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InterPro: IPR000846 Dihydrodipicolinate reductase

Protein matches Help

UniProtKB

Matches:

2116 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

IPR000846 DapB

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01113	DapB_N	2110
Pfam	PF05173	DapB_C	1641
PROSITE pattern	PS01298	DAPB	1487
Signatures in BioMart

InterPro Relationships Help

Children

IPR011770 Dihydrodipicolinate reductase, bacterial/plant

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0055114 oxidation reduction

Function

GO:0008839 dihydrodipicolinate reductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Dihydrodipicolinate reductase catalyzes the second step in the biosynthesis of diaminopimelic acid and lysine, the NAD or NADP-dependent reduction of 2,3-dihydrodipicolinate into 2,3,4,5-tetrahydrodipicolinate.

In Escherichia coli and Mycobacterium tuberculosis, dihydrodipicolinate reductase has equal specificity for NADH and NADPH, however in Thermotoga maritima there it has a greater affinity for NADPH [1]. In addition, the enzyme is inhibited by high concentrations of its substrate, which consequently acts as a feedback control on the lysine biosynthesis pathway. In T. maritima, the enzyme also lacks N-terminal and C-terminal loops which are present in enzyme of the former two organisms.

Structural links Help

PDB - click here

SCOP: c.2.1.3 , d.81.1.3

CATH: 3.30.360.10 , 3.40.50.720

Database links Help

PDBe-motif: PS01298

Enzyme: EC:1.3.1.26

PROSITE doc: PDOC01000

PANDIT: PF01113 , PF05173

Blocks: IPB000846

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

IPR000846

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O80574 Dihydrodipicolinate reductase 1, chloroplastic

P04036 Dihydrodipicolinate reductase

P72642 Dihydrodipicolinate reductase

Q04304 UPF0659 protein YMR090W

Q10P67 Probable dihydrodipicolinate reductase 2, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011770	Dihydrodipicolinate reductase, bacterial/plant
IPR016040	NAD(P)-binding domain
IPR000846	Dihydrodipicolinate reductase
IPR011859	Dihydrodipicolinate reductase, plant
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Pearce FG, Sprissler C, Gerrard JA. Characterization of dihydrodipicolinate reductase from Thermotoga maritima reveals evolution of substrate binding kinetics. J. Biochem. 143 617-23 2008 [PubMed: 18250105] http://dx.doi.org/10.1093/jb/mvn012

Additional Reading Open in usermanual
	Cirilli M, Zheng R, Scapin G, Blanchard JS. The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity. Biochemistry 42 2003 10644-50 [PubMed: 12962488] http://dx.doi.org/10.1021/bi030044v
	Reddy SG, Scapin G, Blanchard JS. Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Biochemistry 35 1996 13294-302 [PubMed: 8873595] http://dx.doi.org/10.1021/bi9615809
	Scapin G, Reddy SG, Zheng R, Blanchard JS. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry 36 1997 15081-8 [PubMed: 9398235] http://dx.doi.org/10.1021/bi9719915
	Scapin G, Cirilli M, Reddy SG, Gao Y, Vederas JC, Blanchard JS. Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase. Biochemistry 37 1998 3278-85 [PubMed: 9521647] http://dx.doi.org/10.1021/bi9727949
	Cirilli M, Scapin G, Sutherland A, Vederas JC, Blanchard JS. The three-dimensional structure of the ternary complex of Corynebacterium glutamicum diaminopimelate dehydrogenase-NADPH-L-2-amino-6-methylene-pimelate. Protein Sci. 9 2000 2034-7 [PubMed: 11106178] http://www.proteinscience.org/cgi/content/abstract/9/10/2034
	Scapin G, Blanchard JS, Sacchettini JC. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34 1995 3502-12 [PubMed: 7893645] http://dx.doi.org/10.1021/bi00011a003
	Scapin G, Reddy SG, Blanchard JS. Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum. Biochemistry 35 1996 13540-51 [PubMed: 8885833] http://dx.doi.org/10.1021/bi961628i

InterPro 23.1