Reviewed, UniProtKB/Swiss-Prot P46235 (LGUL_VIBPA)

Names and origin

Protein names

Recommended name:
    Probable lactoylglutathione lyase
    EC=4.4.1.5
Alternative name(s):
    Methylglyoxalase
    Aldoketomutase
    Glyoxalase I
      Short name=Glx I
    Ketone-aldehyde mutase
    S-D-lactoylglutathione methylglyoxal lyase

Gene names

Name:	gloA
Ordered Locus Names:	VP2109

Organism

Vibrio parahaemolyticus [Complete proteome] [HAMAP]

Taxonomic identifier

670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	138 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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; D-lactate from methylglyoxal: step 1/2.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Ligand	Metal-binding Nickel
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	lactoylglutathione lyase activity Inferred from electronic annotation. Source: EC nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 138	138	Probable lactoylglutathione lyase		PRO_0000168098
Sites
	Metal binding	8	1	Nickel By similarity
	Metal binding	59	1	Nickel By similarity
	Metal binding	77	1	Nickel By similarity
	Metal binding	125	1	Nickel By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46235-1 [UniParc]. Last modified April 4, 2003. Version 2. Checksum: 5738D502E3CA35FC	FASTA	138	15,034
	10 20 30 40 50 60 MSNGRILHTM LRVGDLDKSI KFYTEVMGMQ LLRTNENKEY EYTLAFVGYG DESQGAVIEL 70 80 90 100 110 120 TYNWGKTEYD LGTAFGHIAI GVDDIYATCD AIKAAGGNVT REAGPVKGGT THIAFVKDPD 130 GYMIELIQNK QASAGLEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6.
[2]	"MotY, a component of the sodium-type flagellar motor." McCarter L.L. J. Bacteriol. 176:4219-4225(1994) [PubMed: 8021208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-138. Strain: BB22.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000031 Genomic DNA. Translation: BAC60372.1. U06949 Genomic DNA. Translation: AAA21576.1.
RefSeq	NP_798488.1.
3D structure databases
HSSP	HSSP built from PDB template 1F9Z based on UniProtKB Q59384.
SMR	P46235. Positions 5-128.
ModBase	Search...
Genome annotation databases
GeneID	1189621.
GenomeReviews	Gene locus VP2109 in contig BA000031_GR.
KEGG	vpa:VP2109.
NMPDR	fig|223926.1.peg.2109.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P46235.
OMA	P46235. PGPMKHG.
Enzyme and pathway databases
BioCyc	VPAR223926:VP2109-MON.
BRENDA	4.4.1.5. 3063.
Family and domain databases
InterPro	IPR004360. Glyas_bleo-R_dOase. IPR004361. Glyoxalase_1. IPR018146. Glyoxalase_1_CS. [Graphical view]
Pfam	PF00903. Glyoxalase. 1 hit. [Graphical view]
ProDom	PD002334. Gly_diox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00068. glyox_I. 1 hit.
PROSITE	PS00934. GLYOXALASE_I_1. 1 hit. PS00935. GLYOXALASE_I_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LGUL_VIBPA

Accession

Primary (citable) accession number: P46235

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 4, 2003
Last modified:	June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)