The domain within your query sequence starts at position 180 and ends at position 335; the E-value for the Glyoxalase domain shown below is 2.1e-21.

IIDHIVGNQPDQEMQSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVTNYEESIKMP
INEPAPGRKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGTEFLAAPSSYYKLL
RENLKSAKIQVKESMDVLEELHILVDYDEKGYLLQI

Glyoxalase

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).

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