EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR012133 Alpha-hydroxy acid dehydrogenase, FMN-dependent

Protein matches Help

UniProtKB

Matches:

1756 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

IPR012133 a-Hydoxy_acid_DH_FMN

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000138	Al-hdrx_acd_dh	1381
PROSITE profile	PS51349	FMN_HYDROXY_ACID_DH_2	1756
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000262 FMN-dependent dehydrogenase

Children

IPR014080 L-lactate oxidase
IPR020920 L-lactate dehydrogenase [cytochrome]

Contains

IPR008259 FMN-dependent alpha-hydroxy acid dehydrogenase, active site

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This group represents an alpha-hydroxy acid dehydrogenase, which is FMN-dependent. Human glycolate oxidase (GO) catalyses the FMN-dependent oxidation of glycolate to glyoxylate and glyoxylate to oxalate. The latter is a key metabolite in kidney stone formation. 4-carboxy-5-dodecylsulphanyl-1,2,3-triazole (CDST) is an inhibiter of this enzyme. In contrast to most alpha-hydroxy acid oxidases, including spinach glycolate oxidase, a loop region, known as loop 4, is completely visible when the GO active site contains a small ligand. Since this is an unique structural feature, it has the potential to be a target for drugs to decrease glycolate and glyoxylate levels in primary hyperoxaluria type 1 patients who have the inability to convert peroxisomal glyoxylate to glycine [1]. In addition, L-Lactate oxidase (LOX) belongs to a family of flavin mononucleotide (FMN)-dependent alpha-hydroxy acid-oxidizing enzymes [2].

Structural links Help

PDB - click here

SCOP: c.1.4.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:1.1.2.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012133

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00175 Cytochrome b2, mitochondrial

P20932 (S)-mandelate dehydrogenase

Q9LRR9 Probable peroxisomal (S)-2-hydroxy-acid oxidase 2

Q9NYQ2 Hydroxyacid oxidase 2

Q9UJM8 Hydroxyacid oxidase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR000262	FMN-dependent dehydrogenase
IPR001199	Cytochrome b5
IPR018506	Cytochrome b5, heme-binding site
IPR012133	Alpha-hydroxy acid dehydrogenase, FMN-dependent
IPR008259	FMN-dependent alpha-hydroxy acid dehydrogenase, active site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Murray MS, Holmes RP, Lowther WT. Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design. Biochemistry 47 2439-49 2008 [PubMed: 18215067] http://dx.doi.org/10.1021/bi701710r
2.	Furuichi M, Suzuki N, Dhakshnamoorhty B, Minagawa H, Yamagishi R, Watanabe Y, Goto Y, Kaneko H, Yoshida Y, Yagi H, Waga I, Kumar PK, Mizuno H. X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism. J. Mol. Biol. 378 436-46 2008 [PubMed: 18367206] http://dx.doi.org/10.1016/j.jmb.2008.02.062

Additional Reading Open in usermanual
	Sukumar N, Dewanti AR, Mitra B, Mathews FS. High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase. J. Biol. Chem. 279 2004 3749-57 [PubMed: 14604988] http://dx.doi.org/10.1074/jbc.M310049200
	Cunane LM, Barton JD, Chen ZW, Le KH, Amar D, Lederer F, Mathews FS. Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase. Biochemistry 44 2005 1521-31 [PubMed: 15683236] http://dx.doi.org/10.1021/bi048616e
	Sukumar N, Xu Y, Gatti DL, Mitra B, Mathews FS. Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase. Biochemistry 40 2001 9870-8 [PubMed: 11502180] http://dx.doi.org/10.1021/bi010938k
	Sukumar N, Dewanti A, Merli A, Rossi GL, Mitra B, Mathews FS. Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr. D Biol. Crystallogr. 65 2009 543-52 [PubMed: 19465768] http://dx.doi.org/10.1107/S0907444909010270

InterPro 23.1