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InterPro: IPR011128 NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal

Protein matches Help

UniProtKB

Matches:

2405 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

IPR011128 NAD-dep_Gly3P_DH_N

Secondary

IPR001652 , IPR006168

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01210	NAD_Gly3P_dh_N	2405
Signatures in BioMart

InterPro Relationships Help

Parent

IPR016040 NAD(P)-binding domain

Found in

IPR006168 NAD-dependent glycerol-3-phosphate dehydrogenase
IPR017751 NAD-dependent glycerol-3-phosphate dehydrogenase, eukaryotic

GO Term annotation Help

Process

GO:0046168 glycerol-3-phosphate catabolic process
GO:0055114 oxidation reduction

Function

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

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyses the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain [1].

Structural links Help

PDB - click here

SCOP: c.2.1.6

CATH: 3.40.50.720

Database links Help

Enzyme: EC:1.1.1.94

PANDIT: PF01210

Blocks: IPB011128

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

IPR011128

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

P34517 Probable glycerol-3-phosphate dehydrogenase 2

P41911 Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
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
IPR013328	Dehydrogenase, multihelical
IPR006109	NAD-dependent glycerol-3-phosphate dehydrogenase, C-terminal
IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Suresh S, Turley S, Opperdoes FR, Michels PA, Hol WG. A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana. Structure 8 541-52 2000 [PubMed: 10801498] http://dx.doi.org/10.1016/S0969-2126(00)00135-0

Additional Reading Open in usermanual
	Choe J, Guerra D, Michels PA, Hol WG. Leishmania mexicana glycerol-3-phosphate dehydrogenase showed conformational changes upon binding a bi-substrate adduct. J. Mol. Biol. 329 2003 335-49 [PubMed: 12758080] http://dx.doi.org/10.1016/S0022-2836(03)00421-2
	Choe J, Suresh S, Wisedchaisri G, Kennedy KJ, Gelb MH, Hol WG. Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase. Chem. Biol. 9 2002 1189-97 [PubMed: 12445769] http://dx.doi.org/10.1016/S1074-5521(02)00243-0
	Britton KL, Asano Y, Rice DW. Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase. Nat. Struct. Biol. 5 1998 593-601 [PubMed: 9665174] http://dx.doi.org/10.1038/854
	Sakasegawa S, Hagemeier CH, Thauer RK, Essen LO, Shima S. Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: a glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference. Protein Sci. 13 2004 3161-71 [PubMed: 15557260] http://dx.doi.org/10.1110/ps.04980304
	Pahlman IL, Larsson C, Averet N, Bunoust O, Boubekeur S, Gustafsson L, Rigoulet M. Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J. Biol. Chem. 277 2002 27991-5 [PubMed: 12032156] http://dx.doi.org/10.1074/jbc.M204079200

InterPro 23.1