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P26276 (ALGC_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphomannomutase/phosphoglucomutase

Short name=PMM / PGM
EC=5.4.2.2
EC=5.4.2.8
Gene names
Name:algC
Ordered Locus Names:PA5322
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 rhamnolipid production, an exoproduct correlated with pathogenicity, and for biofilm production. Ref.3 Ref.4

Catalytic activity

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.

Cofactor

Binds 1 magnesium ion per subunit.

Pathway

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

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Monomer.

Induction

By D-mannose 6-phosphate.

Sequence similarities

Belongs to the phosphohexose mutase family.

Mass spectrometry

Molecular mass is 50220 Da from positions 2 - 463. Determined by MALDI. Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 463462Phosphomannomutase/phosphoglucomutase
PRO_0000147814

Sites

Active site1081Phosphoserine intermediate
Metal binding1081Magnesium; via phosphate group
Metal binding2421Magnesium
Metal binding2441Magnesium
Metal binding2461Magnesium
Binding site3251Substrate
Binding site3271Substrate
Binding site3291Substrate
Site4211Interacts with the biphosphorylated intermediate

Experimental info

Mutagenesis1081S → A or V: Decrease in activity; phosphorylation occurs at a different site. Ref.6
Mutagenesis4211R → C: Loss of activity. Ref.1
Sequence conflict41A → V in AAA25701. Ref.1
Sequence conflict211G → R in AAA25701. Ref.1
Sequence conflict4371T → P in AAA25701. Ref.1

Secondary structure

................................................................................ 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26276 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 35EE59406379FFB8

FASTA46350,296
        10         20         30         40         50         60 
MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC VAVGRDGRLS 

        70         80         90        100        110        120 
GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK SGVMLTGSHN PPDYNGFKIV 

       130        140        150        160        170        180 
VAGETLANEQ IQALRERIEK NDLASGVGSV EQVDILPRYF KQIRDDIAMA KPMKVVVDCG 

       190        200        210        220        230        240 
NGVAGVIAPQ LIEALGCSVI PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA 

       250        260        270        280        290        300 
FDGDGDRVGV VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR 

       310        320        330        340        350        360 
PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL EILSQDQRDS 

       370        380        390        400        410        420 
EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE GNITTLDGVR VDYPKGWGLV 

       430        440        450        460 
RASNTTPVLV LRFEADTEEE LERIKTVFRN QLKAVDSSLP VPF 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase."
Zielinski N.A., Chakrabarty A.M., Berry A.
J. Biol. Chem. 266:9754-9763(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, MUTAGENESIS OF ARG-421.
Strain: 8830.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core."
Coyne M.J. Jr., Russell K.S., Coyle C.L., Goldberg J.B.
J. Bacteriol. 176:3500-3507(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 and PAC1R.
[4]"The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis."
Olvera C., Goldberg J.B., Sanchez R., Soberon-Chavez G.
FEMS Microbiol. Lett. 179:85-90(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[5]"Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide."
Ye R.W., Zielinski N.A., Chakrabarty A.M.
J. Bacteriol. 176:4851-4857(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 8830.
[6]"Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase."
Naught L.E., Tipton P.A.
Arch. Biochem. Biophys. 396:111-118(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF SER-108.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[7]"Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors."
Regni C., Tipton P.A., Beamer L.J.
Structure 10:269-279(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60873 Genomic DNA. Translation: AAA25701.1.
AE004091 Genomic DNA. Translation: AAG08707.1.
PIRA40013.
H82979.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K2YX-ray1.75X1-463[»]
1K35X-ray2.20A1-463[»]
1P5DX-ray1.60X1-463[»]
1P5GX-ray1.61X1-463[»]
1PCJX-ray2.00X1-463[»]
1PCMX-ray1.90X1-463[»]
2FKFX-ray2.00A2-462[»]
2FKMX-ray1.90X2-462[»]
2H4LX-ray2.40X1-462[»]
2H5AX-ray1.72X2-462[»]
3BKQX-ray2.05X1-463[»]
3C04X-ray2.20A1-463[»]
3RSMX-ray2.10A1-463[»]
4IL8X-ray1.80A1-463[»]
4MRQX-ray1.90A9-463[»]
ProteinModelPortalP26276.
SMRP26276. Positions 9-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC19845501. VBIPseAer58763_5577.

Organism-specific databases

PseudoCAPPA5322.

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268679.
OMAPAKYNGI.
OrthoDBEOG6W9X55.
ProtClustDBCLSK869263.

Enzyme and pathway databases

SABIO-RKP26276.
UniPathwayUPA00030.
UPA00126; UER00424.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
[Graphical view]
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26276.

Entry information

Entry nameALGC_PSEAE
AccessionPrimary (citable) accession number: P26276
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways