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InterPro: IPR001509 NAD-dependent epimerase/dehydratase

Protein matches Help

UniProtKB

Matches:

20242 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

IPR001509 Epimerase_deHydtase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01370	Epimerase	20242
Signatures in BioMart

InterPro Relationships Help

Children

IPR005886 UDP-glucose 4-epimerase
IPR005888 dTDP-glucose 4,6-dehydratase
IPR006368 GDP-mannose 4,6-dehydratase
IPR008089 Nucleotide sugar epimerase
IPR011912 ADP-L-glycero-D-manno-heptose-6-epimerase
IPR013445 CDP-glucose 4,6-dehydratase
IPR017829 Hopanoid-associated sugar epimerase

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0044237 cellular metabolic process

Function

GO:0003824 catalytic activity
GO:0050662 coenzyme binding

InterPro annotation

Entry Details in BioMart

Abstract

This family of proteins utilise NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions [1]. It contains the NAD(P)- binding domain (IPR016040) which is a commonly found domain with a core Rossmann-type fold. One of the best studied of these proteins is UDP-galactose 4-epimerase which catalyses the conversion of UDP-galactose to UDP-glucose during galactose metabolism [2, 3].

Structural links Help

PDB - click here

SCOP: c.2.1.2

CATH: 3.40.50.720 , 3.90.25.10

Database links Help

PANDIT: PF01370

Blocks: IPB001509

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

IPR001509

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O45583 GDP-mannose 4,6 dehydratase 2

O60547 GDP-mannose 4,6 dehydratase

P04397 Bifunctional protein GAL10

P23591 GDP-L-fucose synthetase

Q9VMW9 GDP-mannose 4,6 dehydratase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014718	Glycoside hydrolase-type carbohydrate-binding, subgroup
IPR018052	Aldose 1-epimerase, conserved site
IPR011013	Glycoside hydrolase-type carbohydrate-binding
IPR016040	NAD(P)-binding domain
IPR006368	GDP-mannose 4,6-dehydratase
IPR001509	NAD-dependent epimerase/dehydratase
IPR008183	Aldose 1-epimerase
IPR005886	UDP-glucose 4-epimerase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Thoden JB, Hegeman AD, Wesenberg G, Chapeau MC, Frey PA, Holden HM. Structural analysis of UDP-sugar binding to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 36 6294-304 1997 [PubMed: 9174344] http://dx.doi.org/10.1021/bi970025j
2.	Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM. Human UDP-galactose 4-epimerase. Accommodation of UDP-N-acetylglucosamine within the active site. J. Biol. Chem. 276 15131-6 2001 [PubMed: 11279032] http://dx.doi.org/10.1074/jbc.M100220200
3.	Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM. Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry 39 5691-701 2000 [PubMed: 10801319] http://dx.doi.org/10.1021/bi000215l

Additional Reading Open in usermanual
	Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr. Ensemble refinement of protein crystal structures: validation and application. Structure 15 2007 1040-52 [PubMed: 17850744] http://dx.doi.org/10.1016/j.str.2007.06.019
	Thoden JB, Holden HM. The molecular architecture of galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae. J. Biol. Chem. 280 2005 21900-7 [PubMed: 15795221] http://dx.doi.org/10.1074/jbc.M502411200
	Kamitori S, Iguchi A, Ohtaki A, Yamada M, Kita K. X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds. J. Mol. Biol. 352 2005 551-8 [PubMed: 16095619] http://dx.doi.org/10.1016/j.jmb.2005.07.011
	Koropatkin NM, Holden HM. Structure of CDP-D-glucose 4,6-dehydratase from Salmonella typhi complexed with CDP-D-xylose. Acta Crystallogr. D Biol. Crystallogr. 61 2005 365-73 [PubMed: 15805590] http://dx.doi.org/10.1107/S0907444904033876
	Alphey MS, Burton A, Urbaniak MD, Boons GJ, Ferguson MA, Hunter WN. Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 829-34 [PubMed: 16946458] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=16946458&action=stream&blobtype=pdf

InterPro 23.1