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InterPro: IPR002198 Short-chain dehydrogenase/reductase SDR

Protein matches Help

UniProtKB

Matches:

47231 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

IPR002198 DH_sc/Rdtase_SDR

Secondary

IPR002347

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00106	adh_short	44126
PRINTS	PR00080	SDRFAMILY	31089
PANTHER	PTHR19410	ADH_short_C2	45556
Signatures in BioMart

InterPro Relationships Help

Children

IPR002347 Glucose/ribitol dehydrogenase
IPR002424 Insect alcohol dehydrogenase family
IPR003560 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
IPR016836 Uncharacterised conserved protein UCP026396, short chain dehydrogenase, Alr5284

Contains

IPR016040 NAD(P)-binding domain
IPR020904 Short-chain dehydrogenase/reductase, conserved site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

The short-chain dehydrogenases/reductases family (SDR) [1] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called [2, 3, 4] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains [5], the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains [5].

Structural links Help

PDB - click here

SCOP: c.2.1.2 , d.106.1.1

CATH: 3.30.1050.10 , 3.40.50.720

Database links Help

PDBe-motif: PS00061

PROSITE doc: PDOC00060

PANDIT: PF00106

Blocks: IPB002198

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

IPR002198

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A6ZLA1 3-ketoacyl-CoA reductase

O16925 Putative steroid dehydrogenase 4

O75828 Carbonyl reductase [NADPH] 3

P00334 Alcohol dehydrogenase

P08074 Carbonyl reductase [NADPH] 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002425	Insect alcohol dehydrogenase
IPR020904	Short-chain dehydrogenase/reductase, conserved site
IPR016040	NAD(P)-binding domain
IPR002347	Glucose/ribitol dehydrogenase
IPR002424	Insect alcohol dehydrogenase family
IPR002198	Short-chain dehydrogenase/reductase SDR
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Jornvall H, Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34 6003-13 1995 [PubMed: 7742302] http://dx.doi.org/10.1021/bi00018a001
2.	Villarroya A, Juan E, Egestad B, Jornvall H. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 180 191-7 1989 [PubMed: 2707261] http://dx.doi.org/10.1111/j.1432-1033.1989.tb14632.x
3.	Persson B, Krook M, Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200 537-43 1991 [PubMed: 1889416] http://dx.doi.org/10.1111/j.1432-1033.1991.tb16215.x
4.	Neidle E, Hartnett C, Ornston LN, Bairoch A, Rekik M, Harayama S. cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 113-20 1992 [PubMed: 1740120] http://dx.doi.org/10.1111/j.1432-1033.1992.tb16612.x
5.	Benyajati C, Place AR, Powers DA, Sofer W. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Proc. Natl. Acad. Sci. U.S.A. 78 2717-21 1981 [PubMed: 6789320] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=6789320

Additional Reading Open in usermanual
	Tu H, Powers JP, Liu J, Ursu S, Sudom A, Yan X, Xu H, Meininger D, Degraffenreid M, He X, Jaen JC, Sun D, Labelle M, Yamamoto H, Shan B, Walker NP, Wang Z. Distinctive molecular inhibition mechanisms for selective inhibitors of human 11beta-hydroxysteroid dehydrogenase type 1. Bioorg. Med. Chem. 16 2008 8922-31 [PubMed: 18789704] http://dx.doi.org/10.1016/j.bmc.2008.08.065
	Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R. The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution. J. Mol. Biol. 282 1998 383-99 [PubMed: 9735295] http://dx.doi.org/10.1006/jmbi.1998.2015
	Hale C, Veniant M, Wang Z, Chen M, McCormick J, Cupples R, Hickman D, Min X, Sudom A, Xu H, Matsumoto G, Fotsch C, St Jean DJ Jr, Wang M. Structural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor. 71 2008 36-44 [PubMed: 18069989] http://dx.doi.org/10.1111/j.1747-0285.2007.00603.x
	Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J. Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. Biochemistry 38 1999 7630-7 [PubMed: 10387002] http://dx.doi.org/10.1021/bi9825044
	Cavazzuti A, Paglietti G, Hunter WN, Gamarro F, Piras S, Loriga M, Allecca S, Corona P, McLuskey K, Tulloch L, Gibellini F, Ferrari S, Costi MP. Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development. Proc. Natl. Acad. Sci. U.S.A. 105 2008 1448-53 [PubMed: 18245389] http://dx.doi.org/10.1073/pnas.0704384105
	Julian LD, Wang Z, Bostick T, Caille S, Choi R, DeGraffenreid M, Di Y, He X, Hungate RW, Jaen JC, Liu J, Monshouwer M, McMinn D, Rew Y, Sudom A, Sun D, Tu H, Ursu S, Walker N, Yan X, Ye Q, Powers JP. Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo model. J. Med. Chem. 51 2008 3953-60 [PubMed: 18553955] http://dx.doi.org/10.1021/jm800310g
	Sun D, Wang Z, Di Y, Jaen JC, Labelle M, Ma J, Miao S, Sudom A, Tang L, Tomooka CS, Tu H, Ursu S, Walker N, Yan X, Ye Q, Powers JP. Discovery and initial SAR of arylsulfonylpiperazine inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1). Bioorg. Med. Chem. Lett. 18 2008 3513-6 [PubMed: 18511278] http://dx.doi.org/10.1016/j.bmcl.2008.05.025

InterPro 23.1