C6XZB6 · HEPB_PEDHD
- ProteinHeparin and heparin-sulfate lyase
- GenehepB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids772 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cleaves both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Cleaves heparin at alpha-D-GlcNp2S6S(1->4) alpha-L-IdoAp2S and heparan sulfate at alpha-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp.
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.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 96 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 145 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 148 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 196 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 202 | |||||
Sequence: H | ||||||
Binding site | 205 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 257 | |||||
Sequence: Y | ||||||
Binding site | 261 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 307 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 405 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 406 | |||||
Sequence: H | ||||||
Binding site | 408 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 425 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 429 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 436-437 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: YN | ||||||
Binding site | 451 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 470 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | heparin binding | |
Molecular Function | heparin lyase activity | |
Molecular Function | heparin-sulfate lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | heparin catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameHeparin and heparin-sulfate lyase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter
Accessions
- Primary accessionC6XZB6
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 202 | Loss of catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 257 | Loss of catalytic activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 406 | Loss of catalytic activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 429 | Impaired catalytic activity. | ||||
Sequence: Y → A or F |
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MKRQLYLYVIFVVVELMVFTTKGYS | ||||||
Chain | PRO_5000144613 | 26-772 | Heparin and heparin-sulfate lyase | |||
Sequence: QTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR | ||||||
Glycosylation | 134 | O-linked (Man...) threonine | ||||
Sequence: T |
Keywords
- PTM
PTM databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length772
- Mass (Da)87,626
- Last updated2009-09-22 v1
- Checksum66D9752035421B99
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 505 | in Ref. 1; AA sequence | ||||
Sequence: R → V | ||||||
Sequence conflict | 758 | in Ref. 1; AAB18277 | ||||
Sequence: A → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U27585 EMBL· GenBank· DDBJ | AAB18277.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001681 EMBL· GenBank· DDBJ | ACU04612.1 EMBL· GenBank· DDBJ | Genomic DNA |