The domain within your query sequence starts at position 3 and ends at position 119; the E-value for the PMI_typeI domain shown below is 3.1e-45.

VFPLSCVVQQYAWGKVGSKSEVACLLASSDPLAQISEDKPYAELWMGTHPRGDAKILDNR
ISQKTLGQWIAENPDCLGSKVKNTFNGKLPFLFKVLSVDTALSIQAHPNKGSWPQAR

PMI_typeI

PMI_typeI
PFAM accession number:PF01238
Interpro abstract (IPR001250):

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 [(PUBMED:11165500)]. Three classes of PMI have been defined [(PUBMED:8307007)].

Type I includes eukaryotic PMI and the enzyme encoded by the manA gene in enterobacteria. PMI has a bound zinc ion, which is essential for activity.

A crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains [(PUBMED:8612079)]. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.

GO process:carbohydrate metabolic process (GO:0005975)
GO function:mannose-6-phosphate isomerase activity (GO:0004476), zinc ion binding (GO:0008270)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PMI_typeI