SMART: Pfam domain Glyoxalase

The domain within your query sequence starts at position 49 and ends at position 175; the E-value for the Glyoxalase domain shown below is 2.7e-14.

RLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDS
PITGFLQKNKAGGMHHVCIEVDNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIFLHPKDC
GGVLVEL

Glyoxalase

PFAM accession number:	PF00903
Interpro abstract (IPR004360):	Glyoxalase I ( EC 4.4.1.5 ) (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid [ (PUBMED:7684374) ]. Glyoxalase I is an ubiquitous enzyme which binds one mole of zinc per subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. The domain represented by this entry is found in glyoxalase I and in other related proteins, including fosfomycin resistance proteins FosB [ (PUBMED:11244082) ], FosA [ (PUBMED:15741169) ], FosX [ (PUBMED:17567049) ] and dioxygenases (eg. 4-hydroxyphenylpyruvate dioxygenase).

PFAM accession number:

PF00903

Interpro abstract (IPR004360):

Glyoxalase I ( EC 4.4.1.5 ) (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid [ (PUBMED:7684374) ]. Glyoxalase I is an ubiquitous enzyme which binds one mole of zinc per subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved.

The domain represented by this entry is found in glyoxalase I and in other related proteins, including fosfomycin resistance proteins FosB [ (PUBMED:11244082) ], FosA [ (PUBMED:15741169) ], FosX [ (PUBMED:17567049) ] and dioxygenases (eg. 4-hydroxyphenylpyruvate dioxygenase).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glyoxalase