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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Nickel; via tele nitrogen; shared with dimeric partner
Binding sitei9 – 91Substrate; shared with dimeric partnerBy similarity
Metal bindingi56 – 561Nickel; shared with dimeric partner
Binding sitei60 – 601Substrate; shared with dimeric partnerBy similarity
Metal bindingi74 – 741Nickel; via tele nitrogen
Binding sitei74 – 741SubstrateBy similarity
Active sitei122 – 1221Proton donor/acceptorBy similarity
Metal bindingi122 – 1221Nickel

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 135135Lactoylglutathione lyasePRO_0000168088Add
BLAST

Proteomic databases

EPDiP0AC81.
PaxDbiP0AC81.
PRIDEiP0AC81.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi13 – 2210Combined sources
Beta strandi27 – 348Combined sources
Turni35 – 384Combined sources
Beta strandi39 – 479Combined sources
Turni49 – 513Combined sources
Beta strandi54 – 607Combined sources
Beta strandi70 – 789Combined sources
Helixi82 – 9110Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi109 – 1146Combined sources
Beta strandi120 – 1256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-126.
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.
OrthoDBiEOG6DVJXX.
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
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. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

EPDiP0AC81.
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.
OrthoDBiEOG6DVJXX.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences."
    Clugston S.L., Daub E., Kinach R., Miedema D., Barnard J.F.J., Honek J.F.
    Gene 186:103-111(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions."
    Clugston S.L., Barnard J.F.J., Kinach R., Miedema D., Ruman R., Daub E., Honek J.F.
    Biochemistry 37:8754-8763(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, CHARACTERIZATION, MASS SPECTROMETRY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Mizugaki M., Miura K., Yonezawa M., Hishinuma T., Tomioka Y.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation."
    He M.M., Clugston S.L., Honek J.F., Matthews B.W.
    Biochemistry 39:8719-8727(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH ZINC; NICKEL; COBALT AND CADMIUM, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.

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: March 16, 2016
This is version 89 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.