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InterPro: IPR003042 Aromatic-ring hydroxylase-like

Protein matches Help

UniProtKB

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8607 proteins

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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

IPR003042 Rng_hydrolase-like

Secondary

IPR000733

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00420	RNGMNOXGNASE	8607
Signatures in BioMart

InterPro Relationships Help

Children

IPR002938 Monooxygenase, FAD-binding
IPR011777 Geranylgeranyl reductase, plant/prokaryotic

Found in

IPR017079 Zeaxanthin epoxidase

Contains

IPR013698 Squalene epoxidase
IPR018168 Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Bacterial aromatic-ring hydroxylases (flavoprotein monooxygenases) incorporate one hydroxyl group into substrates. 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. Flavoprotein hydroxylases that catalyze the monohydroxylation of the aromatic ring carry out two reactions on a single polypeptide chain; the oxidation of NAD(P)H to generate two reducing equivalents, and the hydroxylation of substrates [1].

Structural links Help

PDB - click here

SCOP: c.3.1.2

CATH: 3.30.9.10 , 3.50.50.60

Database links Help

Blocks: IPB003042

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003042

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

P32476 Squalene monooxygenase

P52019 Squalene monooxygenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006076	FAD dependent oxidoreductase
IPR016146	Calponin-homology
IPR013698	Squalene epoxidase
IPR010971	Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6
IPR003042	Aromatic-ring hydroxylase-like
IPR002938	Monooxygenase, FAD-binding
IPR000689	Ubiquinone biosynthesis monooxygenase, COQ6-type
IPR001715	Calponin-like actin-binding
IPR001781	Zinc finger, LIM-type
IPR018168	Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6, conserved site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL

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

Additional Reading Open in usermanual
	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 1999 251-5 [PubMed: 10025942] http://dx.doi.org/10.1016/S0014-5793(98)01726-8
	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
	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, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, van Berkel WJ. Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring. Biochemistry 33 1994 10161-70 [PubMed: 7520279] http://dx.doi.org/10.1021/bi00199a044
	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
	Treiber N, Schulz GE. Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway. J. Mol. Biol. 379 2008 94-104 [PubMed: 18440023] http://dx.doi.org/10.1016/j.jmb.2008.03.032

InterPro 23.1