ID   HEPC_BACSE              Reviewed;         666 AA.
AC   C7EXL6;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Heparin-sulfate lyase;
DE            EC=4.2.2.8;
DE   AltName: Full=Heparin-sulfate eliminase;
DE   AltName: Full=Heparinase III;
DE            Short=HepIII;
DE   AltName: Full=Heparitin-sulfate lyase;
DE   Flags: Precursor;
GN   Name=hepC;
OS   Bacteroides stercoris.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=46506;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-352; CYS-474; CYS-577
RP   AND CYS-624.
RC   STRAIN=HJ-15;
RX   PubMed=19908038; DOI=10.1007/s00253-009-2327-7;
RA   Hyun Y.J., Lee J.H., Kim D.H.;
RT   "Cloning, overexpression, and characterization of recombinant heparinase
RT   III from Bacteroides stercoris HJ-15.";
RL   Appl. Microbiol. Biotechnol. 86:879-890(2010).
CC   -!- FUNCTION: Specifically cleaves heparan sulfate-rich regions of acidic
CC       polysaccharides. Also able to degrade heparin and hyaluronic acid. Does
CC       not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated
CC       glucosamine linkages. Functions in cleaving metazoan heparan sulfate
CC       and providing carbon, nitrogen and sulfate sources for microorganisms.
CC       {ECO:0000269|PubMed:19908038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Elimination of sulfate, appears to act on linkages between N-
CC         acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.;
CC         EC=4.2.2.8; Evidence={ECO:0000269|PubMed:19908038};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=422.75 uM for heparin {ECO:0000269|PubMed:19908038};
CC         KM=88.08 uM for heparan sulfate {ECO:0000269|PubMed:19908038};
CC         Vmax=21.46 umol/min/mg enzyme with heparin as substrate
CC         {ECO:0000269|PubMed:19908038};
CC         Vmax=51.81 umol/min/mg enzyme with heparan sulfate as substrate
CC         {ECO:0000269|PubMed:19908038};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 12 family.
CC       {ECO:0000305}.
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DR   EMBL; GQ304755; ACT66689.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7EXL6; -.
DR   SMR; C7EXL6; -.
DR   STRING; 46506.AA415_01887; -.
DR   CAZy; PL12; Polysaccharide Lyase Family 12.
DR   BRENDA; 4.2.2.8; 7145.
DR   SABIO-RK; C7EXL6; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015021; F:heparin-sulfate lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.50.10.100; -; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR012480; Hepar_II_III.
DR   InterPro; IPR031680; Hepar_II_III_N.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   Pfam; PF16889; Hepar_II_III_N; 1.
DR   SUPFAM; SSF48230; SSF48230; 1.
PE   1: Evidence at protein level;
KW   Lyase; Periplasm; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..666
FT                   /note="Heparin-sulfate lyase"
FT                   /id="PRO_0000424106"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         352
FT                   /note="C->A: Does not affect much catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19908038"
FT   MUTAGEN         474
FT                   /note="C->A: Impaired catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19908038"
FT   MUTAGEN         577
FT                   /note="C->A: Does not affect much catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19908038"
FT   MUTAGEN         624
FT                   /note="C->A: Impaired catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19908038"
SQ   SEQUENCE   666 AA;  77325 MW;  7DF1E1203063869C CRC64;
     MNKTFKYIVL LALACFVGKA NAQELKTEVF SLLNLDYPGL EKVKALHQEG KDADAAKALL
     DYYRARTNVK TPDINLKKVT IGKDEQKMAD EALQHTFFAH KGYQPSFNYG EDIDWRYWPV
     KDNELRWQLH RHKWFTPMGK AYRVSGDEKY AVEWTKQYID WIKKNPLVKV DKKEYEMTGD
     NQLKGDVENA RFAWRPLEVS NRLQDQTSQF QLFLPSPSFT PEFLTEFLVN YHKHAIHILG
     IYSAQGNHLL FEAQRMIYAG AFFPEFKEAA AWRKSGIDIM NREINVQVYN DGGQFELDPH
     YHLAAINIFC KALNIADLYG FRNEFPQEYL DTIEKMIVFY ANVSFPDYTN PCFSDAKLTN
     KKEMLKNYRN WSKMFPKNQF IKYLATDGKE GALPEYLSKG FLKSGFFVFR NSWGTDATQM
     VVKAGPKAFW HCQPDNGTFE LWFNGKNLFP DSGSYVYAGE GEVMEQRNWH RQTCVHNTVT
     LNNKNLDQTE SVTKLWQPEG NVQILVTENP SYKNLKHRRS VFFVDNSYFV IVDEMVGSQK
     GSINLHYQMP KGEIANSRED MTFVTQFEEG SNMKLQCFGP EGMTMKKEPG WCSTAYRKRY
     KRMNVSFNVK KDSEDAVRYI TVICPIKNSA DAPKLSAKFK NKTFNENGLE VEVKVNGKKQ
     SLNYKL