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InterPro: IPR004360 Glyoxalase/bleomycin resistance protein/dioxygenase

Protein matches Help

UniProtKB

Matches:

14662 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004360 Glyas_bleo-R_dOase

Secondary

IPR000325

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00903	Glyoxalase	14662
Signatures in BioMart

InterPro Relationships Help

Children

IPR004361 Glyoxalase I
IPR019883 Lactoylglutathione lyase

Found in

IPR000335 Bleomycin resistance protein
IPR005956 4-hydroxyphenylpyruvate dioxygenase
IPR017515 Methylmalonyl-CoA epimerase

Contains

IPR000486 Extradiol ring-cleavage dioxygenase, class I /II
IPR018146 Glyoxalase I, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

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 [1]. 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. This domain is found in other related proteins including the Bleomycin resistance protein and dioxygenases eg. 4-hydroxyphenylpyruvate dioxygenase.

Structural links Help

PDB - click here

SCOP: d.32.1.1 , d.32.1.10 , d.32.1.2 , d.32.1.3 , d.32.1.4 , d.32.1.6 , d.32.1.7 , d.32.1.8

CATH: 3.10.180.10

Database links Help

PANDIT: PF00903

Blocks: IPB004360

Pfam Clan: CL0104.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004360

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P32754 4-hydroxyphenylpyruvate dioxygenase

P50107 Lactoylglutathione lyase

P93836 4-hydroxyphenylpyruvate dioxygenase

Q09253 Glyoxalase 1

Q9CPU0 Lactoylglutathione lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004361	Glyoxalase I
IPR004360	Glyoxalase/bleomycin resistance protein/dioxygenase
IPR005956	4-hydroxyphenylpyruvate dioxygenase
IPR018146	Glyoxalase I, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Kim NS, Umezawa Y, Ohmura S, Kato S. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 268 11217-21 1993 [PubMed: 7684374] http://intl.jbc.org/cgi/reprint/268/15/11217.pdf

Additional Reading Open in usermanual
	Ariza A, Vickers TJ, Greig N, Armour KA, Dixon MJ, Eggleston IM, Fairlamb AH, Bond CS. Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme. Mol. Microbiol. 59 2006 1239-48 [PubMed: 16430697] http://dx.doi.org/10.1111/j.1365-2958.2006.05022.x
	Kovaleva EG, Lipscomb JD. Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 316 2007 453-7 [PubMed: 17446402] http://dx.doi.org/10.1126/science.1134697
	Han S, Eltis LD, Timmis KN, Muchmore SW, Bolin JT. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270 1995 976-80 [PubMed: 7481800] http://www.sciencemag.org/cgi/content/abstract/270/5238/976
	Ruetschi U, Dellsen A, Sahlin P, Stenman G, Rymo L, Lindstedt S. Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene. Eur. J. Biochem. 213 1993 1081-9 [PubMed: 8504803] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17857.x
	Emerson JP, Kovaleva EG, Farquhar ER, Lipscomb JD, Que L Jr. Swapping metals in Fe- and Mn-dependent dioxygenases: evidence for oxygen activation without a change in metal redox state. Proc. Natl. Acad. Sci. U.S.A. 105 2008 7347-52 [PubMed: 18492808] http://dx.doi.org/10.1073/pnas.0711179105
	Kovaleva EG, Lipscomb JD. Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry 47 2008 11168-70 [PubMed: 18826259] http://dx.doi.org/10.1021/bi801459q
	Fillgrove KL, Pakhomova S, Schaab MR, Newcomer ME, Armstrong RN. Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes. Biochemistry 46 2007 8110-20 [PubMed: 17567049] http://dx.doi.org/10.1021/bi700625p

InterPro 23.1