ExpressionAtlasiQ9CPU0. baseline and differential.
GenevisibleiQ9CPU0. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Kidney, Liver, Medulla oblongata and Spinal cord.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and Czech II.
    Tissue: Brain and Mammary gland.
  3. "Identification of glyoxalase-I as a protein marker in a mouse model of extremes in trait anxiety."
    Kroemer S.A., Kessler M.S., Milfay D., Birg I.N., Bunck M., Czibere L., Panhuysen M., Puetz B., Deussing J.M., Holsboer F., Landgraf R., Turck C.W.
    J. Neurosci. 25:4375-4384(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, EXPRESSION IN CD-1 STRAIN.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-88 AND LYS-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The identification of an osteoclastogenesis inhibitor through the inhibition of glyoxalase I."
    Kawatani M., Okumura H., Honda K., Kanoh N., Muroi M., Dohmae N., Takami M., Kitagawa M., Futamura Y., Imoto M., Osada H.
    Proc. Natl. Acad. Sci. U.S.A. 105:11691-11696(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH METHYL-GERFELIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiLGUL_MOUSE
AccessioniPrimary (citable) accession number: Q9CPU0
Secondary accession number(s): Q543L3, Q8R3T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

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

External Data

Dasty 3

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 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.