ID CSLA_PEDHD Reviewed; 700 AA. AC Q59288; C6Y215; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Chondroitinase-AC; DE EC=4.2.2.5; DE AltName: Full=Chondroitin sulfate AC lyase; DE AltName: Full=Chondroitin-AC eliminase; DE AltName: Full=Chondroitin-AC lyase; DE Flags: Precursor; GN Name=cslA; Synonyms=chnAC; OrderedLocusNames=Phep_0786; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3). OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10618199; DOI=10.1128/aem.66.1.29-35.2000; RA Tkalec A.L., Fink D., Blain F., Zhang-Sun G., Laliberte M., Bennett D.C., RA Gu K., Zimmermann J.J.F., Su H.; RT "Isolation and expression in Escherichia coli of cslA and cslB, genes RT coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and RT chondroitinase B, respectively, from Flavobacterium heparinum."; RL Appl. Environ. Microbiol. 66:29-35(2000). RN [2] 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., Pitluck S., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O., RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762- RT 3)."; RL Stand. Genomic Sci. 1:54-62(2009). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=10329169; DOI=10.1006/jmbi.1999.2698; RA Fethiere J., Eggimann B., Cygler M.; RT "Crystal structure of chondroitin AC lyase, a representative of a family of RT glycosaminoglycan degrading enzymes."; RL J. Mol. Biol. 288:635-647(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=11327856; DOI=10.1021/bi0024254; RA Huang W., Boju L., Tkalec A.L., Su H., Yang H.O., Gunay N.S., RA Linhardt R.J., Kim Y.S., Matte A., Cygler M.; RT "Active site of chondroitin AC lyase revealed by the structure of enzyme- RT oligosaccharide complexes and mutagenesis."; RL Biochemistry 40:2359-2372(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=Eliminative degradation of polysaccharides containing 1,4- CC beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to CC disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.; CC EC=4.2.2.5; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit.; CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family. CC {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; U27583; AAC83383.1; -; Genomic_DNA. DR EMBL; CP001681; ACU03008.1; -; Genomic_DNA. DR RefSeq; WP_012780954.1; NZ_AQGK01000003.1. DR PDB; 1CB8; X-ray; 1.90 A; A=23-700. DR PDB; 1HM2; X-ray; 2.00 A; A=1-700. DR PDB; 1HM3; X-ray; 2.10 A; A=1-700. DR PDB; 1HMU; X-ray; 2.00 A; A=1-700. DR PDB; 1HMW; X-ray; 2.30 A; A=1-700. DR PDBsum; 1CB8; -. DR PDBsum; 1HM2; -. DR PDBsum; 1HM3; -. DR PDBsum; 1HMU; -. DR PDBsum; 1HMW; -. DR AlphaFoldDB; Q59288; -. DR SMR; Q59288; -. DR STRING; 485917.Phep_0786; -. DR DrugBank; DB01872; 2-deoxy-2-acetamido-beta-D-galactose-4-sulfate. DR DrugBank; DB03863; 2-O-Methyl-beta-L-fucopyranose. DR DrugBank; DB02305; 4,5-Dehydro-D-Glucuronic Acid. DR DrugBank; DB03569; 4,5-Dehydro-L-Iduronic Acid. DR DrugBank; DB03389; alpha-D-Xylopyranose. DR DrugBank; DB02945; alpha-L-iduronic acid. DR DrugBank; DB03879; alpha-L-methyl-fucose. DR DrugBank; DB03156; beta-D-glucuronic acid. DR DrugBank; DB02186; N-acetyl-beta-D-galactosamine 6-sulfate. DR CAZy; PL8; Polysaccharide Lyase Family 8. DR GlyCosmos; Q59288; 2 sites, No reported glycans. DR KEGG; phe:Phep_0786; -. DR eggNOG; COG5492; Bacteria. DR HOGENOM; CLU_004172_2_1_10; -. DR OrthoDB; 6394136at2; -. DR BioCyc; MetaCyc:MONOMER-15799; -. DR BRENDA; 4.2.2.5; 2286. DR EvolutionaryTrace; Q59288; -. DR Proteomes; UP000000852; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0030341; F:chondroitin AC lyase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd01083; GAG_Lyase; 1. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1. DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1. DR InterPro; IPR008929; Chondroitin_lyas. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR038970; Lyase_8. DR InterPro; IPR011071; Lyase_8-like_C. DR InterPro; IPR012970; Lyase_8_alpha_N. DR InterPro; IPR004103; Lyase_8_C. DR InterPro; IPR003159; Lyase_8_central_dom. DR PANTHER; PTHR38481; HYALURONATE LYASE; 1. DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1. DR Pfam; PF02278; Lyase_8; 1. DR Pfam; PF02884; Lyase_8_C; 1. DR Pfam; PF08124; Lyase_8_N; 1. DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Glycoprotein; Lyase; Metal-binding; KW Reference proteome; Signal. FT SIGNAL 1..22 FT CHAIN 23..700 FT /note="Chondroitinase-AC" FT /id="PRO_0000024927" FT ACT_SITE 225 FT ACT_SITE 234 FT ACT_SITE 288 FT BINDING 405 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 407 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 416 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 417 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT CARBOHYD 328 FT /note="O-linked (Man...) serine" FT CARBOHYD 455 FT /note="O-linked (Man...) serine" FT HELIX 27..39 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 46..56 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 79..93 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 98..101 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 103..119 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 126..130 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 132..143 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 153..161 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 173..189 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 193..204 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 207..217 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 234..249 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 258..270 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 287..291 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 293..296 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 302..311 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 316..326 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 332..335 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 339..343 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 344..347 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 348..353 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 356..361 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 381..384 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 385..394 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 395..397 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:1HM2" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 436..440 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 445..453 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 456..464 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 469..478 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 480..492 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 502..504 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 509..514 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 519..522 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 541..546 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 557..572 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 574..584 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 590..593 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 596..598 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 601..614 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 615..618 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 619..632 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 635..641 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 643..648 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 655..659 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 666..674 FT /evidence="ECO:0007829|PDB:1CB8" FT TURN 675..677 FT /evidence="ECO:0007829|PDB:1CB8" FT STRAND 680..686 FT /evidence="ECO:0007829|PDB:1CB8" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:1CB8" SQ SEQUENCE 700 AA; 79694 MW; C36B608FCAFFC656 CRC64; MKKLFVTCIV FFSILSPALL IAQQTGTAEL IMKRVMLDLK KPLRNMDKVA EKNLNTLQPD GSWKDVPYKD DAMTNWLPNN HLLQLETIIQ AYIEKDSHYY GDDKVFDQIS KAFKYWYDSD PKSRNWWHNE IATPQALGEM LILMRYGKKP LDEALVHKLT ERMKRGEPEK KTGANKTDIA LHYFYRALLT SDEALLSFAV KELFYPVQFV HYEEGLQYDY SYLQHGPQLQ ISSYGAVFIT GVLKLANYVR DTPYALSTEK LAIFSKYYRD SYLKAIRGSY MDFNVEGRGV SRPDILNKKA EKKRLLVAKM IDLKHTEEWA DAIARTDSTV AAGYKIEPYH HQFWNGDYVQ HLRPAYSFNV RMVSKRTRRS ESGNKENLLG RYLSDGATNI QLRGPEYYNI MPVWEWDKIP GITSRDYLTD RPLTKLWGEQ GSNDFAGGVS DGVYGASAYA LDYDSLQAKK AWFFFDKEIV CLGAGINSNA PENITTTLNQ SWLNGPVIST AGKTGRGKIT TFKAQGQFWL LHDAIGYYFP EGANLSLSTQ SQKGNWFHIN NSHSKDEVSG DVFKLWINHG ARPENAQYAY IVLPGINKPE EIKKYNGTAP KVLANTNQLQ AVYHQQLDMV QAIFYTAGKL SVAGIEIETD KPCAVLIKHI NGKQVIWAAD PLQKEKTAVL SIRDLKTGKT NRVKIDFPQQ EFAGATVELK //