CSLB_PEDHD
ID CSLB_PEDHD Reviewed; 506 AA.
AC Q46079; C6Y218;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Chondroitinase-B;
DE EC=4.2.2.19;
DE AltName: Full=Chondroitin sulfate B lyase;
DE AltName: Full=Chondroitin-B eliminase;
DE AltName: Full=Chondroitin-B lyase;
DE Flags: Precursor;
GN Name=cslB; OrderedLocusNames=Phep_0789;
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 CHARACTERIZATION, AND MUTAGENESIS OF LYS-250; HIS-272; GLU-333; ARG-363 AND
RP ARG-364.
RX PubMed=12063249; DOI=10.1074/jbc.m201552200;
RA Pojasek K., Raman R., Kiley P., Venkataraman G., Sasisekharan R.;
RT "Biochemical characterization of the chondroitinase B active site.";
RL J. Biol. Chem. 277:31179-31186(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
RP GLN-26.
RX PubMed=10600383; DOI=10.1006/jmbi.1999.3292;
RA Huang W., Matte A., Li Y., Kim Y.S., Linhardt R.J., Su H., Cygler M.;
RT "Crystal structure of chondroitinase B from Flavobacterium heparinum and
RT its complex with a disaccharide product at 1.7 A resolution.";
RL J. Mol. Biol. 294:1257-1269(1999).
RN [5]
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 -!- FUNCTION: Cleaves the glycosaminoglycan, dermatan sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of dermatan sulfate containing (1->4)-
CC beta-D-hexosaminyl and (1->3)-beta-D-glucurosonyl or (1->3)-alpha-L-
CC iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-
CC 4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate
CC disaccharide (DeltaUA-GalNAc-4S).; EC=4.2.2.19;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
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DR EMBL; U27584; AAC83384.1; -; Genomic_DNA.
DR EMBL; CP001681; ACU03011.1; -; Genomic_DNA.
DR RefSeq; WP_012780957.1; NZ_AQGK01000003.1.
DR PDB; 1DBG; X-ray; 1.70 A; A=1-506.
DR PDB; 1DBO; X-ray; 1.70 A; A=1-506.
DR PDB; 1OFL; X-ray; 1.70 A; A=27-506.
DR PDB; 1OFM; X-ray; 1.80 A; A=27-506.
DR PDBsum; 1DBG; -.
DR PDBsum; 1DBO; -.
DR PDBsum; 1OFL; -.
DR PDBsum; 1OFM; -.
DR AlphaFoldDB; Q46079; -.
DR SMR; Q46079; -.
DR STRING; 485917.Phep_0789; -.
DR DrugBank; DB04492; 2-(acetylamino)-2-deoxy-4-O-sulfo-alpha-D-galactopyranose.
DR DrugBank; DB01872; 2-deoxy-2-acetamido-beta-D-galactose-4-sulfate.
DR DrugBank; DB04515; 2-O-methyl-alpha-L-fucopyranose.
DR DrugBank; DB03863; 2-O-Methyl-beta-L-fucopyranose.
DR DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; PL6; Polysaccharide Lyase Family 6.
DR EnsemblBacteria; ACU03011; ACU03011; Phep_0789.
DR KEGG; phe:Phep_0789; -.
DR eggNOG; COG3420; Bacteria.
DR HOGENOM; CLU_531940_0_0_10; -.
DR OMA; RNDIGRC; -.
DR OrthoDB; 1055328at2; -.
DR BioCyc; MetaCyc:MON-15800; -.
DR BRENDA; 4.2.2.19; 2286.
DR SABIO-RK; Q46079; -.
DR EvolutionaryTrace; Q46079; -.
DR Proteomes; UP000000852; Chromosome.
DR GO; GO:0033999; F:chondroitin B lyase activity; IEA:UniProtKB-EC.
DR CDD; cd14251; PL-6; 1.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039513; PL-6.
DR Pfam; PF14592; Chondroitinas_B; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Lyase; Pyrrolidone carboxylic acid;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT CHAIN 26..506
FT /note="Chondroitinase-B"
FT /id="PRO_0000024928"
FT ACT_SITE 250
FT ACT_SITE 272
FT ACT_SITE 333
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000305|PubMed:10600383"
FT CARBOHYD 234
FT /note="O-linked (Man...) serine"
FT MUTAGEN 250
FT /note="K->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12063249"
FT MUTAGEN 272
FT /note="H->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:12063249"
FT MUTAGEN 333
FT /note="E->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:12063249"
FT MUTAGEN 363
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:12063249"
FT MUTAGEN 364
FT /note="R->A: Partial loss of activity and altered product
FT profile."
FT /evidence="ECO:0000269|PubMed:12063249"
FT CONFLICT 195
FT /note="A -> G (in Ref. 1; AAC83384)"
FT /evidence="ECO:0000305"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1DBG"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1DBG"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:1DBG"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:1DBG"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:1DBG"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1DBO"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:1DBG"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1DBG"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:1DBG"
FT HELIX 490..502
FT /evidence="ECO:0007829|PDB:1DBG"
SQ SEQUENCE 506 AA; 56337 MW; 454B93EC0AACD2A3 CRC64;
MKMLNKLAGY LLPIMVLLNV APCLGQVVAS NETLYQVVKE VKPGGLVQIA DGTYKDVQLI
VSNSGKSGLP ITIKALNPGK VFFTGDAKVE LRGEHLILEG IWFKDGNRAI QAWKSHGPGL
VAIYGSYNRI TACVFDCFDE ANSAYITTSL TEDGKVPQHC RIDHCSFTDK ITFDQVINLN
NTARAIKDGS VGGPAMYHRV DHCFFSNPQK PGNAGGGIRI GYYRNDIGRC LVDSNLFMRQ
DSEAEIITSK SQENVYYGNT YLNCQGTMNF RHGDHQVAIN NFYIGNDQRF GYGGMFVWGS
RHVIACNYFE LSETIKSRGN AALYLNPGAM ASEHALAFDM LIANNAFINV NGYAIHFNPL
DERRKEYCAA NRLKFETPHQ LMLKGNLFFK DKPYVYPFFK DDYFIAGKNS WTGNVALGVE
KGIPVNISAN RSAYKPVKIK DIQPIEGIAL DLNALISKGI TGKPLSWDEV RPYWLKEMPG
TYALTARLSA DRAAKFKAVI KRNKEH
