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InterPro: IPR003099 Prephenate dehydrogenase

Protein matches Help

UniProtKB

Matches:

1641 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

IPR003099 Prephen_DH

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02153	PDH	1579
PROSITE profile	PS51176	PDH_ADH	1633
PANTHER	PTHR21363	Prephen_DH	1358
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008244 Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
IPR008299 Prephenate dehydrogenase/arogenate dehydrogenase predicted, C-terminal regulatory region-containing
IPR012070 Arogenate/prephenate dehydrogenase, plant
IPR012385 Prephenate dehydrogenase, fungal

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0006571 tyrosine biosynthetic process

Function

GO:0004665 prephenate dehydrogenase (NADP+) activity

InterPro annotation

Entry Details in BioMart

Abstract

Members of this family are prephenate dehydrogenases EC:1.3.1.12 involved in tyrosine biosynthesis.

Structural links Help

PDB - click here

SCOP: a.100.1.12 , c.2.1.6

CATH: 3.40.50.720

Database links Help

Enzyme: EC:1.3.1

PROSITE doc: PDOC51176

PANDIT: PF02153

Blocks: IPB003099

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

IPR003099

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O60078 Probable prephenate dehydrogenase [NADP+]

P20049 Prephenate dehydrogenase [NADP+]

P43902 T-protein

Q58029 Probable arogenate/prephenate dehydrogenase

Q944B6 Arogenate dehydrogenase 1, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011277	Chorismate mutase, T-protein
IPR008299	Prephenate dehydrogenase/arogenate dehydrogenase predicted, C-terminal regulatory region-containing
IPR003099	Prephenate dehydrogenase
IPR020822	Chorismate mutase, type II
IPR012385	Prephenate dehydrogenase, fungal
IPR008244	Bifunctional chorismate mutase/prephenate dehydrogenase T-protein
IPR016040	NAD(P)-binding domain
IPR002701	Chorismate mutase
IPR005121	Phenylalanyl-tRNA synthetase, beta subunit, ferrodoxin-fold anticodon-binding
IPR004455	NADP oxidoreductase, coenzyme F420-dependent
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Christendat D, Saridakis VC, Turnbull JL. Use of site-directed mutagenesis to identify residues specific for each reaction catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry 37 1998 15703-12 [PubMed: 9843375] http://dx.doi.org/10.1021/bi981412b
	Rippert P, Matringe M. Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana. Eur. J. Biochem. 269 2002 4753-61 [PubMed: 12354106] http://dx.doi.org/10.1046/j.1432-1033.2002.03172.x
	Zhao G, Xia T, Ingram LO, Jensen RA. An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis. Eur. J. Biochem. 212 1993 157-65 [PubMed: 7916685] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17646.x
	Sun W, Singh S, Zhang R, Turnbull JL, Christendat D. Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism. J. Biol. Chem. 281 2006 12919-28 [PubMed: 16513644] http://dx.doi.org/10.1074/jbc.M511986200
	Legrand P, Dumas R, Seux M, Rippert P, Ravelli R, Ferrer JL, Matringe M. Biochemical characterization and crystal structure of Synechocystis arogenate dehydrogenase provide insights into catalytic reaction. Structure 14 2006 767-76 [PubMed: 16615917] http://dx.doi.org/10.1016/j.str.2006.01.006
	Bonner CA, Jensen RA, Gander JE, Keyhani NO. A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. Biochem. J. 382 2004 279-91 [PubMed: 15171683] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=15171683&action=stream&blobtype=pdf

InterPro 23.1