UniProt functional annotation for P26276



	UniProt functional annotation for P26276

UniProt code: P26276.

Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Function: 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). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.

Catalytic activity: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};

Catalytic activity: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23517223}; Note=Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn(2+) can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672). {ECO:0000269|PubMed:23517223, ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16595672, ECO:0000305|PubMed:16880541};

Activity regulation: Requires glucose 1,6-bisphosphate (G1,6P) as an activator (PubMed:8050998, PubMed:11716469). Reaction making glucose 6- phosphate is subject to substrate inhibition, reactions making mannose 1-phosphate or glucose 1-phosphate are not. 1-deoxyglucose 6-phosphate competitively inhibits glucose 1-phosphate (PubMed:11716469). Inhibited by xylose 1-phosphate (PubMed:16880541). {ECO:0000269|PubMed:11716469, ECO:0000269|PubMed:8050998, ECO:0000305|PubMed:16880541}.

Biophysicochemical properties: Kinetic parameters: KM=22 uM for glucose 1-phosphate {ECO:0000269|PubMed:8050998}; KM=17 uM for mannose 1-phosphate {ECO:0000269|PubMed:8050998}; KM=5.4 uM for glucose 1-phosphate {ECO:0000269|PubMed:11716469}; KM=0.38 mM for glucose 6-phosphate {ECO:0000269|PubMed:11716469}; KM=0.51 mM for mannose 6-phosphate {ECO:0000269|PubMed:11716469}; KM=27.3 uM for glucose 6-phosphate {ECO:0000269|PubMed:16595672}; Note=kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate. {ECO:0000269|PubMed:8050998}; Temperature dependence: TM is 66 degrees Celsius for phosphorylated protein and 62 degrees Celsius for unphosphorylated protein. {ECO:0000269|PubMed:24403075};

Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.

Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit: Monomer. {ECO:0000269|PubMed:8050998}.

Induction: By D-mannose 6-phosphate.

Domain: Consists of 4 domains; domains 1-3 have a similar toplological core while domain 4 folds over and closes the active site from a hinge region. Mutants in the hinge region (residues 262 and 368-369) generally increase KM for glucose 1-phosphate 2-fold while reducing kcat about 10-fold (PubMed:18690721). {ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625}.

Mass spectrometry: Mass=50220; Method=MALDI; Note=May be phosphorylated, protein expressed in E.coli.; Evidence={ECO:0000269|PubMed:11716469};

Disruption phenotype: No longer expresses O-antigen LPS side chain or A-band LPS, sensitive to serum, resistant to virus E79. Has no phosphomannomutase nor phosphoglucomutase activities (PubMed:7515870, PubMed:8050998). Does not make rhamnolipid (PubMed:10481091). {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.

Miscellaneous: Most crystals have Zn(2+) rather than Mg(2+) and are catalytically inactive. {ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16595672, ECO:0000305|PubMed:16880541}.

Similarity: Belongs to the phosphohexose mutase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.



Function:		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). {ECO:0000269\|PubMed:10481091, ECO:0000269\|PubMed:11716469, ECO:0000269\|PubMed:16595672, ECO:0000269\|PubMed:16880541, ECO:0000269\|PubMed:18690721, ECO:0000269\|PubMed:1903398, ECO:0000269\|PubMed:22242625, ECO:0000269\|PubMed:23517223, ECO:0000269\|PubMed:7515870, ECO:0000269\|PubMed:8050998}.


Catalytic activity:		Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269\|PubMed:8050998};
Catalytic activity:		Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269\|PubMed:8050998};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:23517223}; Note=Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn(2+) can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672). {ECO:0000269\|PubMed:23517223, ECO:0000305\|PubMed:14725765, ECO:0000305\|PubMed:16595672, ECO:0000305\|PubMed:16880541};
Activity regulation:		Requires glucose 1,6-bisphosphate (G1,6P) as an activator (PubMed:8050998, PubMed:11716469). Reaction making glucose 6- phosphate is subject to substrate inhibition, reactions making mannose 1-phosphate or glucose 1-phosphate are not. 1-deoxyglucose 6-phosphate competitively inhibits glucose 1-phosphate (PubMed:11716469). Inhibited by xylose 1-phosphate (PubMed:16880541). {ECO:0000269\|PubMed:11716469, ECO:0000269\|PubMed:8050998, ECO:0000305\|PubMed:16880541}.
Biophysicochemical properties:		Kinetic parameters: KM=22 uM for glucose 1-phosphate {ECO:0000269\|PubMed:8050998}; KM=17 uM for mannose 1-phosphate {ECO:0000269\|PubMed:8050998}; KM=5.4 uM for glucose 1-phosphate {ECO:0000269\|PubMed:11716469}; KM=0.38 mM for glucose 6-phosphate {ECO:0000269\|PubMed:11716469}; KM=0.51 mM for mannose 6-phosphate {ECO:0000269\|PubMed:11716469}; KM=27.3 uM for glucose 6-phosphate {ECO:0000269\|PubMed:16595672}; Note=kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate. {ECO:0000269\|PubMed:8050998}; Temperature dependence: TM is 66 degrees Celsius for phosphorylated protein and 62 degrees Celsius for unphosphorylated protein. {ECO:0000269\|PubMed:24403075};
Pathway:		Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Pathway:		Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
Subunit:		Monomer. {ECO:0000269\|PubMed:8050998}.
Induction:		By D-mannose 6-phosphate.
Domain:		Consists of 4 domains; domains 1-3 have a similar toplological core while domain 4 folds over and closes the active site from a hinge region. Mutants in the hinge region (residues 262 and 368-369) generally increase KM for glucose 1-phosphate 2-fold while reducing kcat about 10-fold (PubMed:18690721). {ECO:0000269\|PubMed:11839312, ECO:0000269\|PubMed:18690721, ECO:0000269\|PubMed:22242625}.
Mass spectrometry:		Mass=50220; Method=MALDI; Note=May be phosphorylated, protein expressed in E.coli.; Evidence={ECO:0000269\|PubMed:11716469};
Disruption phenotype:		No longer expresses O-antigen LPS side chain or A-band LPS, sensitive to serum, resistant to virus E79. Has no phosphomannomutase nor phosphoglucomutase activities (PubMed:7515870, PubMed:8050998). Does not make rhamnolipid (PubMed:10481091). {ECO:0000269\|PubMed:10481091, ECO:0000269\|PubMed:7515870, ECO:0000269\|PubMed:8050998}.
Miscellaneous:		Most crystals have Zn(2+) rather than Mg(2+) and are catalytically inactive. {ECO:0000305\|PubMed:14725765, ECO:0000305\|PubMed:16595672, ECO:0000305\|PubMed:16880541}.
Similarity:		Belongs to the phosphohexose mutase family. {ECO:0000305}.