Phosphomannomutase/phosphoglucomutase

Details

Name
Phosphomannomutase/phosphoglucomutase
Synonyms
  • 5.4.2.2
  • PMM / PGM
Gene Name
algC
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Amino acid sequence
>lcl|BSEQ0019106|Phosphomannomutase/phosphoglucomutase
MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLS
GPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIV
VAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCG
NGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLA
FDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGR
PVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDS
EHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLV
RASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF
Number of residues
463
Molecular Weight
50295.09
Theoretical pI
4.95
GO Classification
Functions
magnesium ion binding / phosphoglucomutase activity / phosphomannomutase activity
Processes
alginic acid biosynthetic process / GDP-mannose biosynthetic process / lipopolysaccharide core region biosynthetic process / O antigen biosynthetic process / pathogenesis
Components
cytosol
General Function
Phosphomannomutase activity
Specific Function
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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0002716|1392 bp
ATGAGCACTGTAAAAGCACCGACGCTGCCCGCCAGCATCTTCCGCGCCTACGACATCCGT
CGCGTGGTAGGCGATACCCTCACCGCCGAGACCGCCTACTGGATCGGTCGCGCCATCGGC
TCGGAAAGCCTCGCCCGCGGCGAACCGTGCGTCGCTGTCGGCCGCGATGGCCGCCTGTCC
GGTCCCGAGCTGGTCAAGCAGCTGATCCAGGGCCTGGTGGACTGCGGTTGCCAGGTCAGC
GACGTGGGCATGGTGCCTACCCCGGTGCTGTACTACGCGGCCAACGTGCTCGAGGGCAAG
TCCGGGGTGATGCTGACCGGCAGCCACAATCCGCCGGACTACAACGGCTTCAAGATCGTG
GTCGCCGGCGAGACCCTGGCCAACGAGCAGATCCAGGCCCTGCGCGAGCGCATCGAGAAA
AACGACCTGGCATCCGGCGTCGGCAGCGTAGAGCAGGTCGACATCCTGCCGCGCTACTTC
AAGCAGATCCGCGACGACATCGCCATGGCCAAGCCGATGAAGGTGGTGGTCGACTGCGGC
AACGGCGTGGCCGGGGTGATCGCCCCGCAGTTGATCGAGGCCCTGGGCTGCAGCGTGATC
CCGCTGTACTGCGAGGTCGACGGCAACTTCCCGAACCACCATCCGGACCCGGGCAAGCCG
GAGAACCTGAAGGACCTGATCGCCAAGGTCAAGGCCGAGAACGCCGACCTGGGCCTGGCC
TTCGACGGCGACGGCGATCGCGTCGGCGTGGTCACCAATACCGGTACCATCATCTATCCG
GACCGTCTGCTGATGCTGTTCGCCAAGGACGTGGTCTCGCGCAACCCGGGGGCCGACATC
ATCTTCGACGTCAAGTGCACCCGCCGTCTGATCGCCCTGATCAGCGGCTACGGCGGCCGT
CCGGTGATGTGGAAGACCGGCCACTCGCTGATCAAGAAGAAGATGAAGGAAACCGGCGCC
CTGCTGGCTGGCGAGATGAGCGGCCACGTGTTCTTCAAGGAGCGCTGGTTCGGCTTCGAC
GATGGCATCTACAGCGCCGCCCGCCTGCTGGAAATCCTCAGCCAGGATCAGCGTGACAGC
GAGCACGTGTTCTCGGCCTTCCCGAGCGACATTTCCACCCCGGAAATCAACATCACCGTC
ACCGAGGACAGCAAGTTCGCCATCATCGAGGCGCTGCAACGCGACGCCCAATGGGGCGAA
GGCAACATCACCACCCTCGACGGCGTGCGGGTCGACTACCCCAAAGGCTGGGGCCTGGTA
CGCGCCTCCAACACCACTCCCGTGCTGGTCCTGCGCTTCGAAGCGGACCCCGAGGAAGAG
CTGGAGCGCATCAAGACCGTCTTCCGTAACCAACTGAAGGCAGTGGATTCCTCGCTGCCC
GTGCCCTTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP26276
UniProtKB Entry NameALGC_PSEAE
GenBank Protein ID150994
GenBank Gene IDM60873
General References
  1. Zielinski NA, Chakrabarty AM, Berry A: Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase. J Biol Chem. 1991 May 25;266(15):9754-63. [Article]
  2. Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV: Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature. 2000 Aug 31;406(6799):959-64. [Article]
  3. Coyne MJ Jr, Russell KS, Coyle CL, Goldberg JB: The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core. J Bacteriol. 1994 Jun;176(12):3500-7. [Article]
  4. Ye RW, Zielinski NA, Chakrabarty AM: Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide. J Bacteriol. 1994 Aug;176(16):4851-7. [Article]
  5. Olvera C, Goldberg JB, Sanchez R, Soberon-Chavez G: The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis. FEMS Microbiol Lett. 1999 Oct 1;179(1):85-90. [Article]
  6. Naught LE, Tipton PA: Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase. Arch Biochem Biophys. 2001 Dec 1;396(1):111-8. [Article]
  7. Regni C, Tipton PA, Beamer LJ: Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure. 2002 Feb;10(2):269-79. [Article]
  8. Regni C, Naught L, Tipton PA, Beamer LJ: Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure. 2004 Jan;12(1):55-63. [Article]
  9. Regni C, Shackelford GS, Beamer LJ: Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt 8):722-6. Epub 2006 Jul 24. [Article]
  10. Regni C, Schramm AM, Beamer LJ: The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme. J Biol Chem. 2006 Jun 2;281(22):15564-71. Epub 2006 Apr 4. [Article]
  11. Schramm AM, Mehra-Chaudhary R, Furdui CM, Beamer LJ: Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa. Biochemistry. 2008 Sep 2;47(35):9154-62. doi: 10.1021/bi8005219. Epub 2008 Aug 9. [Article]
  12. Sarma AV, Anbanandam A, Kelm A, Mehra-Chaudhary R, Wei Y, Qin P, Lee Y, Berjanskii MV, Mick JA, Beamer LJ, Van Doren SR: Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect. Biochemistry. 2012 Jan 24;51(3):807-19. doi: 10.1021/bi201609n. Epub 2012 Jan 17. [Article]
  13. Lee Y, Mehra-Chaudhary R, Furdui C, Beamer LJ: Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily. FEBS J. 2013 Jun;280(11):2622-32. doi: 10.1111/febs.12249. Epub 2013 Apr 8. [Article]
  14. Lee Y, Villar MT, Artigues A, Beamer LJ: Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase. J Biol Chem. 2014 Feb 21;289(8):4674-82. doi: 10.1074/jbc.M113.532226. Epub 2014 Jan 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02007alpha-D-glucose 6-phosphateexperimentalunknownDetails
DB02843alpha-D-glucose-1-phosphateexperimentalunknownDetails
DB02867D-Mannose 1-phosphateexperimentalunknownDetails
DB02900alpha-D-mannose 6-phosphateexperimentalunknownDetails
DB04522DexfosfoserineexperimentalunknownDetails