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Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Mus musculus (Mouse)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotation

Pathway:imethylglyoxal degradation

This protein is involved in step 1 of the subpathway that synthesizes (R)-lactate from methylglyoxal.UniRule annotation
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Ligandi

Metal-bindingUniRule annotation, ZincUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactoylglutathione lyaseUniRule annotation (EC:4.4.1.5UniRule annotation)
Alternative name(s):
Glyoxalase IUniRule annotation
Gene namesi
Name:Glo1Imported
ORF Names:mCG_50439Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Organism-specific databases

MGIiMGI:95742. Glo1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024823.

Family & Domainsi

Sequence similaritiesi

Belongs to the glyoxalase I family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG025852.
KOiK01759.
OMAiWMKSIPG.

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.

A5GZX3-1 [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:June 12, 2007 - v1
Checksum:iF6B5667A65454D18
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ487161 mRNA. Translation: ABF48483.1.
DQ487162 mRNA. Translation: ABF48484.1.
CH466542 Genomic DNA. Translation: EDL08651.1.
RefSeqiNP_001107032.1. NM_001113560.1.
NP_079650.3. NM_025374.3.
UniGeneiMm.261984.

Genome annotation databases

GeneIDi109801.
KEGGimmu:109801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ487161 mRNA. Translation: ABF48483.1.
DQ487162 mRNA. Translation: ABF48484.1.
CH466542 Genomic DNA. Translation: EDL08651.1.
RefSeqiNP_001107032.1. NM_001113560.1.
NP_079650.3. NM_025374.3.
UniGeneiMm.261984.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi109801.
KEGGimmu:109801.

Organism-specific databases

CTDi2739.
MGIiMGI:95742. Glo1.

Phylogenomic databases

HOVERGENiHBG025852.
KOiK01759.
OMAiWMKSIPG.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.

Miscellaneous databases

ChiTaRSiGlo1. mouse.
NextBioi362781.
SOURCEiSearch...

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

  1. "A comparison of whole-genome shotgun-derived mouse chromosome 16 and the human genome."
    Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.
    , Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.
    Science 296:1661-1671(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MixedImported.
  3. "Verification of quantitative trait loci for increased carbohydrate and total energy intake in a congenic segment on mouse chromosome 17."
    Kumar G.K., Poole A.C., Volaufova J., York B., Zuberi A., Smith Richards B.K.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6JImported and CAST/EiImported.

Entry informationi

Entry nameiA5GZX3_MOUSE
AccessioniPrimary (citable) accession number: A5GZX3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: June 24, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.