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 07-NOV-2018, entry version 64. 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 / CIP 104194 / JCM OS 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3). 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 / CIP 104194 / JCM 7457 / NBRC 12017 / RC NCIMB 9290 / NRRL B-14731 / HIM 762-3; 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 / CIP 104194 / JCM 7457 / NBRC 12017 / RC NCIMB 9290 / NRRL B-14731 / HIM 762-3; 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. {ECO:0000269|PubMed:10747789, CC ECO:0000269|PubMed:8702264}. 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. {ECO:0000269|PubMed:8702264}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=143 uM for heparan sulfate {ECO:0000269|PubMed:10747789}; CC KM=80 uM for heparan sulfate (with recombinant enzyme) CC {ECO:0000269|PubMed:10747789}; CC Note=kcat is 94 sec(-1). Kcat is 78 sec(-1) with recombinant CC enzyme.; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8702264}. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 12 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ACU05988.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; 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 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 SMR; Q59289; -. DR STRING; 485917.Phep_3797; -. DR CAZy; PL12; Polysaccharide Lyase Family 12. DR EnsemblBacteria; ACU05988; ACU05988; Phep_3797. DR KEGG; phe:Phep_3797; -. DR eggNOG; ENOG4108PTS; Bacteria. DR eggNOG; ENOG410XPUT; LUCA. DR HOGENOM; HOG000147638; -. DR KO; K19052; -. DR OrthoDB; POG091H0FGM; -. DR BioCyc; MetaCyc:MONOMER-19212; -. DR Proteomes; UP000000852; Chromosome. DR GO; GO:0042597; C:periplasmic space; TAS:UniProtKB. DR GO; GO:0015021; F:heparin-sulfate lyase activity; IDA:UniProtKB. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IDA:UniProtKB. 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; Complete proteome; Direct protein sequencing; Lyase; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000269|PubMed:8702264}. FT CHAIN 25 659 Heparin-sulfate lyase. FT /FTId=PRO_5000144614. FT ACT_SITE 294 294 Proton acceptor. {ECO:0000255}. FT MUTAGEN 295 295 H->A: Impaired catalytic activity. FT {ECO:0000269|PubMed:10747789}. FT MUTAGEN 510 510 H->A: Impaired catalytic activity. FT {ECO:0000269|PubMed:10747789}. FT CONFLICT 128 129 PV -> LI (in Ref. 1; AA sequence). FT {ECO:0000305}. FT HELIX 32 34 {ECO:0000244|PDB:4MMH}. FT TURN 42 44 {ECO:0000244|PDB:4MMH}. FT HELIX 45 52 {ECO:0000244|PDB:4MMH}. FT HELIX 56 72 {ECO:0000244|PDB:4MMH}. FT STRAND 81 83 {ECO:0000244|PDB:4MMH}. FT STRAND 87 89 {ECO:0000244|PDB:4MMH}. FT HELIX 93 103 {ECO:0000244|PDB:4MMH}. FT TURN 119 122 {ECO:0000244|PDB:4MMH}. FT STRAND 128 130 {ECO:0000244|PDB:4MMH}. FT HELIX 132 138 {ECO:0000244|PDB:4MMH}. FT HELIX 143 154 {ECO:0000244|PDB:4MMH}. FT HELIX 157 173 {ECO:0000244|PDB:4MMH}. FT HELIX 180 186 {ECO:0000244|PDB:4MMH}. FT HELIX 189 206 {ECO:0000244|PDB:4MMH}. FT HELIX 214 232 {ECO:0000244|PDB:4MMH}. FT STRAND 237 239 {ECO:0000244|PDB:4MMH}. FT HELIX 242 255 {ECO:0000244|PDB:4MMH}. FT HELIX 262 280 {ECO:0000244|PDB:4MMH}. FT HELIX 292 310 {ECO:0000244|PDB:4MMH}. FT TURN 311 313 {ECO:0000244|PDB:4MMH}. FT HELIX 315 317 {ECO:0000244|PDB:4MMH}. FT HELIX 320 335 {ECO:0000244|PDB:4MMH}. FT HELIX 354 367 {ECO:0000244|PDB:4MMH}. FT HELIX 372 378 {ECO:0000244|PDB:4MMH}. FT TURN 379 381 {ECO:0000244|PDB:4MMH}. FT STRAND 382 384 {ECO:0000244|PDB:4MMH}. FT STRAND 390 394 {ECO:0000244|PDB:4MMH}. FT TURN 395 398 {ECO:0000244|PDB:4MMH}. FT STRAND 399 404 {ECO:0000244|PDB:4MMH}. FT STRAND 411 416 {ECO:0000244|PDB:4MMH}. FT STRAND 432 436 {ECO:0000244|PDB:4MMH}. FT STRAND 439 442 {ECO:0000244|PDB:4MMH}. FT HELIX 454 463 {ECO:0000244|PDB:4MMH}. FT HELIX 466 468 {ECO:0000244|PDB:4MMH}. FT STRAND 469 474 {ECO:0000244|PDB:4MMH}. FT STRAND 485 490 {ECO:0000244|PDB:4MMH}. FT STRAND 493 505 {ECO:0000244|PDB:4MMH}. FT STRAND 508 517 {ECO:0000244|PDB:4MMH}. FT TURN 518 520 {ECO:0000244|PDB:4MMH}. FT STRAND 521 531 {ECO:0000244|PDB:4MMH}. FT STRAND 534 541 {ECO:0000244|PDB:4MMH}. FT STRAND 549 551 {ECO:0000244|PDB:4MMH}. FT TURN 552 555 {ECO:0000244|PDB:4MMH}. FT STRAND 556 558 {ECO:0000244|PDB:4MMH}. FT STRAND 564 571 {ECO:0000244|PDB:4MMH}. FT STRAND 578 582 {ECO:0000244|PDB:4MMH}. FT STRAND 585 589 {ECO:0000244|PDB:4MMH}. FT STRAND 592 595 {ECO:0000244|PDB:4MMH}. FT STRAND 598 605 {ECO:0000244|PDB:4MMH}. FT STRAND 607 609 {ECO:0000244|PDB:4MMH}. FT STRAND 611 624 {ECO:0000244|PDB:4MMH}. FT STRAND 628 632 {ECO:0000244|PDB:4MMH}. FT TURN 638 641 {ECO:0000244|PDB:4MMH}. FT STRAND 642 649 {ECO:0000244|PDB:4MMH}. FT STRAND 652 659 {ECO:0000244|PDB:4MMH}. 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 //