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Protein

Lactoylglutathione lyase

Gene

gloA

Organism
Escherichia coli (strain K12)
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.1 Publication

Catalytic activityi

(R)-S-lactoylglutathione = glutathione + methylglyoxal.1 Publication

Cofactori

Ni2+1 PublicationNote: Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits. Is not active with zinc ions.1 Publication

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 (gloA)
  2. Hydroxyacylglutathione hydrolase (gloB)
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)DescriptionActionsGraphical viewLength
Metal bindingi5Nickel; via tele nitrogen; shared with dimeric partner1
Binding sitei9Substrate; shared with dimeric partnerBy similarity1
Metal bindingi56Nickel; shared with dimeric partner1
Binding sitei60Substrate; shared with dimeric partnerBy similarity1
Metal bindingi74Nickel; via tele nitrogen1
Binding sitei74SubstrateBy similarity1
Active sitei122Proton donor/acceptorBy similarity1
Metal bindingi122Nickel1

GO - Molecular functioni

  • lactoylglutathione lyase activity Source: EcoCyc
  • nickel cation binding Source: EcoCyc

GO - Biological processi

  • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciEcoCyc:GLYOXI-MONOMER.
ECOL316407:JW1643-MONOMER.
MetaCyc:GLYOXI-MONOMER.
BRENDAi4.4.1.5. 2026.
SABIO-RKP0AC81.
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:gloA
Ordered Locus Names:b1651, JW1643
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13421. gloA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001680881 – 135Lactoylglutathione lyaseAdd BLAST135

Proteomic databases

PaxDbiP0AC81.
PRIDEiP0AC81.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaKP0A6Y82EBI-551143,EBI-542092

Protein-protein interaction databases

BioGridi4259387. 10 interactors.
DIPiDIP-47995N.
IntActiP0AC81. 6 interactors.
MINTiMINT-1255986.
STRINGi511145.b1651.

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi13 – 22Combined sources10
Beta strandi27 – 34Combined sources8
Turni35 – 38Combined sources4
Beta strandi39 – 47Combined sources9
Turni49 – 51Combined sources3
Beta strandi54 – 60Combined sources7
Beta strandi70 – 78Combined sources9
Helixi82 – 91Combined sources10
Beta strandi95 – 102Combined sources8
Beta strandi109 – 114Combined sources6
Beta strandi120 – 125Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F9ZX-ray1.50A/B1-135[»]
1FA5X-ray1.80A/B1-135[»]
1FA6X-ray1.90A/B1-135[»]
1FA7X-ray1.90A/B1-135[»]
1FA8X-ray1.70A/B1-135[»]
ProteinModelPortaliP0AC81.
SMRiP0AC81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AC81.

Family & Domainsi

Sequence similaritiesi

Belongs to the glyoxalase I family.Curated

Phylogenomic databases

eggNOGiENOG4108UYE. Bacteria.
COG0346. LUCA.
HOGENOMiHOG000232011.
InParanoidiP0AC81.
KOiK01759.
OMAiTHNWDTP.
PhylomeDBiP0AC81.

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.

P0AC81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLHTMLRV GDLQRSIDFY TKVLGMKLLR TSENPEYKYS LAFVGYGPET
60 70 80 90 100
EEAVIELTYN WGVDKYELGT AYGHIALSVD NAAEACEKIR QNGGNVTREA
110 120 130
GPVKGGTTVI AFVEDPDGYK IELIEEKDAG RGLGN
Length:135
Mass (Da):14,920
Last modified:November 8, 2005 - v1
Checksum:iA53FC5412B9A6CE3
GO

Mass spectrometryi

Molecular mass is 14919 Da from positions 1 - 135. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57363 Genomic DNA. Translation: AAC27133.1.
U00096 Genomic DNA. Translation: AAC74723.1.
AP009048 Genomic DNA. Translation: BAE76494.1.
D86931 Genomic DNA. Translation: BAA13187.1.
PIRiE64922.
RefSeqiNP_416168.1. NC_000913.3.
WP_001237796.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74723; AAC74723; b1651.
BAE76494; BAE76494; BAE76494.
GeneIDi946161.
KEGGiecj:JW1643.
eco:b1651.
PATRICi32118604. VBIEscCol129921_1722.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57363 Genomic DNA. Translation: AAC27133.1.
U00096 Genomic DNA. Translation: AAC74723.1.
AP009048 Genomic DNA. Translation: BAE76494.1.
D86931 Genomic DNA. Translation: BAA13187.1.
PIRiE64922.
RefSeqiNP_416168.1. NC_000913.3.
WP_001237796.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F9ZX-ray1.50A/B1-135[»]
1FA5X-ray1.80A/B1-135[»]
1FA6X-ray1.90A/B1-135[»]
1FA7X-ray1.90A/B1-135[»]
1FA8X-ray1.70A/B1-135[»]
ProteinModelPortaliP0AC81.
SMRiP0AC81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259387. 10 interactors.
DIPiDIP-47995N.
IntActiP0AC81. 6 interactors.
MINTiMINT-1255986.
STRINGi511145.b1651.

Proteomic databases

PaxDbiP0AC81.
PRIDEiP0AC81.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74723; AAC74723; b1651.
BAE76494; BAE76494; BAE76494.
GeneIDi946161.
KEGGiecj:JW1643.
eco:b1651.
PATRICi32118604. VBIEscCol129921_1722.

Organism-specific databases

EchoBASEiEB3197.
EcoGeneiEG13421. gloA.

Phylogenomic databases

eggNOGiENOG4108UYE. Bacteria.
COG0346. LUCA.
HOGENOMiHOG000232011.
InParanoidiP0AC81.
KOiK01759.
OMAiTHNWDTP.
PhylomeDBiP0AC81.

Enzyme and pathway databases

UniPathwayiUPA00619; UER00675.
BioCyciEcoCyc:GLYOXI-MONOMER.
ECOL316407:JW1643-MONOMER.
MetaCyc:GLYOXI-MONOMER.
BRENDAi4.4.1.5. 2026.
SABIO-RKP0AC81.

Miscellaneous databases

EvolutionaryTraceiP0AC81.
PROiP0AC81.

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...

Entry informationi

Entry nameiLGUL_ECOLI
AccessioniPrimary (citable) accession number: P0AC81
Secondary accession number(s): P77036, Q2MB62, Q59384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  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

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.