HEPC_BACTN
ID HEPC_BACTN Reviewed; 702 AA.
AC Q89YR9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; OrderedLocusNames=BT_4662;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23011846; DOI=10.1007/s13238-012-2056-z;
RA Dong W., Lu W., McKeehan W.L., Luo Y., Ye S.;
RT "Structural basis of heparan sulfate-specific degradation by heparinase
RT III.";
RL Protein Cell 3:950-961(2012).
CC -!- FUNCTION: Specifically cleaves heparan sulfate-rich regions of acidic
CC polysaccharides. Does not act on N,O-desulfated glucosamine or N-
CC acetyl-O-sulfated glucosamine linkages. Functions in cleaving metazoan
CC heparan sulfate and providing carbon, nitrogen and sulfate sources for
CC microorganisms. {ECO:0000269|PubMed:23011846}.
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:23011846};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.8 uM for heparan sulfate {ECO:0000269|PubMed:23011846};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 12 family.
CC {ECO:0000305}.
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DR EMBL; AE015928; AAO79767.1; -; Genomic_DNA.
DR RefSeq; NP_813573.1; NC_004663.1.
DR RefSeq; WP_008760377.1; NC_004663.1.
DR PDB; 4FNV; X-ray; 1.60 A; A=1-702.
DR PDBsum; 4FNV; -.
DR AlphaFoldDB; Q89YR9; -.
DR SMR; Q89YR9; -.
DR STRING; 226186.BT_4662; -.
DR CAZy; PL12; Polysaccharide Lyase Family 12.
DR PaxDb; Q89YR9; -.
DR PRIDE; Q89YR9; -.
DR EnsemblBacteria; AAO79767; AAO79767; BT_4662.
DR GeneID; 60925835; -.
DR KEGG; bth:BT_4662; -.
DR PATRIC; fig|226186.12.peg.4743; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_013047_1_0_10; -.
DR InParanoid; Q89YR9; -.
DR OMA; GWHKEMS; -.
DR BRENDA; 4.2.2.8; 709.
DR SABIO-RK; Q89YR9; -.
DR Proteomes; UP000001414; Chromosome.
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 3D-structure; Lyase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..702
FT /note="Heparin-sulfate lyase"
FT /id="PRO_0000424105"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:4FNV"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 208..225
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 282..299
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 312..331
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4FNV"
FT TURN 340..345
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 388..395
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4FNV"
FT TURN 427..430
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 532..544
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 547..556
FT /evidence="ECO:0007829|PDB:4FNV"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 560..570
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:4FNV"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:4FNV"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 606..616
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 619..633
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 636..647
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 653..664
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 684..691
FT /evidence="ECO:0007829|PDB:4FNV"
FT STRAND 694..701
FT /evidence="ECO:0007829|PDB:4FNV"
SQ SEQUENCE 702 AA; 79423 MW; A0F23F65E5046B50 CRC64;
MKNIFFICFC ALFAFSGCAD DDDDLLTGGN VDIDLLPDAK PNDVVDPQVF EAINLNYPGL
EKVKEFYEAG EHYYAANALL EYYRTRTNVT NPNLSLINVT ISEAEQAKAD YALVDYRFHV
NNFYEDKETL KPYSVKQDGG INWEYSPKDA SDEYQKQLHR HQWFIPQAKA YRVSGDEKYI
QSWIEVYKNW IENNPKPTTG PNTTSWWQLQ VSTRIGDQVQ LLEYFKNSVN FTPEWLSTFL
VEFAEQADFL VDYPYESGGN ILISQANALA TAGTLMPEFK NAEKWMNTGY QILSEEVQNQ
IMSDGWHKEM SLHYHIGIVA DFYEAMKLAE ANQLSSKLPS DFTEPLRKAA EVVMYFTYPN
YFIKGSDNVV PMFNDSWSRT RNVLKNTNFK QYVEMFPDSE ELKYMQTAGN GGTAQGRTPN
NDMKLFDQAG YYVLRNGWTP ASTVMILSNN KSNDASNSLS AYSHNQPDNG TFELYHNGRN
FFPDSGVCTY YTSGGDNDLR YWFRGIDKHN TLSIGKQNIK KAAGKLLKSE EGATELVVFE
NQGYDNLKHR RAVFYVNKKF FVLVDEGIGN AEGTINLSFN LCEGTASEVV MDTDKNGVHT
AFSNNNNIIV RTFANKAVTC SPFTGRIAYL VDGAYNTRQS YTIDMNKSAD ETARYITVIL
PVNGSTDTSS ISAKFIDSGY SENSASVEVS VNGETHTLSY TL
