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Protein

Lactoylglutathione lyase

Gene

Glo1

Organism
Rattus norvegicus (Rat)
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 (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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Zinc; shared with dimeric partnerBy similarity
Binding sitei34 – 341Substrate; shared with dimeric partnerBy similarity
Binding sitei38 – 381Substrate; shared with dimeric partnerBy similarity
Metal bindingi100 – 1001Zinc; shared with dimeric partnerBy similarity
Binding sitei104 – 1041Substrate; shared with dimeric partnerBy similarity
Binding sitei123 – 1231SubstrateBy similarity
Metal bindingi127 – 1271Zinc; via tele nitrogenBy similarity
Binding sitei127 – 1271SubstrateBy similarity
Active sitei173 – 1731Proton donor/acceptorBy similarity
Metal bindingi173 – 1731ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-70268. Pyruvate metabolism.
SABIO-RKQ6P7Q4.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2702. Glo1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2306.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 184183Lactoylglutathione lyasePRO_0000168079Add
BLAST

Amino acid modifications

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

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.

Expressioni

Gene expression databases

GenevisibleiQ6P7Q4. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000650.

Structurei

3D structure databases

ProteinModelPortaliQ6P7Q4.
SMRiQ6P7Q4. Positions 4-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

eggNOGiENOG410IU7X. Eukaryota.
ENOG4111FDV. LUCA.
GeneTreeiENSGT00390000009312.
HOGENOMiHOG000232011.
HOVERGENiHBG025852.
InParanoidiQ6P7Q4.
KOiK01759.
OMAiDPDQSYH.
OrthoDBiEOG7XPZ6W.
PhylomeDBiQ6P7Q4.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ6P7Q4.
SMRiQ6P7Q4. Positions 4-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000650.

Chemistry

ChEMBLiCHEMBL2306.

PTM databases

iPTMnetiQ6P7Q4.

Proteomic databases

PaxDbiQ6P7Q4.
PRIDEiQ6P7Q4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2739.
RGDi2702. Glo1.

Phylogenomic databases

eggNOGiENOG410IU7X. Eukaryota.
ENOG4111FDV. LUCA.
GeneTreeiENSGT00390000009312.
HOGENOMiHOG000232011.
HOVERGENiHBG025852.
InParanoidiQ6P7Q4.
KOiK01759.
OMAiDPDQSYH.
OrthoDBiEOG7XPZ6W.
PhylomeDBiQ6P7Q4.
TreeFamiTF105011.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.
ReactomeiR-RNO-70268. Pyruvate metabolism.
SABIO-RKQ6P7Q4.

Miscellaneous databases

PROiQ6P7Q4.

Gene expression databases

GenevisibleiQ6P7Q4. RN.

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 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].
    Tissue: Pituitary.
  2. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-38; 44-83; 89-95 AND 124-148, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiLGUL_RAT
AccessioniPrimary (citable) accession number: Q6P7Q4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 103 of the entry and version 3 of the sequence. [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

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 one 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.