algC

Phosphomannomutase/phosphoglucomutase

465 amino acids

The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for biofilm production (By similarity).

Belongs to the phosphohexose mutase family.

50.692 kDa

MNSPASVAPILPDTIFRAYDIRGVVEDTLNAETAYWIGRAIGSESLAQNEPNVSVGRDGRLSGPELVQQLIQGLHDSGCHVSDVGLVPTPALYYAANVLAGKTGVMLTGSHNPKDYNGFKIVIAGDTLANEQIQALHERIKTNNLTSQKGSITQVNILDRYFKQIKDDIVMARKLKVVVDCGNGAAGVIAPQLIEALGCEVISLFAEVDGNFPNHHPDPGKLENLQDLIAKVKETGADLGLAFDGDGDRVGVVTNAGNVVYPDRLLMLFALDVLKRNPGADIIFDVKCTRRLTPLISEHGGRPVMWKTGHSLIKKEMKKSGALLAGEMSGHIFFKERWFGFDDGIYSAARLLEILSQEPANAEDLFETFPNDISTPEINIKVTDVTKFSIIEALEKDAQWGDAKLTTIDGVRVDYPKGWGLVRASNTTPVLVLRFEAETQAELERIQGVFHAELKKVAPDLDLPF

algC

Phosphomannomutase/phosphoglucomutase

463 amino acids

The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for biofilm production (By similarity).

Belongs to the phosphohexose mutase family.

50.272 kDa

MAHLVPAALPDSIFRAYDIRGVVGKTLHAETAYWIGRAIGAQSLAQGEPQVSVGRDGRLSGPMLVEQLIKGLVDAGCNVSDVGLVPTPALYYAANVLAGKSGVMLTGSHNPSDYNGFKIVIAGDTLANEQIQALLTRLKTNDLTLAQGRVEKVEILDRYFKQIVGDVKLAKKLKVVVDCGNGAAGVVAPQLIEALGCEVIPLFCEVDGNFPNHHPDPGKPENLEDLIAKVKETGADIGLAFDGDGDRVGVVTNTGSIVYPDRLLMLFAQDVLSRNPGAEIIFDVKCTRRLTPLIEQHGGRALMWKTGHSLIKKKMKQTGSLLAGEMSGHIFIKERWYGFDDGIYSAARLLEILSKTEQSAENLFAAFPNDISTPEINIDVTDEGKFSIIDALQRDADWGEANLTTIDGVRVDYANGWGLVRASNTTPVLVLRFEADSDAELQRIKDVFRTQLLRVEPELQLPF

algC

Phosphomannomutase/phosphoglucomutase

463 amino acids

Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity. Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme.

Belongs to the phosphohexose mutase family.

50.296 kDa

MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF

algC

Phosphomannomutase/phosphoglucomutase

463 amino acids

Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625).

Belongs to the phosphohexose mutase family.

50.296 kDa

MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF