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Q6P7Q4 (LGUL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:Glo1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.

Subunit structure

Homodimer By similarity.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the glyoxalase I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 184183Lactoylglutathione lyase
PRO_0000168079

Sites

Metal binding341Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1271Zinc By similarity
Metal binding1731Zinc By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1071Phosphothreonine By similarity
Modified residue1391S-glutathionyl cysteine By similarity
Modified residue1481N6-acetyllysine By similarity
Disulfide bond19 ↔ 20 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P7Q4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1834FA5E9871A1C7

FASTA18420,820
        10         20         30         40         50         60 
MAEPQPASSG LTDEAALSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK 

        70         80         90        100        110        120 
LDFPSMKFSL YFLAYEDKND IPKDKTERTA WAFSRKATLE LTHNWGTEDD ETQSYHNGNS 

       130        140        150        160        170        180 
DPRGFGHIGI AVPDVYEACK RFEELGVKFV KKPDDGKMKG LAFVQDPDGY WIEILNPNKM 


ATII 

« Hide

References

« Hide 'large scale' references
[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, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC061570 mRNA. Translation: AAH61570.1.
IPIIPI00188304.
RefSeqNP_997477.1. NM_207594.2.
UniGeneRn.108014.

3D structure databases

ProteinModelPortalQ6P7Q4.
SMRQ6P7Q4. Positions 4-183.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000000650.

Proteomic databases

PaxDbQ6P7Q4.
PRIDEQ6P7Q4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000650; ENSRNOP00000000650; ENSRNOG00000000541.
GeneID294320.
KEGGrno:294320.
UCSCRGD:2702. rat.

Organism-specific databases

CTD2739.
RGD2702. Glo1.

Phylogenomic databases

eggNOGCOG0346.
GeneTreeENSGT00390000009312.
HOGENOMHOG000232011.
HOVERGENHBG025852.
InParanoidQ6P7Q4.
KOK01759.
OMAWALSRKA.
OrthoDBEOG4TQMB3.

Enzyme and pathway databases

SABIO-RKQ6P7Q4.
UniPathwayUPA00619; UER00675.

Gene expression databases

GenevestigatorQ6P7Q4.
GermOnlineENSRNOG00000000541. Rattus norvegicus.

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00068. glyox_I. 1 hit.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL2306.
NextBio637974.

Entry information

Entry nameLGUL_RAT
AccessionPrimary (citable) accession number: Q6P7Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families