C6XZB6 · HEPB_PEDHD

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

  • Elimination of sulfate, appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
    EC:4.2.2.8 (UniProtKB | ENZYME | Rhea)
  • 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.
    EC:4.2.2.7 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site96N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site145N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site148N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site196N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Active site202
Binding site205N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Active site257
Binding site261N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site307N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site405N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Active site406
Binding site408Zn2+ (UniProtKB | ChEBI)
Binding site425Zn2+ (UniProtKB | ChEBI)
Binding site429N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site436-437N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site451Zn2+ (UniProtKB | ChEBI)
Binding site470N-acetyl-D-glucosamine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentperiplasmic space
Molecular Functionheparin binding
Molecular Functionheparin lyase activity
Molecular Functionheparin-sulfate lyase activity
Molecular Functionmetal ion binding
Biological Processheparin catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Heparin and heparin-sulfate lyase
  • Alternative names

Gene names

    • Name
      hepB
    • Ordered locus names
      Phep_2408

Organism names

Accessions

  • Primary accession
    C6XZB6
  • Secondary accessions
    • Q46080

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis202Loss of catalytic activity.
Mutagenesis257Loss of catalytic activity.
Mutagenesis406Loss of catalytic activity.
Mutagenesis429Impaired catalytic activity.

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_500014461326-772Heparin and heparin-sulfate lyase
Glycosylation134O-linked (Man...) threonine

Keywords

PTM databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the polysaccharide lyase 12 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    772
  • Mass (Da)
    87,626
  • Last updated
    2009-09-22 v1
  • Checksum
    66D9752035421B99
MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict505in Ref. 1; AA sequence
Sequence conflict758in Ref. 1; AAB18277

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U27585
EMBL· GenBank· DDBJ
AAB18277.1
EMBL· GenBank· DDBJ
Genomic DNA
CP001681
EMBL· GenBank· DDBJ
ACU04612.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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