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P26276

- ALGC_PSEAE

UniProt

P26276 - ALGC_PSEAE

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Protein

Phosphomannomutase/phosphoglucomutase

Gene

algC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg(2+) ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Phosphoserine intermediate
Metal bindingi108 – 1081Magnesium; via phosphate group
Metal bindingi242 – 2421Magnesium
Metal bindingi244 – 2441Magnesium
Metal bindingi246 – 2461Magnesium
Binding sitei325 – 3251Substrate
Binding sitei327 – 3271Substrate
Binding sitei329 – 3291Substrate
Sitei421 – 4211Interacts with the biphosphorylated intermediate

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphoglucomutase activity Source: PseudoCAP
  3. phosphomannomutase activity Source: PseudoCAP

GO - Biological processi

  1. alginic acid biosynthetic process Source: PseudoCAP
  2. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  3. lipopolysaccharide core region biosynthetic process Source: PseudoCAP
  4. O antigen biosynthetic process Source: CACAO
  5. pathogenesis Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Alginate biosynthesis, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKP26276.
UniPathwayiUPA00030.
UPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase/phosphoglucomutase (EC:5.4.2.2, EC:5.4.2.8)
Short name:
PMM / PGM
Gene namesi
Name:algC
Ordered Locus Names:PA5322
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5322.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081S → A or V: Decrease in activity; phosphorylation occurs at a different site. 1 Publication
Mutagenesisi421 – 4211R → C: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 463462Phosphomannomutase/phosphoglucomutasePRO_0000147814Add
BLAST

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

By D-mannose 6-phosphate.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi208964.PA5322.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Beta strandi16 – 238Combined sources
Turni24 – 263Combined sources
Helixi29 – 4517Combined sources
Beta strandi50 – 556Combined sources
Helixi61 – 7313Combined sources
Turni74 – 763Combined sources
Beta strandi78 – 847Combined sources
Helixi87 – 9610Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi114 – 1218Combined sources
Helixi129 – 14012Combined sources
Beta strandi149 – 1524Combined sources
Helixi156 – 1649Combined sources
Beta strandi173 – 1786Combined sources
Helixi183 – 1864Combined sources
Helixi188 – 1969Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi211 – 2133Combined sources
Helixi220 – 2234Combined sources
Helixi224 – 2329Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi245 – 2528Combined sources
Helixi260 – 27415Combined sources
Beta strandi279 – 2835Combined sources
Helixi289 – 2968Combined sources
Beta strandi300 – 3045Combined sources
Helixi308 – 31811Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi328 – 3325Combined sources
Turni333 – 3364Combined sources
Beta strandi338 – 3403Combined sources
Helixi342 – 35413Combined sources
Beta strandi356 – 3583Combined sources
Helixi360 – 3656Combined sources
Beta strandi376 – 3794Combined sources
Turni382 – 3843Combined sources
Helixi385 – 39511Combined sources
Beta strandi400 – 4045Combined sources
Beta strandi406 – 4138Combined sources
Beta strandi416 – 4227Combined sources
Beta strandi424 – 43714Combined sources
Helixi438 – 45518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray2.00A2-463[»]
2FKMX-ray1.90X2-463[»]
2H4LX-ray2.40X1-463[»]
2H5AX-ray1.72X1-463[»]
3BKQX-ray2.05X1-463[»]
3C04X-ray2.20A1-463[»]
3RSMX-ray2.10A1-463[»]
4IL8X-ray1.80A1-463[»]
4MRQX-ray1.90A9-463[»]
ProteinModelPortaliP26276.
SMRiP26276. Positions 9-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26276.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
InParanoidiP26276.
OMAiEPMVKPT.
OrthoDBiEOG6W9X55.
PhylomeDBiP26276.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26276-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC
60 70 80 90 100
VAVGRDGRLS GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK
110 120 130 140 150
SGVMLTGSHN PPDYNGFKIV VAGETLANEQ IQALRERIEK NDLASGVGSV
160 170 180 190 200
EQVDILPRYF KQIRDDIAMA KPMKVVVDCG NGVAGVIAPQ LIEALGCSVI
210 220 230 240 250
PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA FDGDGDRVGV
260 270 280 290 300
VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR
310 320 330 340 350
PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL
360 370 380 390 400
EILSQDQRDS EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE
410 420 430 440 450
GNITTLDGVR VDYPKGWGLV RASNTTPVLV LRFEADTEEE LERIKTVFRN
460
QLKAVDSSLP VPF
Length:463
Mass (Da):50,296
Last modified:January 23, 2007 - v4
Checksum:i35EE59406379FFB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41A → V in AAA25701. (PubMed:1903398)Curated
Sequence conflicti21 – 211G → R in AAA25701. (PubMed:1903398)Curated
Sequence conflicti437 – 4371T → P in AAA25701. (PubMed:1903398)Curated

Mass spectrometryi

Molecular mass is 50220 Da from positions 2 - 463. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60873 Genomic DNA. Translation: AAA25701.1.
AE004091 Genomic DNA. Translation: AAG08707.1.
PIRiA40013.
H82979.

Genome annotation databases

EnsemblBacteriaiAAG08707; AAG08707; PA5322.
PATRICi19845501. VBIPseAer58763_5577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60873 Genomic DNA. Translation: AAA25701.1 .
AE004091 Genomic DNA. Translation: AAG08707.1 .
PIRi A40013.
H82979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K2Y X-ray 1.75 X 1-463 [» ]
1K35 X-ray 2.20 A 1-463 [» ]
1P5D X-ray 1.60 X 1-463 [» ]
1P5G X-ray 1.61 X 1-463 [» ]
1PCJ X-ray 2.00 X 1-463 [» ]
1PCM X-ray 1.90 X 1-463 [» ]
2FKF X-ray 2.00 A 2-463 [» ]
2FKM X-ray 1.90 X 2-463 [» ]
2H4L X-ray 2.40 X 1-463 [» ]
2H5A X-ray 1.72 X 1-463 [» ]
3BKQ X-ray 2.05 X 1-463 [» ]
3C04 X-ray 2.20 A 1-463 [» ]
3RSM X-ray 2.10 A 1-463 [» ]
4IL8 X-ray 1.80 A 1-463 [» ]
4MRQ X-ray 1.90 A 9-463 [» ]
ProteinModelPortali P26276.
SMRi P26276. Positions 9-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA5322.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08707 ; AAG08707 ; PA5322 .
PATRICi 19845501. VBIPseAer58763_5577.

Organism-specific databases

PseudoCAPi PA5322.

Phylogenomic databases

eggNOGi COG1109.
HOGENOMi HOG000268679.
InParanoidi P26276.
OMAi EPMVKPT.
OrthoDBi EOG6W9X55.
PhylomeDBi P26276.

Enzyme and pathway databases

UniPathwayi UPA00030 .
UPA00126 ; UER00424 .
SABIO-RK P26276.

Miscellaneous databases

EvolutionaryTracei P26276.

Family and domain databases

Gene3Di 3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProi IPR005844. 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 ]
Pfami PF02878. 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 ]
PRINTSi PR00509. PGMPMM.
SUPFAMi SSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEi PS00710. PGM_PMM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiALGC_PSEAE
AccessioniPrimary (citable) accession number: P26276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3