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InterPro: IPR013328 Dehydrogenase, multihelical

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UniProtKB

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15490 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
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Accession List
Matches in BioMart

Accession

IPR013328 DH_multihelical

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:1.10.1040.10	Opine_DH	15490
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like

Children

IPR003421 Opine dehydrogenase
IPR006108 3-hydroxyacyl-CoA dehydrogenase, C-terminal
IPR006109 NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
IPR006114 6-phosphogluconate dehydrogenase, C-terminal
IPR013118 Mannitol dehydrogenase, C-terminal
IPR013752 Ketopantoate reductase ApbA/PanE, C-terminal
IPR015814 Phosphogluconate dehydrogenase, NAD-binding, putative, C-terminal

Found in

IPR006398 2-hydroxy-3-oxopropionate reductase
IPR011548 3-hydroxyisobutyrate dehydrogenase
IPR012799 Fatty oxidation complex, alpha subunit FadB
IPR014028 UDP-glucose/GDP-mannose dehydrogenase, dimerisation and substrate-binding domain
IPR015815 3-hydroxyacid dehydrogenase/reductase
IPR016206 Ketol-acid reductoisomerase, plant
IPR016207 Ketol-acid reductoisomerase, fungi

Contains

IPR006180 3-hydroxyacyl-CoA dehydrogenase, conserved site
IPR006184 6-phosphogluconate-binding site

GO Term annotation Help

Function

GO:0016491 oxidoreductase activity
GO:0050662 coenzyme binding

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a multi-helical domain found in several NAD or NADP-utilizing dehydrogenases, including 6-phosphogluconate dehydrogenase [1], classes I and II ketol-acid reductoisomerases [2], L-3-hydroxyacyl CoA dehydrogenase [3], UDP-glucose dehydrogenase [4], glycerol-3-phosphate dehydrogenase [5], ketopantoate reductase [6], N-(1-D-carboxylethyl)-L-norvaline dehydrogenase [7], and mannitol 2-dehydrogenase [8]. This domain is often found in the C-terminal region of the protein.

Structural links Help

PDB - click here

SCOP: a.100.1.1 , a.100.1.2 , a.100.1.3 , a.100.1.5 , a.100.1.6 , a.100.1.7 , a.100.1.8 , a.100.1.9 , c.2.1.6

CATH: 1.10.1040.10

Database links Help

Enzyme: EC:1.1.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013328

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P13706 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P13707 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P21695 Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic

P34439 Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1

P38720 6-phosphogluconate dehydrogenase, decarboxylating 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006180	3-hydroxyacyl-CoA dehydrogenase, conserved site
IPR012284	Fibritin/6-phosphogluconate dehydrogenase, C-terminal extension
IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
IPR006168	NAD-dependent glycerol-3-phosphate dehydrogenase
IPR008927	6-phosphogluconate dehydrogenase, C-terminal-like
IPR016040	NAD(P)-binding domain
IPR017751	NAD-dependent glycerol-3-phosphate dehydrogenase, eukaryotic
IPR006113	6-phosphogluconate dehydrogenase, decarboxylating
IPR006114	6-phosphogluconate dehydrogenase, C-terminal
IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
IPR006108	3-hydroxyacyl-CoA dehydrogenase, C-terminal
IPR006183	6-phosphogluconate dehydrogenase
IPR006109	NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
IPR013328	Dehydrogenase, multihelical
IPR006184	6-phosphogluconate-binding site
IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL

Publications Open in usermanual
1.	Li L, Dworkowski FS, Cook PF. Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase. J. Biol. Chem. 281 25568-76 2006 [PubMed: 16803886] http://dx.doi.org/10.1074/jbc.M601154200
2.	Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG. The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Protein Sci. 14 3089-100 2005 [PubMed: 16322583] http://dx.doi.org/10.1110/ps.051791305
3.	Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ. Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. J. Biol. Chem. 276 36718-26 2001 [PubMed: 11451959] http://dx.doi.org/10.1074/jbc.M104839200
4.	Huh JW, Lee HJ, Choi MM, Yang SJ, Yoon SY, Kim DW, Kim SY, Choi SY, Cho SW. Identification of a UDP-glucose-binding site of human UDP-glucose dehydrogenase by photoaffinity labeling and cassette mutagenesis. Bioconjug. Chem. 16 710-6 2005 [PubMed: 15898741] http://dx.doi.org/10.1021/bc0500387
5.	Ou X, Ji C, Han X, Zhao X, Li X, Mao Y, Wong LL, Bartlam M, Rao Z. Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1). J. Mol. Biol. 357 858-69 2006 [PubMed: 16460752] http://dx.doi.org/10.1016/j.jmb.2005.12.074
6.	Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL. The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. Biochemistry 44 8930-9 2005 [PubMed: 15966718] http://dx.doi.org/10.1021/bi0502036
7.	Britton KL, Asano Y, Rice DW. Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase. Nat. Struct. Biol. 5 593-601 1998 [PubMed: 9665174] http://dx.doi.org/10.1038/854
8.	Simon-Nobbe B, Denk U, Schneider PB, Radauer C, Teige M, Crameri R, Hawranek T, Lang R, Richter K, Schmid-Grendelmeier P, Nobbe S, Hartl A, Breitenbach M. NADP-dependent mannitol dehydrogenase, a major allergen of Cladosporium herbarum. J. Biol. Chem. 281 16354-60 2006 [PubMed: 16608840] http://dx.doi.org/10.1074/jbc.M513638200

Additional Reading Open in usermanual
	Sundaramoorthy R, Iulek J, Barrett MP, Bidet O, Ruda GF, Gilbert IH, Hunter WN. Crystal structures of a bacterial 6-phosphogluconate dehydrogenase reveal aspects of specificity, mechanism and mode of inhibition by analogues of high-energy reaction intermediates. FEBS J. 274 2007 275-86 [PubMed: 17222187] http://dx.doi.org/10.1111/j.1742-4658.2006.05585.x
	Ciulli A, Lobley CM, Tuck KL, Smith AG, Blundell TL, Abell C. pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study. Acta Crystallogr. D Biol. Crystallogr. 63 2007 171-8 [PubMed: 17242510] http://dx.doi.org/10.1107/S0907444906044465
	Osipiuk J, Zhou M, Moy S, Collart F, Joachimiak A. X-Ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium. J. Struct. Funct. Genomics 2009 [PubMed: 19184529]
	He W, Wang Y, Liu W, Zhou CZ. Crystal structure of Saccharomyces cerevisiae 6-phosphogluconate dehydrogenase Gnd1. BMC Struct. Biol. 7 2007 38 [PubMed: 17570834] http://dx.doi.org/10.1186/1472-6807-7-38
	Ciulli A, Chirgadze DY, Smith AG, Blundell TL, Abell C. Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity. J. Biol. Chem. 282 2007 8487-97 [PubMed: 17229734] http://dx.doi.org/10.1074/jbc.M611171200

InterPro 23.1