HMM Summary Page: TIGR01479

AccessionTIGR01479
NameGMP_PMI
Functionmannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase
Trusted Cutoff372.95
Domain Trusted Cutoff372.95
Noise Cutoff209.40
Domain Noise Cutoff209.40
Isology Typeequivalog
EC Number5.3.1.8 2.7.7.13
HMM Length467
Mainrole CategoryCell envelope
Subrole CategoryBiosynthesis and degradation of surface polysaccharides and lipopolysaccharides
Gene Ontology TermGO:0004476: mannose-6-phosphate isomerase activity molecular_function
GO:0008905: mannose-phosphate guanylyltransferase activity molecular_function
GO:0009103: lipopolysaccharide biosynthetic process biological_process
AuthorHaft DH
Entry DateMar 22 2002 2:27PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal.
ReferencesDR PFAM; PF01050; MannoseP_isomer DR PFAM; PF00483; NTP_transferase DR EXPERIMENTAL; OMNI|NTL03PA03551; Pseudomonas aeruginosa DR EXPERIMENTAL; SP:P29956; Xanthomonas campestris DR EXPERIMENTAL; GP|2569943; Gluconacetobacter xylinus
Genome PropertyGenProp1017: GDP-D-mannose biosynthesis from b-D-fructose-6-phosphate (HMM)
GenProp1017: GDP-D-mannose biosynthesis from b-D-fructose-6-phosphate (HMM)