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InterPro: IPR002937 Amine oxidase

Protein matches Help

UniProtKB

Matches:

4530 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

IPR002937 Amino_oxidase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01593	Amino_oxidase	4530
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001613 Flavin-containing amine oxidase
IPR004572 Protoporphyrinogen oxidase
IPR012142 Tryptophan 2-monooxygenase
IPR014102 Phytoene desaturase
IPR014103 Carotene 7,8-desaturase
IPR014104 Myxoxanthophyll biosynthesis, C-3',4' desaturase CrtD
IPR014105 Zeta-phytoene desaturase
IPR017366 Histone lysine-specific demethylase
IPR017830 Squalene-associated FAD-dependent desaturase

Contains

IPR008150 Phytoene dehydrogenase, bacterial type, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

This entry consists of various amine oxidases, including maize polyamine oxidase (PAO) [1], L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. In vertebrates MAO plays an important role in regulating the intracellular levels of amines via their oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidise spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.

Structural links Help

PDB - click here

SCOP: c.3.1.2 , d.16.1.5

CATH: 1.10.3110.10 , 1.10.405.10 , 3.50.50.60 , 3.90.660.10 , 3.90.660.20

Database links Help

Enzyme: EC:1

PANDIT: PF01593

COMe: PRX000443

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002937

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O09046 L-amino-acid oxidase

O60341 Lysine-specific histone demethylase 1

P18487 Protein anon-37Cs

P50264 Polyamine oxidase FMS1

Q21988 Amine oxidase family member 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR007526	SWIRM
IPR001613	Flavin-containing amine oxidase
IPR017366	Histone lysine-specific demethylase
IPR002937	Amine oxidase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Tavladoraki P, Schinina ME, Cecconi F, Di Agostino S, Manera F, Rea G, Mariottini P, Federico R, Angelini R. Maize polyamine oxidase: primary structure from protein and cDNA sequencing. FEBS Lett. 426 62-6 1998 [PubMed: 9598979] http://dx.doi.org/10.1016/S0014-5793(98)00311-1
2.	Tsugeno Y, Ito A. A key amino acid responsible for substrate selectivity of monoamine oxidase A and B. J. Biol. Chem. 272 14033-6 1997 [PubMed: 9162023] http://dx.doi.org/10.1074/jbc.272.22.14033
3.	Schilling B, Lerch K. Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger. Mol. Gen. Genet. 247 430-8 1995 [PubMed: 7770050] http://dx.doi.org/10.1007/BF00293144

Additional Reading Open in usermanual
	Binda C, Wang J, Li M, Hubalek F, Mattevi A, Edmondson DE. Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B. Biochemistry 47 2008 5616-25 [PubMed: 18426226] http://dx.doi.org/10.1021/bi8002814
	Mimasu S, Sengoku T, Fukuzawa S, Umehara T, Yokoyama S. Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A. Biochem. Biophys. Res. Commun. 366 2008 15-22 [PubMed: 18039463] http://dx.doi.org/10.1016/j.bbrc.2007.11.066
	Yang M, Culhane JC, Szewczuk LM, Gocke CB, Brautigam CA, Tomchick DR, Machius M, Cole PA, Yu H. Structural basis of histone demethylation by LSD1 revealed by suicide inactivation. Nat. Struct. Mol. Biol. 14 2007 535-9 [PubMed: 17529991] http://dx.doi.org/10.1038/nsmb1255
	Binda C, Wang J, Pisani L, Caccia C, Carotti A, Salvati P, Edmondson DE, Mattevi A. Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs. J. Med. Chem. 50 2007 5848-52 [PubMed: 17915852] http://dx.doi.org/10.1021/jm070677y
	Yang M, Culhane JC, Szewczuk LM, Jalili P, Ball HL, Machius M, Cole PA, Yu H. Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine. Biochemistry 46 2007 8058-65 [PubMed: 17569509] http://dx.doi.org/10.1021/bi700664y

InterPro 23.1