Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0A0T2 (LGUL_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:gloA
Ordered Locus Names:NMA2147
OrganismNeisseria meningitidis serogroup A [Complete proteome] [HAMAP]
Taxonomic identifier65699 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione By similarity.

Catalytic activity

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

Cofactor

Binds 1 nickel ion per subunit By similarity.

Pathway

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

Sequence similarities

Belongs to the glyoxalase I family.

Ontologies

Keywords
   LigandMetal-binding
Nickel
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionlactoylglutathione lyase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 138138Lactoylglutathione lyase
PRO_0000168094

Sites

Metal binding51Nickel By similarity
Metal binding561Nickel By similarity
Metal binding741Nickel By similarity
Metal binding1221Nickel By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A0T2 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 3C3EFEA4FACAAFD3

FASTA13815,669
        10         20         30         40         50         60 
MRLLHTMLRV GNLEKSLDFY QNVLGMKLLR RKDYPEGRFT LAFVGYGDET DSTVLELTHN 

        70         80         90        100        110        120 
WDTERYDLGN AYGHIAVEVD DAYEACERVK RQGGNVVREA GPMKHGTTVI AFVEDPDGYK 

       130 
IEFIQKKSGD DSVAYQTA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM09244.1.
PIRG81211.
RefSeqYP_002343396.1. NC_003116.1.

3D structure databases

ProteinModelPortalP0A0T2.
SMRP0A0T2. Positions 1-126.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000000165; EBNEIP00000000165; EBNEIG00000000165.
GeneID907300.
GenomeReviewsGene locus NMA2147 in contig AL157959_GR.
KEGGnma:NMA2147.
PATRIC20365810. VBINeiMen132687_2594.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000021776.
HOGENOMHBG704761.
OMAPGPMKHG.
ProtClustDBCLSK877504.

Enzyme and pathway databases

BioCycNMEN122587:NMA2147-MONOMER.

Family and domain databases

InterProIPR004360. Glyas_Fos-R_dOase.
IPR004361. Glyoxalase_1.
IPR018146. Glyoxalase_1_CS.
[Graphical view]
KOK01759.
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...

Entry information

Entry nameLGUL_NEIMA
AccessionPrimary (citable) accession number: P0A0T2
Secondary accession number(s): A1ITX5, O33393
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families