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P26276

- ALGC_PSEAE

UniProt

P26276 - ALGC_PSEAE

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
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    Binds 1 magnesium 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

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC    50
    VAVGRDGRLS GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK 100
    SGVMLTGSHN PPDYNGFKIV VAGETLANEQ IQALRERIEK NDLASGVGSV 150
    EQVDILPRYF KQIRDDIAMA KPMKVVVDCG NGVAGVIAPQ LIEALGCSVI 200
    PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA FDGDGDRVGV 250
    VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR 300
    PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL 350
    EILSQDQRDS EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE 400
    GNITTLDGVR VDYPKGWGLV RASNTTPVLV LRFEADTEEE LERIKTVFRN 450
    QLKAVDSSLP VPF 463
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60873 Genomic DNA. Translation: AAA25701.1 .
    AE004091 Genomic DNA. Translation: AAG08707.1 .
    PIRi A40013.
    H82979.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 126 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