EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR013118 Mannitol dehydrogenase, C-terminal

Protein matches Help

UniProtKB

Matches:

1647 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

IPR013118 Mannitol_DH_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF08125	Mannitol_dh_C	1647
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013328 Dehydrogenase, multihelical

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity
GO:0050662 coenzyme binding

InterPro annotation

Entry Details in BioMart

Abstract

Long-chain mannitol dehydrogenases are a group of secondary alcohol dehydrogenases that differ from other alcohol or polyol dehydrogenases in that they do not utilise Zn(2+) or other metal cofactors and do not contain a conserved catalytic tyrosine residue. The proteins in this family that have been studied are monomeric enzymes of ~54 kDa and include:

Mannitol-1-phosphate 5-dehydrogenase (EC:1.1.1.17) [1]
Mannitol 2-dehydrogenase (EC:1.1.1.67) [2]
D-arabinitol 4-dehydrogenase (EC:1.1.1.11) [3]
Altronate oxidoreductase (EC:1.1.1.58)
D-mannonate oxidoreductase (EC:1.1.1.57)

These enzymes are mostly found in bacteria, though they are also present in some fungal species.

This entry represents the C-terminal substrate-binding domain of long-chain mannitol dehydrogenases. This domain is primarily alpha-helical in nature, being composed of eleven helices and a small beta hairpin [4]. Most of the residues implicated in substrate binding are located within this region, and a conserved lysine residue is thought to act as a proton acceptor during catalysis.

Structural links Help

PDB - click here

SCOP: a.100.1.9 , c.2.1.6

CATH: 1.10.1040.10 , 3.40.50.720

Database links Help

Enzyme: EC:1.1.1

PANDIT: PF08125

Blocks: IPB013118

Pfam Clan: CL0106.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013118

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A1C6B4 Mannitol-1-phosphate 5-dehydrogenase

P39941 Mannitol dehydrogenase DSF1

Q83PQ0 Mannitol-1-phosphate 5-dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008927	6-phosphogluconate dehydrogenase, C-terminal-like
IPR013118	Mannitol dehydrogenase, C-terminal
IPR016040	NAD(P)-binding domain
IPR013131	Mannitol dehydrogenase, N-terminal
IPR013328	Dehydrogenase, multihelical
IPR000669	Mannitol dehydrogenase, core
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Behrens S, Mitchell W, Bahl H. Molecular analysis of the mannitol operon of Clostridium acetobutylicum encoding a phosphotransferase system and a putative PTS-modulated regulator. Microbiology (Reading, Engl.) 147 75-86 2001 [PubMed: 11160802] http://mic.sgmjournals.org/cgi/content/abstract/147/1/75
2.	Schneider KH, Giffhorn F, Kaplan S. Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodobacter sphaeroides. J. Gen. Microbiol. 139 2475-84 1993 [PubMed: 8254318]
3.	Heuel H, Shakeri-Garakani A, Turgut S, Lengeler JW. Genes for D-arabinitol and ribitol catabolism from Klebsiella pneumoniae. Microbiology (Reading, Engl.) 144 ( Pt 6) 1631-9 1998 [PubMed: 9639934]
4.	Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK. Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism. J. Biol. Chem. 277 43433-42 2002 [PubMed: 12196534] http://dx.doi.org/10.1074/jbc.M206914200

InterPro 23.1