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InterPro: IPR001538 Mannose-6-phosphate isomerase, type II, C-terminal

Protein matchesHelp
UniProtKB
Matches:
1344 proteins
AccessionHelp IPR001538 Man6P_isomerase-2_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR011051 Cupin, RmlC-type
Found in IPR006375 Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase
IPR014710 RmlC-like jelly roll fold
GO Term annotationHelp
Process GO:0005976 polysaccharide metabolic process
Function GO:0016779 nucleotidyltransferase activity
InterPro annotation
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AbstractHelp

Mannose-6-phosphate isomerase or phosphomannose isomerase (EC:5.3.1.8) (PMI) is the enzyme that catalyses the interconversion of mannose-6-phosphate and fructose-6-phosphate. In eukaryotes PMI is involved in the synthesis of GDP-mannose, a constituent of N- and O-linked glycans and GPI anchors and in prokaryotes it participates in a variety of pathways, including capsular polysaccharide biosynthesis and D-mannose metabolism. PMI's belong to the cupin superfamily whose functions range from isomerase and epimerase activities involved in the modification of cell wall carbohydrates in bacteria and plants, to non-enzymatic storage proteins in plant seeds, and transcription factors linked to congenital baldness in mammals [1]. Three classes of PMI have been defined [2].

The type II phosphomannose isomerases are bifunctional enzymes EC:5.3.1.8. This entry covers the isomerase region of the protein [3]. The guanosine diphospho-D-mannose pyrophosphorylase region is described in another InterPro entry (see IPR005836).

Structural linksHelp
SCOP: b.81.4.1
Database linksHelp
Enzyme: EC:2.7.7.13
PANDIT: PF01050
Blocks: IPB001538
Pfam Clan: CL0029.16

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001538 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
B0RVK6 Xanthan biosynthesis protein xanB

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001538 Mannose-6-phosphate isomerase, type II, C-terminal
IPR014710 RmlC-like jelly roll fold
IPR011051 Cupin, RmlC-type
IPR005835 Nucleotidyl transferase
IPR006375 Mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase
SWISS-MODEL
ModBase

PublicationsHelp
1. Clissold PM, Ponting CP.
JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.
Trends Biochem. Sci. 26 7-9 2001 [PubMed: 11165500]
http://dx.doi.org/10.1016/S0968-0004(00)01700-X
2. Proudfoot AE, Turcatti G, Wells TN, Payton MA, Smith DJ.
Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase.
Eur. J. Biochem. 219 415-23 1994 [PubMed: 8307007]
http://dx.doi.org/10.1111/j.1432-1033.1994.tb19954.x
3. Jensen SO, Reeves PR.
Domain organisation in phosphomannose isomerases (types I and II).
Biochim. Biophys. Acta 1382 5-7 1998 [PubMed: 9507048]
http://dx.doi.org/10.1016/S0167-4838(97)00122-2

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InterPro 23.1