ID HEPC_PEDHD Reviewed; 659 AA. AC Q59289; C6XUY0; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-MAR-2014, entry version 41. 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=Phep_3797; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290). OC Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, RP PROTEIN SEQUENCE OF 99-123; 128-142 AND 414-436, FUNCTION, CATALYTIC RP ACTIVITY, AND SUBCELLULAR LOCATION. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290; RX PubMed=8702264; RA Su H., Blain F., Musil R.A., Zimmermann J.J., Gu K., Bennett D.C.; RT "Isolation and expression in Escherichia coli of hepB and hepC, genes RT coding for the glycosaminoglycan-degrading enzymes heparinase II and RT heparinase III, respectively, from Flavobacterium heparinum."; RL Appl. Environ. Microbiol. 62:2723-2734(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 62-68; RP 75-88; 249-264; 383-390; 404-408; 459-464; 468-483; 513-519; 597-605 RP AND 625-631. RX PubMed=8780685; DOI=10.1006/bbrc.1996.1246; RA Godavarti R., Davis M., Venkataraman G., Cooney C., Langer R., RA Sasisekharan R.; RT "Heparinase III from Flavobacterium heparinum: cloning and recombinant RT expression in Escherichia coli."; RL Biochem. Biophys. Res. Commun. 225:751-758(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., RA Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM RT 762-3)."; RL Stand. Genomic Sci. 1:54-62(2009). RN [4] RP IDENTIFICATION. RX PubMed=2211596; RA Nader H.B., Porcionatto M.A., Tersariol I.L., Pinhal M.A., RA Oliveira F.W., Moraes C.T., Dietrich C.P.; RT "Purification and substrate specificity of heparitinase I and RT heparitinase II from Flavobacterium heparinum. Analyses of the heparin RT and heparan sulfate degradation products by 13C NMR spectroscopy."; RL J. Biol. Chem. 265:16807-16813(1990). RN [5] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-295 RP AND HIS-510. RX PubMed=10747789; DOI=10.1021/bi992514k; RA Pojasek K., Shriver Z., Hu Y., Sasisekharan R.; RT "Histidine 295 and histidine 510 are crucial for the enzymatic RT degradation of heparan sulfate by heparinase III."; RL Biochemistry 39:4012-4019(2000). CC -!- FUNCTION: Specifically cleaves heparan sulfate-rich regions of CC acidic polysaccharides. Does not act on N,O-desulfated glucosamine CC or N-acetyl-O-sulfated glucosamine linkages. Functions in cleaving CC metazoan heparan sulfate and providing carbon, nitrogen and CC sulfate sources for microorganisms. CC -!- CATALYTIC ACTIVITY: Elimination of sulfate; appears to act on CC linkages between N-acetyl-D-glucosamine and uronate. Product is an CC unsaturated sugar. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=143 uM for heparan sulfate; CC KM=80 uM for heparan sulfate (with recombinant enzyme); CC Note=kcat is 94 sec(-1). Kcat is 78 sec(-1) with recombinant CC enzyme; CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 12 family. CC -!- SEQUENCE CAUTION: CC Sequence=ACU05988.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U27586; AAB18278.1; -; Genomic_DNA. DR EMBL; CP001681; ACU05988.1; ALT_INIT; Genomic_DNA. DR PIR; JC4910; JC4910. DR RefSeq; YP_003094050.1; NC_013061.1. DR PDB; 4MMH; X-ray; 2.20 A; A=25-659. DR PDB; 4MMI; X-ray; 2.40 A; A=25-659. DR PDBsum; 4MMH; -. DR PDBsum; 4MMI; -. DR STRING; 485917.Phep_3797; -. DR CAZy; PL12; Polysaccharide Lyase Family 12. DR GeneID; 8254931; -. DR KEGG; phe:Phep_3797; -. DR PATRIC; 22884831; VBIPedHep98714_3864. DR OrthoDB; EOG690M98; -. DR ProtClustDB; CLSK246672; -. DR BioCyc; PHEP485917:GHL9-3848-MONOMER; -. DR GO; GO:0042597; C:periplasmic space; TAS:UniProtKB. DR GO; GO:0015021; F:heparin-sulfate lyase activity; IDA:UniProtKB. DR GO; GO:0045135; F:poly(beta-D-mannuronate) lyase activity; IEA:InterPro. DR GO; GO:0042122; P:alginic acid catabolic process; IEA:InterPro. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IDA:UniProtKB. DR Gene3D; 1.50.10.110; -; 1. DR InterPro; IPR008397; Alginate_lyase_dom. DR InterPro; IPR008929; Chondroitin_lyas. DR InterPro; IPR012480; Hepar_II_III. DR Pfam; PF07940; Hepar_II_III; 1. DR SUPFAM; SSF48230; SSF48230; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Lyase; KW Periplasm; Signal. FT SIGNAL 1 24 FT CHAIN 25 659 Heparin-sulfate lyase. FT /FTId=PRO_5000144614. FT ACT_SITE 294 294 Proton acceptor (Potential). FT MUTAGEN 295 295 H->A: Impaired catalytic activity. FT MUTAGEN 510 510 H->A: Impaired catalytic activity. FT CONFLICT 128 129 PV -> LI (in Ref. 1; AA sequence). SQ SEQUENCE 659 AA; 75807 MW; B73EDF10A1256FE2 CRC64; MTTKIFKRII VFAVIALSSG NILAQSSSIT RKDFDHINLE YSGLEKVNKA VAAGNYDDAA KALLAYYREK SKAREPDFSN AEKPADIRQP IDKVTREMAD KALVHQFQPH KGYGYFDYGK DINWQMWPVK DNEVRWQLHR VKWWQAMALV YHATGDEKYA REWVYQYSDW ARKNPLGLSQ DNDKFVWRPL EVSDRVQSLP PTFSLFVNSP AFTPAFLMEF LNSYHQQADY LSTHYAEQGN HRLFEAQRNL FAGVSFPEFK DSPRWRQTGI SVLNTEIKKQ VYADGMQFEL SPIYHVAAID IFLKAYGSAK RVNLEKEFPQ SYVQTVENMI MALISISLPD YNTPMFGDSW ITDKNFRMAQ FASWARVFPA NQAIKYFATD GKQGKAPNFL SKALSNAGFY TFRSGWDKNA TVMVLKASPP GEFHAQPDNG TFELFIKGRN FTPDAGVFVY SGDEAIMKLR NWYRQTRIHS TLTLDNQNMV ITKARQNKWE TGNNLDVLTY TNPSYPNLDH QRSVLFINKK YFLVIDRAIG EATGNLGVHW QLKEDSNPVF DKTKNRVYTT YRDGNNLMIQ SLNADRTSLN EEEGKVSYVY NKELKRPAFV FEKPKKNAGT QNFVSIVYPY DGQKAPEISI RENKGNDFEK GKLNLTLTIN GKQQLVLVP //