Accession | TIGR01479 |
Name | GMP_PMI |
Function | mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase |
Trusted Cutoff | 372.95 |
Domain Trusted Cutoff | 372.95 |
Noise Cutoff | 209.40 |
Domain Noise Cutoff | 209.40 |
Isology Type | equivalog |
EC Number | 5.3.1.8 2.7.7.13 |
HMM Length | 467 |
Mainrole Category | Cell envelope |
Subrole Category | Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides |
Gene Ontology Term | GO:0004476: mannose-6-phosphate isomerase activity molecular_function |
| GO:0008905: mannose-phosphate guanylyltransferase activity molecular_function |
| GO:0009103: lipopolysaccharide biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Mar 22 2002 2:27PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This 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. |
References | DR 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 Property | GenProp1017: GDP-D-mannose biosynthesis from b-D-fructose-6-phosphate (HMM) |
| GenProp1017: GDP-D-mannose biosynthesis from b-D-fructose-6-phosphate (HMM) |