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Q9KT93 (LGUL_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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:
Probable 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:VC_1010
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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.

Sequence caution

The sequence AAF94171.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 138138Probable lactoylglutathione lyase
PRO_0000168097

Sites

Active site1251Proton donor/acceptor By similarity
Metal binding81Nickel; via tele nitrogen By similarity
Metal binding591Nickel By similarity
Metal binding771Nickel; via tele nitrogen By similarity
Metal binding1251Nickel By similarity
Binding site121Substrate By similarity
Binding site631Substrate By similarity
Binding site771Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KT93 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 21427CF9AA2E51BD

FASTA13815,176
        10         20         30         40         50         60 
MSNHRILHTM LRVGDLDKSI EFYTQVMGMS LLRKNENTEY KYTLAFLGYG DESQGAVIEL 

        70         80         90        100        110        120 
TYNWGVADYE KGNAYGHIAI GVDDIYATCD TIKAAGGIVT REPGPVKGGT THIAFVKDPD 

       130 
GYMIELIQNK QAHAGLEG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94171.1. Different initiation.
PIRH82251.
RefSeqNP_230656.2. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KT93.
SMRQ9KT93. Positions 5-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC1010.

Protocols and materials databases

DNASU2614263.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94171; AAF94171; VC_1010.
GeneID2614263.
KEGGvch:VC1010.
PATRIC20081120. VBIVibCho83274_0964.

Phylogenomic databases

eggNOGCOG0346.
KOK01759.
OMAIGEEDIY.
OrthoDBEOG6DVJXX.

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_VIBCH
AccessionPrimary (citable) accession number: Q9KT93
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: March 20, 2007
Last modified: June 11, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways