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PSEAE:ALGC

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Species (Taxon ID) Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228). (208964)
Gene Name(s) algC
Protein Name(s) Phosphomannomutase/phosphoglucomutase

PMM / PGM

External Links
UniProt P26276
EMBL M60873
AE004091
PIR A40013
H82979
PDB 1K2Y
1K35
1P5D
1P5G
1PCJ
1PCM
2FKF
2FKM
2H4L
2H5A
3BKQ
3C04
3RSM
4IL8
4MRQ
PDBsum 1K2Y
1K35
1P5D
1P5G
1PCJ
1PCM
2FKF
2FKM
2H4L
2H5A
3BKQ
3C04
3RSM
4IL8
4MRQ
ProteinModelPortal P26276
SMR P26276
STRING 208964.PA5322
EnsemblBacteria AAG08707
PATRIC 19845501
PseudoCAP PA5322
eggNOG COG1109
HOGENOM HOG000268679
InParanoid P26276
OMA AWFNLRA
OrthoDB EOG6W9X55
PhylomeDB P26276
SABIO-RK P26276
UniPathway UPA00030
UPA00126
EvolutionaryTrace P26276
Proteomes UP000002438
GO GO:0005829
GO:0000287
GO:0004614
GO:0004615
GO:0042121
GO:0009298
GO:0009244
GO:0009243
GO:0009405
Gene3D 3.30.310.50
3.40.120.10
InterPro IPR005844
IPR016055
IPR005845
IPR005846
IPR005843
IPR016066
IPR005841
Pfam PF02878
PF02879
PF02880
PF00408
PRINTS PR00509
SUPFAM SSF53738
SSF55957
PROSITE PS00710

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009243

O antigen biosynthetic process

PMID:7515870[1]

ECO:0000315

P

(Fig. 1A: The LPS from the algC mutants, PAO1 algC::tet and PAClR algC::tet did not produce the wildtype laddering pattern of smooth LPS. The laddering is because of O-antigen.)

Fig 1B: CONFIRMATION THAT LADDERING IS DUE TO EXPRESSION OF O-ANTIGENIC LPS: Polyclonal rabbit antisera raised to purified P. aeruginosa serotype 05 or serotype 03 LPS did not react to LPS recovered from the algC::tet mutant strains, while strong reactions occurred to LPS from the parental and complemented strains.

complete
CACAO 4719

enables

GO:0004615

phosphomannomutase activity

PMID:8050998[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004614

phosphoglucomutase activity

PMID:8050998[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:23517223[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009243

O antigen biosynthetic process

PMID:7515870[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042121

alginic acid biosynthetic process

PMID:22513190[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042121

alginic acid biosynthetic process

PMID:1903398[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:7558335[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009244

lipopolysaccharide core region biosynthetic process

PMID:7515870[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009243

O antigen biosynthetic process

PMID:22513190[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004615

phosphomannomutase activity

PMID:22513190[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004615

phosphomannomutase activity

PMID:1903398[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004614

phosphoglucomutase activity

PMID:7515870[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016066

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005841
InterPro:IPR005844
InterPro:IPR005845
InterPro:IPR005846
InterPro:IPR016055

P

Seeded From UniProt

complete

enables

GO:0016868

intramolecular transferase activity, phosphotransferases

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005841
InterPro:IPR005843
InterPro:IPR005844
InterPro:IPR005846
InterPro:IPR016055
InterPro:IPR036900

F

Seeded From UniProt

complete

involved_in

GO:0071704

organic substance metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005843
InterPro:IPR036900

P

Seeded From UniProt

complete

enables

GO:0004615

phosphomannomutase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.4.2.8

F

Seeded From UniProt

complete

enables

GO:0004614

phosphoglucomutase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:5.4.2.2

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0843

P

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

involved_in

GO:0042121

alginic acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0016

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0009103

lipopolysaccharide biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0448
UniPathway:UPA00030

P

Seeded From UniProt

complete

involved_in

GO:0009298

GDP-mannose biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00126

P

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 Coyne, MJ Jr et al. (1994) The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core. J. Bacteriol. 176 3500-7 PubMed GONUTS page
  2. ↑ 2.0 2.1 Ye, RW et al. (1994) Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide. J. Bacteriol. 176 4851-7 PubMed GONUTS page
  3. ↑ Lee, Y et al. (2013) Identification of an essential active-site residue in the α-D-phosphohexomutase enzyme superfamily. FEBS J. 280 2622-32 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Ma, L et al. (2012) Synthesis of multiple Pseudomonas aeruginosa biofilm matrix exopolysaccharides is post-transcriptionally regulated. Environ. Microbiol. 14 1995-2005 PubMed GONUTS page
  5. ↑ 5.0 5.1 Zielinski, NA et al. (1991) Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. J. Biol. Chem. 266 9754-63 PubMed GONUTS page
  6. ↑ Goldberg, JB et al. (1995) Avirulence of a Pseudomonas aeruginosa algC mutant in a burned-mouse model of infection. Infect. Immun. 63 4166-9 PubMed GONUTS page
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