CSLA_PEDHD
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 03-AUG-2022, entry version 118.
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; Bacteroidetes; 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 / NCIMB
RC 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}.
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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 EnsemblBacteria; ACU03008; ACU03008; Phep_0786.
DR KEGG; phe:Phep_0786; -.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_004172_2_1_10; -.
DR OMA; RYYQDET; -.
DR OrthoDB; 941406at2; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.70.98.10; -; 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; PTHR38481; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 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
