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
- Functionsmagnesium ion binding / phosphoglucomutase activity / phosphomannomutase activityProcessesalginic acid biosynthetic process / GDP-mannose biosynthetic process / lipopolysaccharide core region biosynthetic process / O antigen biosynthetic process / pathogenesisComponentscytosol
- 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
Resource Link UniProtKB ID P26276 UniProtKB Entry Name ALGC_PSEAE GenBank Protein ID 150994 GenBank Gene ID M60873 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB02007 alpha-D-glucose 6-phosphate experimental unknown Details DB02843 alpha-D-glucose-1-phosphate experimental unknown Details DB02867 D-Mannose 1-phosphate experimental unknown Details DB02900 alpha-D-mannose 6-phosphate experimental unknown Details DB04522 Dexfosfoserine experimental unknown Details