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InterPro: IPR002938 Monooxygenase, FAD-binding

Protein matches Help

UniProtKB

Matches:

6935 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

IPR002938 mOase_FAD_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01494	FAD_binding_3	6935
Signatures in BioMart

InterPro Relationships Help

Parent

IPR003042 Aromatic-ring hydroxylase-like

Children

IPR010971 Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6
IPR012733 4-hydroxybenzoate 3-monooxygenase
IPR017631 Salicylate 1-monooxygenase

Found in

IPR017079 Zeaxanthin epoxidase

Contains

IPR018168 Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0004497 monooxygenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Monooxygenases incorporate one hydroxyl group into substrates and are found in many metabolic pathways. In this reaction, two atoms of dioxygen are reduced to one hydroxyl group and one H₂O molecule by the concomitant oxidation of NAD(P)H [1]. P-hydroxybenzoate hydroxylase from Pseudomonas fluorescens contains this sequence motif (present in in flavoprotein hydroxylases) with a putative dual function in FAD and NADPH binding [2].

Structural links Help

PDB - click here

SCOP: c.3.1.2 , d.16.1.2

CATH: 3.30.9.10 , 3.50.50.60

Database links Help

PANDIT: PF01494

Blocks: IPB002938

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

IPR002938

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1Z746 Kynurenine 3-monooxygenase

O01884 Probable ubiquinone biosynthesis monooxygenase coq-6

O94851 Protein MICAL-2

P53318 Ubiquinone biosynthesis monooxygenase COQ6

Q8VDP3 NEDD9-interacting protein with calponin homology and LIM domains

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016146	Calponin-homology
IPR010971	Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6
IPR003042	Aromatic-ring hydroxylase-like
IPR018168	Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site
IPR000689	Ubiquinone biosynthesis monooxygenase, COQ6-type
IPR002938	Monooxygenase, FAD-binding
IPR001715	Calponin-like actin-binding
IPR001781	Zinc finger, LIM-type
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Harayama S, Kok M, Neidle EL. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46 565-601 1992 [PubMed: 1444267] http://dx.doi.org/10.1146/annurev.mi.46.100192.003025
2.	Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ. Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. FEBS Lett. 443 251-5 1999 [PubMed: 10025942] http://dx.doi.org/10.1016/S0014-5793(98)01726-8

Additional Reading Open in usermanual
	Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL. Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase. Proc. Natl. Acad. Sci. U.S.A. 99 2002 608-13 [PubMed: 11805318] http://dx.doi.org/10.1073/pnas.022640199
	Ortiz-Maldonado M, Gatti D, Ballou DP, Massey V. Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins. Biochemistry 38 1999 16636-47 [PubMed: 10600126] http://dx.doi.org/10.1021/bi991603u
	Cole LJ, Gatti DL, Entsch B, Ballou DP. Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase. Biochemistry 44 2005 8047-58 [PubMed: 15924424] http://dx.doi.org/10.1021/bi050108x
	Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J. Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution. Proteins 14 1992 178-90 [PubMed: 1409567] http://dx.doi.org/10.1002/prot.340140205
	Enroth C. High-resolution structure of phenol hydroxylase and correction of sequence errors. Acta Crystallogr. D Biol. Crystallogr. 59 2003 1597-602 [PubMed: 12925790] http://dx.doi.org/10.1107/S0907444903014902

InterPro 23.1