Reviewed, UniProtKB/Swiss-Prot P16635 (LGUL_PSEPU)

Names and origin

Protein names

Recommended name:
    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

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
Catalytic activity	(R)-S-lactoylglutathione = glutathione + methylglyoxal.
Cofactor	Binds 1 zinc ion per subunit.
Pathway	Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glyoxalase I family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	lactoylglutathione lyase activity Inferred from electronic annotation. Source: EC zinc 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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 173	172	Lactoylglutathione lyase		PRO_0000168099
Sites
	Metal binding	93	1	Zinc Potential
	Metal binding	96	1	Zinc Potential
	Metal binding	109	1	Zinc Potential
	Metal binding	120	1	Zinc Potential
Experimental info
	Sequence conflict	11 – 54	44	GVTAQ…LVDKR → ALLPKRTLPLRNSFQPHHRA RQGHREVADSIPACLVSNWW TS in BAA00248. Ref.1
	Sequence conflict	110	1	H → D in BAA00248. Ref.1
	Sequence conflict	161 – 173	13	DGYWV…QPTPL → MVTGSK in BAA00248. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P16635-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DD3E559B4C261BB3	FASTA	173	19,540
	10 20 30 40 50 60 MSLNDLNTLP GVTAQADPAT AQFVFNHTML RVKDIEKSLD FYTRVLGFKL VDKRDFVEAK 70 80 90 100 110 120 FSLYFLALVD PATIPADDDA RHQWMKSIPG VLELTHNHGT ERDADFAYHH GNTDPRGFGH 130 140 150 160 170 ICVSVPDVVA ACERFEALQV PFQKRLSDGR MNHLAFIKDP DGYWVEVIQP TPL

References

[1]	"Nucleotide sequence of the glyoxalase I gene of Pseudomonas putida." Rhee H., Sato N., Murata K., Kimura A. Agric. Biol. Chem. 52:2243-2246(1988) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10. Strain: ATCC 8209 / IFO 3738 / NCIB 8296 / NRS 77.
[2]	"The gene encoding glyoxalase I from Pseudomonas putida: cloning, overexpression, and sequence comparisons with human glyoxalase I." Lu T., Creighton D.J., Antoine M., Fenselau C., Lovett P.S. Gene 150:93-96(1994) [PubMed: 7959071] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00342 Genomic DNA. Translation: BAA00248.1. L33880 Genomic DNA. Translation: AAA61758.1.
PIR	WZPSLP. JU0070.
3D structure databases
HSSP	HSSP built from PDB template 1QIP based on UniProtKB Q04760.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-12895.
BRENDA	4.4.1.5. 403.
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_PSEPU

Accession

Primary (citable) accession number: P16635
Secondary accession number(s): Q52084

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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