Hmdb loader
Identification
HMDB Protein ID HMDBP12358
Secondary Accession Numbers None
Name Pullulanase A
Synonyms
  1. Alpha-dextrin endo-1,6-alpha-glucosidase
  2. Pullulan 6-glucanohydrolase
Gene Name SPUA
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes the alpha-1,6-branchpoints of glycogen (PubMed:20497336, PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran (PubMed:20497336). Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose) (PubMed:17187076).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
pathogenesis
alpha-glucan biosynthetic process
Cellular Component
cell surface
extracellular region
cell wall
Molecular Function
calcium ion binding
polysaccharide binding
amylopectin binding
glycogen binding
limit dextrinase activity
pullulan binding
pullulanase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 1280
Molecular Weight 142618.275
Theoretical pI 5.694
Pfam Domain Function
Signals
  • 1-44;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID A0A0H2UNG0
UniProtKB/Swiss-Prot Entry Name PULA_STRPN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Tettelin H, Nelson KE, Paulsen IT, Eisen JA, Read TD, Peterson S, Heidelberg J, DeBoy RT, Haft DH, Dodson RJ, Durkin AS, Gwinn M, Kolonay JF, Nelson WC, Peterson JD, Umayam LA, White O, Salzberg SL, Lewis MR, Radune D, Holtzapple E, Khouri H, Wolf AM, Utterback TR, Hansen CL, McDonald LA, Feldblyum TV, Angiuoli S, Dickinson T, Hickey EK, Holt IE, Loftus BJ, Yang F, Smith HO, Venter JC, Dougherty BA, Morrison DA, Hollingshead SK, Fraser CM: Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science. 2001 Jul 20;293(5529):498-506. doi: 10.1126/science.1061217. [PubMed:11463916 ]
  2. Abbott DW, Higgins MA, Hyrnuik S, Pluvinage B, Lammerts van Bueren A, Boraston AB: The molecular basis of glycogen breakdown and transport in Streptococcus pneumoniae. Mol Microbiol. 2010 Jul 1;77(1):183-99. doi: 10.1111/j.1365-2958.2010.07199.x. Epub 2010 May 19. [PubMed:20497336 ]
  3. van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB: Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol. 2007 Jan;14(1):76-84. doi: 10.1038/nsmb1187. Epub 2006 Dec 24. [PubMed:17187076 ]
  4. Lammerts van Bueren A, Ficko-Blean E, Pluvinage B, Hehemann JH, Higgins MA, Deng L, Ogunniyi AD, Stroeher UH, El Warry N, Burke RD, Czjzek M, Paton JC, Vocadlo DJ, Boraston AB: The conformation and function of a multimodular glycogen-degrading pneumococcal virulence factor. Structure. 2011 May 11;19(5):640-51. doi: 10.1016/j.str.2011.03.001. [PubMed:21565699 ]