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InterPro: IPR006139 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain

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UniProtKB

Matches:

6800 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
Matches in BioMart

Accession

IPR006139 D-isomer_2_OHA_DH_cat_dom

Secondary

IPR002162

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00389	2-Hacid_dh	6800
Signatures in BioMart

InterPro Relationships Help

Children

IPR020921 Erythronate-4-phosphate dehydrogenase

Found in

IPR006236 D-3-phosphoglycerate dehydrogenase
IPR015508 D-3-phosphogylcerate Dehydrogenase

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD or NADH binding

InterPro annotation

Entry Details in BioMart

Abstract

A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. The catalytic domain contains a number of conserved charged residues which may play a role in the catalytic mechanism. The NAD-binding domain is described in IPR006140

Structural links Help

PDB - click here

SCOP: c.2.1.4 , c.23.12.1

CATH: 3.40.50.720

Database links Help

Enzyme: EC:1.1.1

PANDIT: PF00389

Blocks: IPB006139

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006139

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O04130 D-3-phosphoglycerate dehydrogenase, chloroplastic

O43175 D-3-phosphoglycerate dehydrogenase

O46036 C-terminal-binding protein

O88712 C-terminal-binding protein 1

P40054 D-3-phosphoglycerate dehydrogenase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006236	D-3-phosphoglycerate dehydrogenase
IPR016040	NAD(P)-binding domain
IPR002912	Amino acid-binding ACT
IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
IPR015508	D-3-phosphogylcerate Dehydrogenase
IPR006139	D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Help

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
	Quinlan KG, Nardini M, Verger A, Francescato P, Yaswen P, Corda D, Bolognesi M, Crossley M. Specific recognition of ZNF217 and other zinc finger proteins at a surface groove of C-terminal binding proteins. Mol. Cell. Biol. 26 2006 8159-72 [PubMed: 16940172] http://dx.doi.org/10.1128/MCB.00680-06
	Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA. The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase. J. Biol. Chem. 282 2007 18418-26 [PubMed: 17459882] http://dx.doi.org/10.1074/jbc.M701174200
	Dey S, Grant GA, Sacchettini JC. Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits. J. Biol. Chem. 280 2005 14892-9 [PubMed: 15668249] http://dx.doi.org/10.1074/jbc.M414489200
	Dengler U, Niefind K, Kiess M, Schomburg D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. J. Mol. Biol. 267 1997 640-60 [PubMed: 9126843] http://dx.doi.org/10.1006/jmbi.1996.0864
	Booth MP, Conners R, Rumsby G, Brady RL. Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase. J. Mol. Biol. 360 2006 178-89 [PubMed: 16756993] http://dx.doi.org/10.1016/j.jmb.2006.05.018

InterPro 23.1