ProGP106 (Heparin lyase I or Heparinase I)
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ProGP ID | ProGP106 (Heparin lyase I or Heparinase I) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Pedobacter heparinus (Flavobacterium heparinum) |
Domain | Bacteria |
Classification | Phylum : Bacteroides Class : Sphingobacteriia Orders : Sphingobaccteriales Family : Sphingobacteriaceae Genus : Pedobacter Species : heparinus |
Taxonomic ID (NCBI) | 984 |
Genome Information | |
GenBank | CP001681.1 |
EMBL | L12534 |
Organism Additional Information | Pedobacter heparinus is a Gram-negative, nonpathogenic soil organism. |
Gene Information | |
Gene Name | hep A |
NCBI Gene ID | 8251559 |
GenBank Gene Sequence | NC_013061 |
Protein Information | |
Protein Name | Heparin lyase I or Heparinase I |
UniProtKB/SwissProt ID | Q05819 |
NCBI RefSeq | WP_012780649.1 |
EMBL-CDS | AAA24920.1 |
UniProtKB Sequence | >sp|Q05819|HEP1_PEDHE Heparin lyase I OS=Pedobacter heparinus PE=1 SV=1 MKKQILYLIVLQQLFLCSAYAQQKKSGNIPYRVNVQADSAKQKAIIDNKWVAVGINKPYA LQYDDKLRFNGKPSYRFELKAEDNSLEGYAAGETKGRTELSYSYATTNDFKKFPPSVYQN AQKLKTVYHYGKGICEQGSSRSYTFSVYIPSSFPDNATTIFAQWHGAPSRTLVATPEGEI KTLSIEEFLALYDRMIFKKNIAHDKVEKKDKDGKITYVAGKPNGWKVEQGGYPTLAFGFS KGYFYIKANSDRQWLTDKADRNNANPENSEVMKPYSSEYKTSTIAYKMPFAQFPKDCWIT FDVAIDWTKYGKEANTILKPGKLDVMMTYTKNKKPQKAHIVNQQEILIGRNDDDGYYFKF GIYRVGNSTVPVTYNLSGYSETAR |
Sequence length | 384 AA |
Subcellular Location | Periplasm |
Function | GAG lyase. EC= 4.2.2.7. It has been assigned to the polysaccharide lyase family PL13. Degrades heparin and heparan sulfate. Also implicated in the release of heparin-bound growth factors from the extracellular matrix. |
Glycosylation Status | |
Glycosylation Type | O- (Ser) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | S39 |
Experimentally Validated Glycosite(s ) in Mature Protein | S39 |
Glycosite(s) Annotated Protein Sequence | >sp|Q05819|HEP1_PEDHE Heparin lyase I OS=Pedobacter heparinus PE=1 SV=1 MKKQILYLIVLQQLFLCSAYAQQKKSGNIPYRVNVQADS*(39)AKQKAIIDNKWVAVGINKPYA LQYDDKLRFNGKPSYRFELKAEDNSLEGYAAGETKGRTELSYSYATTNDFKKFPPSVYQN AQKLKTVYHYGKGICEQGSSRSYTFSVYIPSSFPDNATTIFAQWHGAPSRTLVATPEGEI KTLSIEEFLALYDRMIFKKNIAHDKVEKKDKDGKITYVAGKPNGWKVEQGGYPTLAFGFS KGYFYIKANSDRQWLTDKADRNNANPENSEVMKPYSSEYKTSTIAYKMPFAQFPKDCWIT FDVAIDWTKYGKEANTILKPGKLDVMMTYTKNKKPQKAHIVNQQEILIGRNDDDGYYFKF GIYRVGNSTVPVTYNLSGYSETAR |
Sequence Around Glycosites (21 AA) | IPYRVNVQADSAKQKAIIDNK |
Technique(s) used for Glycosylation Detection | Presence of multiple isoforms in the RPHPLC (reverse-phase high pressure liquid chromatography) profile, and mass excess (approx. 1.1 kDa) detected using mass spectrometry. |
Technique(s) used for Glycosylated Residue(s) Detection | NMR and mass spectrometry |
Glycan Information | |
Glycan Annotation | Linkage: Man-Ser. Branched heptasaccharide is: galactose-β(1–4)[galactose-α(1–3)](2-O-Me)fucose-β(1–4)xylose-β (1–4)glucuronic acid-α(1–2)[rhamnose-α(1–4)]mannose-α(1-O)Ser. |
GlyTouCan | G07644FE |
Technique(s) used for Glycan Identification | Combination of enzymatic digestion, NMR and mass spectroscopy. |
Protein Glycosylation linked (PGL) gene(s) | |
Characterized Accessory Gene(s) | Information currently not available with us. |
Additional Comment | Sequon features: Asp-Ser consensus sequon is found in this protein. Post translational modification was detected as early as 1993 but the glycosylation was confirmed in 1995. |
Literature | |
Year of Identification | 1995 |
Year of Identification Month Wise | 1995.05 |
Year of Validation | 1995 |
Reference | Shaya, D., Tocilj, A., Li, Y., Myette, J., Venkataraman, G., Sasisekharan, R. and Cygler, M., 2006. Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product. Journal of Biological Chemistry, 281(22), pp.15525-15535. |
Corresponding Author | Miroslaw Cygler |
Contact | Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. |
Reference | Godavarti, R. and Sasisekharan, R., 1996. A Comparative Analysis of the Primary Sequences and Characteristics of Heparinases I, II, and III fromFlavobacterium heparinum. Biochemical and biophysical research communications, 229(3), pp.770-777. |
Corresponding Author | R Godavarti |
Contact | Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA. |
Reference | Huang, L., Van Halbeek, H., Eggimann, B. and Zimmermann, J., 1995. Structural characterization of the novel O-linked carbohydrate structure of Flavobacterium heparinum heparinase I. Glycobiology, 5, p.712. |
Reference | Sasisekharan, R., Bulmer, M., Moremen, K.W., Cooney, C.L. and Langer, R., 1993. Cloning and expression of heparinase I gene from Flavobacterium heparinum. Proceedings of the National Academy of Sciences, 90(8), pp.3660-3664. |
Corresponding Author | R Sasisekharan |
Contact | Division of Medical Sciences, Harvard Medical School, Boston, MA 02115. |