Pfam 22.0 :: FAD_binding

Pfam 22.0 :: FAD_binding_3
Description of the FAD_binding_3 family

FAD_binding_2 <--	--> FAD_binding_4
FAD_binding_3

Accession number: PF01494
FAD binding domain

This domain is involved in FAD binding in a number of enzymes.

Description
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 PUBMED:1444267. 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 PUBMED:10025942.
Description text from InterPro entry IPR002938

Sequence information

Alignment

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Visualize domain structures

Seed (20) Full (1756)

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Species distribution

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Literature References

[1]
Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3A resolution.
Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J;
Proteins 1992;14:178-190.

Database References

HOMSTRAD	PHBH
PFAMB The following Pfam-B families contain sequences that according to Prodom are members of this Pfam-A family.	PB001944 PB004775 PB010425 PB021014 PB028701 PB036510 PB067193 PB070826 PB073122 PB120701 PB127368 PB133845 PB139012 PB139030 PB145330 PB153761 PB173506 PB173519 PB176207 PB176230 PB178503 PB180854 PB181485 PB181493 PB181917 PB182073
SCOP	2phh (family)
INTERPRO	IPR002938

HMMER build information

	Pfam_ls [download HMM]	Pfam_fs [download HMM]
Gathering cutoff	-136.60 -136.60	14.90 14.90
Trusted cutoff	-136.50 -136.50	14.90 14.90
Noise cutoff	-136.70 -136.70	14.80 14.80
Build method of HMM	hmmbuild -F HMM_ls SEED hmmcalibrate --seed 0 HMM_ls	hmmbuild -f -F HMM_fs SEED hmmcalibrate --seed 0 HMM_fs

Pfam specific information

Author of entry	Bashton M, Bateman A
Type definition	Family
Source of seed members	Pfam-B_549 (release 4.0)