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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: 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 Mg(2+) 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

  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

    Pathway:iGDP-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.

    Pathway:ilipopolysaccharide 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei17 – 171Substrate phosphate group4 Publications
    Active sitei20 – 201Proton donor1 Publication
    Active sitei108 – 1081Non-phosphorylated intermediate3 Publications
    Metal bindingi108 – 1081Magnesium; via phosphate group6 Publications
    Metal bindingi242 – 2421Magnesium8 Publications
    Metal bindingi244 – 2441Magnesium8 Publications
    Metal bindingi246 – 2461Magnesium8 Publications
    Binding sitei285 – 2851Substrate sugar group2 Publications
    Binding sitei308 – 3081Substrate sugar group4 Publications
    Active sitei329 – 3291Proton acceptor1 Publication

    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

    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 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151R → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 25-fold. 1 Publication
    Mutagenesisi20 – 201R → A: No phosphoglucomutase activity. 1 Publication
    Mutagenesisi108 – 1081S → 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 Publication
    Mutagenesisi108 – 1081S → 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 Publication
    Mutagenesisi110 – 1101N → A: KM halves, decreases processivity as dissociation of G1,6P intermediate increases 30-fold. 1 Publication
    Mutagenesisi247 – 2471R → A: Small reduction in KM, small increase in dissociation of G1,6P intermediate. 1 Publication
    Mutagenesisi262 – 2621R → A: Increases KM 2-fold, decreases kcat 9-fold for G1P. Alters flexibility of the hinge region. 1 Publication
    Mutagenesisi325 – 3251E → A: Reduces KM and Vmax approximately 2-fold. 1 Publication
    Mutagenesisi329 – 3291H → A: No phosphoglucomutase activity using G1P as substrate, protein is less easily phosphorylated, no significant change in structure. 1 Publication
    Mutagenesisi368 – 3681P → G: Increases KM 2-fold, decreases kcat 6-fold for G1P. Alters flexibility of the hinge region, structure is less compact. 1 Publication
    Mutagenesisi421 – 4211R → C: Loss of phosphomannomutase activity, very low phosphoglucomutase activity. 2 Publications

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei108 – 1081Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Inductioni

    By D-mannose 6-phosphate.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 142130Topological domain 11 PublicationAdd
    BLAST
    Regioni159 – 25597Topological domain 21 PublicationAdd
    BLAST
    Regioni260 – 364105Topological domain 31 PublicationAdd
    BLAST
    Regioni325 – 3295Binds substrate sugar group3 Publications
    Regioni375 – 45379Topological domain 41 PublicationAdd
    BLAST
    Regioni421 – 4255Binds substrate phosphate group3 Publications

    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

    eggNOGiCOG1109.
    HOGENOMiHOG000268679.
    InParanoidiP26276.
    OMAiAWFNLRA.
    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. 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
    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...

    Protein-protein interaction databases

    STRINGi208964.PA5322.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAG08707; AAG08707; PA5322.
    PATRICi19845501. VBIPseAer58763_5577.

    Organism-specific databases

    PseudoCAPiPA5322.

    Phylogenomic databases

    eggNOGiCOG1109.
    HOGENOMiHOG000268679.
    InParanoidiP26276.
    OMAiAWFNLRA.
    OrthoDBiEOG6W9X55.
    PhylomeDBiP26276.

    Enzyme and pathway databases

    UniPathwayiUPA00030.
    UPA00126; UER00424.
    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...

    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, FUNCTION AS A PHOSPHOMANNOMUTASE, 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 AS A PHOSPHOGLUCOMUTASE, DISRUPTION PHENOTYPE.
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 and PAC1R.
    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.
      Strain: 8830.
    5. "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, DISRUPTION PHENOTYPE.
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    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: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE REACTION MECHANISM, MASS SPECTROMETRY, PHOSPHORYLATION, 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 (1.75 ANGSTROMS) IN COMPLEX WITH METAL OF WILD-TYPE AND ASP-108 MUTANT, DOMAIN, ACTIVE SITE, PHOSPHORYLATION AT SER-108.
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    8. "Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa."
      Regni C., Naught L., Tipton P.A., Beamer L.J.
      Structure 12:55-63(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH METAL AND SUBSTRATES, COFACTOR, ACTIVE SITE, PHOSPHORYLATION AT SER-108, MUTAGENESIS OF GLU-325.
    9. "Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor."
      Regni C., Shackelford G.S., Beamer L.J.
      Acta Crystallogr. F 62:722-726(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH METAL AND SUBSTRATE OR INHIBITOR, FUNCTION, COFACTOR, ENZYME REGULATION, ACTIVE SITE, PHOSPHORYLATION AT SER-108.
    10. "The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme."
      Regni C., Schramm A.M., Beamer L.J.
      J. Biol. Chem. 281:15564-15571(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-463 IN COMPLEX WITH METAL AND REACTION INTERMEDIATE, FUNCTION, COFACTOR, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT SER-108, MUTAGENESIS OF ARG-15; ARG-20; ASN-110; ARG-247 AND ARG-421.
    11. "Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa."
      Schramm A.M., Mehra-Chaudhary R., Furdui C.M., Beamer L.J.
      Biochemistry 47:9154-9162(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF GLY-368 MUTANT IN COMPLEX WITH METAL OF APOPROTEIN AND IN COMPLEX WITH SUBSTRATE, FUNCTION, COFACTOR, DOMAIN, MUTAGENESIS OF ARG-262 AND PRO-368.
    12. "Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect."
      Sarma A.V., Anbanandam A., Kelm A., Mehra-Chaudhary R., Wei Y., Qin P., Lee Y., Berjanskii M.V., Mick J.A., Beamer L.J., Van Doren S.R.
      Biochemistry 51:807-819(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF CYS-108 MUTANT IN COMPLEX WITH METAL, FUNCTION, DOMAIN, MUTAGENESIS OF SER-108.
    13. "Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily."
      Lee Y., Mehra-Chaudhary R., Furdui C., Beamer L.J.
      FEBS J. 280:2622-2632(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF ALA-329 MUTANT IN COMPLEX WITH MAGNESIUM, FUNCTION, COFACTOR, REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF HIS-329.
    14. "Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase."
      Lee Y., Villar M.T., Artigues A., Beamer L.J.
      J. Biol. Chem. 289:4674-4682(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF DEPHOSPHORYLATED PROTEIN IN COMPLEX WITH METAL, BIOPHYSICOCHEMICAL PROPERTIES.

    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: April 1, 2015
    This is version 132 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

    External Data

    Dasty 3

    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 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.