ID   HEP1_PEDHE              Reviewed;         384 AA.
AC   Q05819;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Heparin lyase I;
DE            Short=Heparinase I;
DE            EC=4.2.2.7;
DE   Flags: Precursor;
OS   Pedobacter heparinus (Flavobacterium heparinum).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=984;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8475114; DOI=10.1073/pnas.90.8.3660;
RA   Sasisekharan R., Bulmer M., Moremen K.W., Cooney C.L., Langer R.;
RT   "Cloning and expression of heparinase I gene from Flavobacterium
RT   heparinum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:3660-3664(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-27, AND CHARACTERIZATION.
RX   PubMed=8615834; DOI=10.1042/bj3150589;
RA   Ernst S., Venkataraman G., Winkler S., Godavarti R., Langer R.,
RA   Cooney C.L., Sasisekharan R.;
RT   "Expression in Escherichia coli, purification and characterization of
RT   heparinase I from Flavobacterium heparinum.";
RL   Biochem. J. 315:589-597(1996).
RN   [3]
RP   GLYCOSYLATION AT SER-39, STRUCTURE OF CARBOHYDRATE, AND MASS SPECTROMETRY.
RA   Huang L., van Halbeek H., Eggimann B., Zimmermannn J.;
RT   "Structural characterization of the novel O-linked carbohydrate structure
RT   of Flavobacterium heparinum heparinase I.";
RL   Glycobiology 5:712-712(1995).
CC   -!- FUNCTION: Degrades heparin and heparan sulfate. Also implicated in the
CC       release of heparin-bound growth factors from the extracellular matrix.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=33 uM for native heparinase;
CC         KM=47 uM for recombinant heparinase;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By heparin.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MASS SPECTROMETRY: Mass=42502; Mass_error=2.8; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.3};
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DR   EMBL; L12534; AAA24920.1; -; Genomic_DNA.
DR   PIR; A47479; A47479.
DR   AlphaFoldDB; Q05819; -.
DR   SMR; Q05819; -.
DR   CAZy; PL13; Polysaccharide Lyase Family 13.
DR   BioCyc; MetaCyc:MON-19213; -.
DR   BRENDA; 4.2.2.8; 2286.
DR   SABIO-RK; Q05819; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0047488; F:heparin lyase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR025975; Polysacc_lyase.
DR   Pfam; PF14099; Polysacc_lyase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Heparin-binding; Lyase; Periplasm;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:8615834"
FT   CHAIN           22..384
FT                   /note="Heparin lyase I"
FT                   /id="PRO_0000021411"
FT   MOD_RES         22
FT                   /note="Blocked amino end (Gln)"
FT   CARBOHYD        39
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|Ref.3"
SQ   SEQUENCE   384 AA;  43807 MW;  B082E0B571DEA699 CRC64;
     MKKQILYLIV LQQLFLCSAY AQQKKSGNIP YRVNVQADSA KQKAIIDNKW VAVGINKPYA
     LQYDDKLRFN GKPSYRFELK AEDNSLEGYA AGETKGRTEL SYSYATTNDF KKFPPSVYQN
     AQKLKTVYHY GKGICEQGSS RSYTFSVYIP SSFPDNATTI FAQWHGAPSR TLVATPEGEI
     KTLSIEEFLA LYDRMIFKKN IAHDKVEKKD KDGKITYVAG KPNGWKVEQG GYPTLAFGFS
     KGYFYIKANS DRQWLTDKAD RNNANPENSE VMKPYSSEYK TSTIAYKMPF AQFPKDCWIT
     FDVAIDWTKY GKEANTILKP GKLDVMMTYT KNKKPQKAHI VNQQEILIGR NDDDGYYFKF
     GIYRVGNSTV PVTYNLSGYS ETAR