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Q4R5F2 (LGUL_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:QnpA-15219
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. In the homodimer, two zinc ions are bound between subunits 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_0000168077

Regions

Region157 – 1582Substrate binding By similarity

Sites

Active site1731Proton donor/acceptor By similarity
Metal binding341Zinc; shared with dimeric partner By similarity
Metal binding1001Zinc; shared with dimeric partner By similarity
Metal binding1271Zinc; via tele nitrogen By similarity
Metal binding1731Zinc By similarity
Binding site341Substrate; shared with dimeric partner By similarity
Binding site381Substrate; shared with dimeric partner By similarity
Binding site1041Substrate; shared with dimeric partner By similarity
Binding site1231Substrate By similarity
Binding site1271Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue881N6-succinyllysine By similarity
Modified residue1071Phosphothreonine By similarity
Modified residue1391S-glutathionyl cysteine; alternate By similarity
Modified residue1481N6-acetyllysine; alternate By similarity
Modified residue1481N6-succinyllysine; alternate By similarity
Disulfide bond19 ↔ 20 By similarity
Disulfide bond61 ↔ 139Alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4R5F2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8E8B276CB80EAB34

FASTA18420,710
        10         20         30         40         50         60 
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK 

        70         80         90        100        110        120 
CDFPAMKFSL YFLAYEDKND IPKDKEEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS 

       130        140        150        160        170        180 
DPRGFGHIGI AVPDVHSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM 


ATLM 

« Hide

References

[1]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Parietal cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB169591 mRNA. Translation: BAE01673.1.
RefSeqNP_001271981.1. NM_001285052.1.
UniGeneMfa.8289.

3D structure databases

ProteinModelPortalQ4R5F2.
SMRQ4R5F2. Positions 2-184.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ4R5F2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101926610.
KEGGmcf:101926610.

Organism-specific databases

CTD2739.

Phylogenomic databases

HOVERGENHBG025852.
KOK01759.

Enzyme and pathway databases

UniPathwayUPA00619; UER00675.

Family and domain databases

Gene3D3.10.180.10. 1 hit.
InterProIPR029068. Glyas_Bleomycin-R_OHBP_Dase.
IPR004360. Glyas_Fos-R_dOase_dom.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
PfamPF00903. Glyoxalase. 1 hit.
[Graphical view]
SUPFAMSSF54593. SSF54593. 1 hit.
TIGRFAMsTIGR00068. glyox_I. 1 hit.
PROSITEPS00934. GLYOXALASE_I_1. 1 hit.
PS00935. GLYOXALASE_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLGUL_MACFA
AccessionPrimary (citable) accession number: Q4R5F2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 53 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways