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Protein

Phosphomannomutase/phosphoglucomutase

Gene

algC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).10 Publications

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit (PubMed:23517223). Zn2+ can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672).3 Publications1 Publication

Enzyme regulationi

Both activities are stimulated by EDTA and Mg2+, the dual presence of Mg2+ and another divalent cation inhibits both activities. 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).1 Publication2 Publications

Kineticsi

kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate.1 Publication

Manual assertion based on experiment ini

  • Ref.4
    "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: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.

  1. KM=22 µM for glucose 1-phosphate1 Publication
  2. KM=17 µM for mannose 1-phosphate1 Publication
  3. KM=5.4 µM for glucose 1-phosphate1 Publication
  4. KM=0.38 mM for glucose 6-phosphate1 Publication
  5. KM=0.51 mM for mannose 6-phosphate1 Publication
  6. KM=27.3 µM for glucose 6-phosphate1 Publication

    Temperature dependencei

    TM is 66 degrees Celsius for phosphorylated protein and 62 degrees Celsius for unphosphorylated protein.1 Publication

    Pathwayi: GDP-alpha-D-mannose biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Alginate biosynthesis protein AlgA (algA)
    2. Phosphomannomutase/phosphoglucomutase (algC)
    This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

    Pathwayi: lipopolysaccharide biosynthesis

    This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.
    View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei17Substrate phosphate group4 Publications1
    Active sitei20Proton donor1 Publication1
    Active sitei108Non-phosphorylated intermediate3 Publications1
    Metal bindingi108Magnesium; via phosphate group6 Publications1
    Metal bindingi242Magnesium8 Publications1
    Metal bindingi244Magnesium8 Publications1
    Metal bindingi246Magnesium8 Publications1
    Binding sitei285Substrate sugar group2 Publications1
    Binding sitei308Substrate sugar group4 Publications1
    Active sitei329Proton acceptor1 Publication1

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB
    • phosphoglucomutase activity Source: UniProtKB
    • phosphomannomutase activity Source: UniProtKB

    GO - Biological processi

    • alginic acid biosynthetic process Source: PseudoCAP
    • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
    • lipopolysaccharide core region biosynthetic process Source: PseudoCAP
    • O antigen biosynthetic process Source: CACAO
    • pathogenesis Source: PseudoCAP
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Alginate biosynthesis, Lipopolysaccharide biosynthesis, Virulence

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-19202.
    BRENDAi5.4.2.2. 5087.
    5.4.2.8. 5087.
    SABIO-RKP26276.
    UniPathwayiUPA00030.
    UPA00126; UER00424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase/phosphoglucomutase (EC:5.4.2.21 Publication, EC:5.4.2.81 Publication)
    Short name:
    PMM / PGM
    Gene namesi
    Name:algC
    Ordered Locus Names:PA5322
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    Proteomesi
    • UP000002438 Componenti: Chromosome

    Organism-specific databases

    PseudoCAPiPA5322.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    No longer expresses O-antigen LPS side chain or A-band LPS, sensitive to serum, resistant to virus E79. Has no phosphomannomutase nor phosphoglucomutase activites (PubMed:7515870, PubMed:8050998). Does not make rhamnolipid (PubMed:10481091).3 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi15R → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold. 1 Publication1
    Mutagenesisi20R → A: No phosphoglucomutase activity. 1 Publication1
    Mutagenesisi108S → A or V: About 5% activity, still subject to substrate inhibition and requires G1,6P as an activator; phosphorylation occurs at a different site. 1 Publication1
    Mutagenesisi108S → C: KM for G1P unchanged, kcat decreases 24-fold; G1,6P stimulates reaction by 2-3 orders of magnitude. No stable protein phosphorylation detected, altered ligation of metal residue. 1 Publication1
    Mutagenesisi110N → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold. 1 Publication1
    Mutagenesisi247R → A: Small reduction in KM, small increase in dissociation of G1,6P intermediate. 1 Publication1
    Mutagenesisi262R → A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region. 1 Publication1
    Mutagenesisi325E → A: Reduces KM and Vmax approximately 2-fold. 1 Publication1
    Mutagenesisi329H → A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure. 1 Publication1
    Mutagenesisi368P → G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact. 1 Publication1
    Mutagenesisi421R → C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001478142 – 463Phosphomannomutase/phosphoglucomutaseAdd BLAST462

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei108Phosphoserine4 Publications1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP26276.
    PRIDEiP26276.

    PTM databases

    iPTMnetiP26276.

    Expressioni

    Inductioni

    By D-mannose 6-phosphate.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi208964.PA5322.

    Structurei

    Secondary structure

    1463
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi11 – 13Combined sources3
    Beta strandi16 – 23Combined sources8
    Turni24 – 26Combined sources3
    Helixi29 – 45Combined sources17
    Beta strandi50 – 55Combined sources6
    Helixi61 – 73Combined sources13
    Turni74 – 76Combined sources3
    Beta strandi78 – 84Combined sources7
    Helixi87 – 96Combined sources10
    Beta strandi100 – 105Combined sources6
    Beta strandi114 – 121Combined sources8
    Helixi129 – 140Combined sources12
    Beta strandi149 – 152Combined sources4
    Helixi156 – 164Combined sources9
    Beta strandi173 – 178Combined sources6
    Helixi183 – 186Combined sources4
    Helixi188 – 196Combined sources9
    Beta strandi197 – 203Combined sources7
    Beta strandi211 – 213Combined sources3
    Helixi220 – 223Combined sources4
    Helixi224 – 232Combined sources9
    Beta strandi236 – 241Combined sources6
    Beta strandi245 – 252Combined sources8
    Helixi260 – 274Combined sources15
    Beta strandi279 – 283Combined sources5
    Helixi289 – 296Combined sources8
    Beta strandi300 – 304Combined sources5
    Helixi308 – 318Combined sources11
    Beta strandi321 – 324Combined sources4
    Beta strandi328 – 332Combined sources5
    Turni333 – 336Combined sources4
    Beta strandi338 – 340Combined sources3
    Helixi342 – 354Combined sources13
    Beta strandi356 – 358Combined sources3
    Helixi360 – 365Combined sources6
    Beta strandi376 – 379Combined sources4
    Turni382 – 384Combined sources3
    Helixi385 – 395Combined sources11
    Beta strandi400 – 404Combined sources5
    Beta strandi406 – 413Combined sources8
    Beta strandi416 – 422Combined sources7
    Beta strandi424 – 437Combined sources14
    Helixi438 – 455Combined sources18

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26276.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni13 – 142Topological domain 11 PublicationAdd BLAST130
    Regioni159 – 255Topological domain 21 PublicationAdd BLAST97
    Regioni260 – 364Topological domain 31 PublicationAdd BLAST105
    Regioni325 – 329Binds substrate sugar group3 Publications5
    Regioni375 – 453Topological domain 41 PublicationAdd BLAST79
    Regioni421 – 425Binds substrate phosphate group3 Publications5

    Domaini

    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).3 Publications

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiENOG4107QKV. Bacteria.
    COG1109. LUCA.
    HOGENOMiHOG000268679.
    InParanoidiP26276.
    OMAiAWFNLRA.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti4A → V in AAA25701 (PubMed:1903398).Curated1
    Sequence conflicti21G → R in AAA25701 (PubMed:1903398).Curated1
    Sequence conflicti437T → P in AAA25701 (PubMed:1903398).Curated1

    Mass spectrometryi

    Molecular mass is 50220 Da from positions 2 - 463. Determined by MALDI. May be phosphorylated, protein expressed in E.coli.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.
    PIRiA40013.
    H82979.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi208964.PA5322.

    PTM databases

    iPTMnetiP26276.

    Proteomic databases

    PaxDbiP26276.
    PRIDEiP26276.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG08707; AAG08707; PA5322.
    PATRICi19845501. VBIPseAer58763_5577.

    Organism-specific databases

    PseudoCAPiPA5322.

    Phylogenomic databases

    eggNOGiENOG4107QKV. Bacteria.
    COG1109. LUCA.
    HOGENOMiHOG000268679.
    InParanoidiP26276.
    OMAiAWFNLRA.
    PhylomeDBiP26276.

    Enzyme and pathway databases

    UniPathwayiUPA00030.
    UPA00126; UER00424.
    BioCyciMetaCyc:MONOMER-19202.
    BRENDAi5.4.2.2. 5087.
    5.4.2.8. 5087.
    SABIO-RKP26276.

    Miscellaneous databases

    EvolutionaryTraceiP26276.

    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]
    ProtoNetiSearch...

    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 2, 2016
    This is version 137 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Most crystals have Zn2+ rather than Mg2+ and are catalytically inactive.3 Publications

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.