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InterPro: IPR016305 Mannose-6-phosphate isomerase

Protein matchesHelp
UniProtKB
Matches:
655 proteins
AccessionHelp IPR016305 Mannose-6-P_Isomerase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR001250 Mannose-6-phosphate isomerase, type I
Contains IPR011051 Cupin, RmlC-type
IPR014710 RmlC-like jelly roll fold
IPR018050 Phosphomannose isomerase, type I, conserved site
GO Term annotationHelp
Function GO:0004476 mannose-6-phosphate isomerase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
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].

This group represents a mannose-6-phosphate isomerase.

Structural linksHelp
SCOP: b.82.1.3
Database linksHelp
Enzyme: EC:5.3.1.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016305 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P25081 Mannose-6-phosphate isomerase

P29952 Mannose-6-phosphate isomerase

P34650 Probable mannose-6-phosphate isomerase

P34949 Mannose-6-phosphate isomerase

Q924M7 Mannose-6-phosphate isomerase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR016305 Mannose-6-phosphate isomerase
IPR001250 Mannose-6-phosphate isomerase, type I
IPR018050 Phosphomannose isomerase, type I, conserved site
IPR014710 RmlC-like jelly roll fold
IPR011051 Cupin, RmlC-type
SWISS-MODEL
PDB Chain
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

Additional ReadingHelp
Cleasby A, Wonacott A, Skarzynski T, Hubbard RE, Davies GJ, Proudfoot AE, Bernard AR, Payton MA, Wells TN.
The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution.
Nat. Struct. Biol. 3 1996 470-9 [PubMed: 8612079]
http://dx.doi.org/10.1038/nsb0596-470
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InterPro 23.1