Reviewed,
UniProtKB/Swiss-Prot Q05819 (HEP1_PEDHE)
Last modified
June 16, 2009.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heparin lyase I Short name=Heparinase I EC=4.2.2.7 |
| Organism | Pedobacter heparinus (Flavobacterium heparinum) |
| Taxonomic identifier | 984 [NCBI] |
| Taxonomic lineage | Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Sphingobacteriaceae › Pedobacter |
Protein attributes
| Sequence length | 384 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Degrades heparin and heparan sulfate. Also implicated in the release of heparin-bound growth factors from the extracellular matrix. |
| Catalytic activity | Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Induction | By heparin. |
| Post-translational modification | The N-terminus is blocked. |
| biophysicochemical properties | Kinetic parameters: KM=33 µM for native heparinase KM=47 µM for recombinant heparinase |
| Mass spectrometry | Molecular mass is 42502±2.8 Da from positions 22 - 384. Determined by ESI. Ref.3 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Heparin-binding |
| Molecular function | Lyase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | heparin binding Inferred from electronic annotation. Source: UniProtKB-KW heparin lyase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning and expression of heparinase I gene from Flavobacterium heparinum." Sasisekharan R., Bulmer M., Moremen K.W., Cooney C.L., Langer R. Proc. Natl. Acad. Sci. U.S.A. 90:3660-3664(1993) [PubMed: 8475114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. |
| [2] | "Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum." Ernst S., Venkataraman G., Winkler S., Godavarti R., Langer R., Cooney C.L., Sasisekharan R. Biochem. J. 315:589-597(1996) [PubMed: 8615834] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-27, CHARACTERIZATION. |
| [3] | "Structural characterization of the novel O-linked carbohydrate structure of Flavobacterium heparinum heparinase I." Huang L., van Halbeek H., Eggimann B., Zimmermannn J. Glycobiology 5:712-712(1995) Cited for: GLYCOSYLATION AT SER-39, STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY. |
Cross-references
Entry information
| Entry name | HEP1_PEDHE | ||||||||
| Accession | Primary (citable) accession number: Q05819 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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