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InterPro: IPR006368 GDP-mannose 4,6-dehydratase

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UniProtKB

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1059 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

IPR006368 GDP_Man_deHydtase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR10366:SF32	GDP_mann_dehyd	1052
TIGRFAMs	TIGR01472	gmd	841
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001509 NAD-dependent epimerase/dehydratase

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0019673 GDP-mannose metabolic process

Function

GO:0008446 GDP-mannose 4,6-dehydratase activity

Component

GO:0005622 intracellular

InterPro annotation

Entry Details in BioMart

Abstract

This family represent GDP-mannose 4,6-dehydratase, also known as GDP-D-mannose dehydratase. This enzyme converts GDP-mannose to GDP-4-dehydro-6-deoxy-D-mannose, the first of three steps for the conversion of GDP-mannose to GDP-fucose in animals, plants, and bacteria. In bacteria, GDP-L-fucose acts as a precursor of surface antigens such as the extracellular polysaccharide colanic acid of Escherichia coli. Excluded from this family are members of the clade that are poorly related because of highly dervied (phylogenetically long-branch) sequences, e.g. Aneurinibacillus thermoaerophilus Gmd, described as a bifunctional GDP-mannose 4,6-dehydratase/GDP-6-deoxy-D-lyxo-4-hexulose reductase [1].

Structural links Help

PDB - click here

SCOP: c.2.1.2

CATH: 3.40.50.720 , 3.90.25.10

Database links Help

Enzyme: EC:4.2.1.47

CluSTr: ALLvsALL:29772:86.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006368

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O45583 GDP-mannose 4,6 dehydratase 2

O60547 GDP-mannose 4,6 dehydratase

P93031 GDP-mannose 4,6 dehydratase 2

Q8K0C9 GDP-mannose 4,6 dehydratase

Q9VMW9 GDP-mannose 4,6 dehydratase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016040	NAD(P)-binding domain
IPR006368	GDP-mannose 4,6-dehydratase
IPR001509	NAD-dependent epimerase/dehydratase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Kneidinger B, Graninger M, Adam G, Puchberger M, Kosma P, Zayni S, Messner P. Identification of two GDP-6-deoxy-D-lyxo-4-hexulose reductases synthesizing GDP-D-rhamnose in Aneurinibacillus thermoaerophilus L420-91T. J. Biol. Chem. 276 5577-83 2001 [PubMed: 11096116] http://dx.doi.org/10.1074/jbc.M010027200

Additional Reading Open in usermanual
	Somoza JR, Menon S, Schmidt H, Joseph-McCarthy D, Dessen A, Stahl ML, Somers WS, Sullivan FX. Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose. Structure 8 2000 123-35 [PubMed: 10673432] http://dx.doi.org/10.1016/S0969-2126(00)00088-5
	Webb NA, Mulichak AM, Lam JS, Rocchetta HL, Garavito RM. Crystal structure of a tetrameric GDP-D-mannose 4,6-dehydratase from a bacterial GDP-D-rhamnose biosynthetic pathway. Protein Sci. 13 2004 529-39 [PubMed: 14739333] http://dx.doi.org/10.1110/ps.03393904
	Mulichak AM, Bonin CP, Reiter WD, Garavito RM. Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity. Biochemistry 41 2002 15578-89 [PubMed: 12501186] http://dx.doi.org/10.1021/bi0266683
	Sullivan FX, Kumar R, Kriz R, Stahl M, Xu GY, Rouse J, Chang XJ, Boodhoo A, Potvin B, Cumming DA. Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution of GDP-fucose biosynthesis in vitro. J. Biol. Chem. 273 1998 8193-202 [PubMed: 9525924] http://dx.doi.org/10.1074/jbc.273.14.8193

InterPro 23.1