ID   HEP1_BACSE              Reviewed;          12 AA.
AC   P83054;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 35.
DE   RecName: Full=Heparin lyase;
DE            EC=4.2.2.7;
DE   AltName: Full=Heparin eliminase;
DE            Short=Heparinase;
DE   Flags: Fragment;
OS   Bacteroides stercoris.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=46506 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=HJ-15;
RX   PubMed=10920269; DOI=10.1093/oxfordjournals.jbchem.a022756;
RA   Kim B.-T., Kim W.-S., Kim Y.S., Linhardt R.J., Kim D.-H.;
RT   "Purification and characterization of a novel heparinase from Bacteroides
RT   stercoris HJ-15.";
RL   J. Biochem. 128:323-328(2000).
CC   -!- FUNCTION: Degrades heparin and heparan sulfate.
CC       {ECO:0000250|UniProtKB:Q05819}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of polysaccharides containing (1->4)-
CC         linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked
CC         2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give
CC         oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl
CC         groups at their non-reducing ends.; EC=4.2.2.7;
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+) ion, lead and some agents that
CC       modify histidine and cysteine residues. Activated by KCl and by
CC       reducing agents, such as dithiothreitol and 2-mercaptoethanol.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.2.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.;
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10920269}.
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DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0047488; F:heparin lyase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heparin-binding; Lyase.
FT   CHAIN           <1..>12
FT                   /note="Heparin lyase"
FT                   /id="PRO_0000083951"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         12
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   12 AA;  1381 MW;  CD9CCD8B98F6D72D CRC64;
     MADEALQHTF FA