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Chondroitinase-B (EC 4.2.2.19) (Chondroitin sulfate B lyase) (Chondroitin-B eliminase) (Chondroitin-B lyase)

 CSLB_PEDHD              Reviewed;         506 AA.
Q46079; C6Y218;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 2.
23-MAY-2018, entry version 100.
RecName: Full=Chondroitinase-B;
EC=4.2.2.19;
AltName: Full=Chondroitin sulfate B lyase;
AltName: Full=Chondroitin-B eliminase;
AltName: Full=Chondroitin-B lyase;
Flags: Precursor;
Name=cslB; OrderedLocusNames=Phep_0789;
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM
7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Pedobacter.
NCBI_TaxID=485917;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10618199; DOI=10.1128/AEM.66.1.29-35.2000;
Tkalec A.L., Fink D., Blain F., Zhang-Sun G., Laliberte M.,
Bennett D.C., Gu K., Zimmermann J.J.F., Su H.;
"Isolation and expression in Escherichia coli of cslA and cslB, genes
coding for the chondroitin sulfate-degrading enzymes chondroitinase AC
and chondroitinase B, respectively, from Flavobacterium heparinum.";
Appl. Environ. Microbiol. 66:29-35(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
NCIMB 9290 / NRRL B-14731 / HIM 762-3;
PubMed=21304637; DOI=10.4056/sigs.22138;
Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M.,
Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
Kyrpides N.C., Klenk H.P., Detter J.C.;
"Complete genome sequence of Pedobacter heparinus type strain (HIM
762-3).";
Stand. Genomic Sci. 1:54-62(2009).
[3]
CHARACTERIZATION, AND MUTAGENESIS OF LYS-250; HIS-272; GLU-333;
ARG-363 AND ARG-364.
PubMed=12063249; DOI=10.1074/jbc.M201552200;
Pojasek K., Raman R., Kiley P., Venkataraman G., Sasisekharan R.;
"Biochemical characterization of the chondroitinase B active site.";
J. Biol. Chem. 277:31179-31186(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND PYROGLUTAMATE FORMATION AT
GLN-26.
PubMed=10600383; DOI=10.1006/jmbi.1999.3292;
Huang W., Matte A., Li Y., Kim Y.S., Linhardt R.J., Su H., Cygler M.;
"Crystal structure of chondroitinase B from Flavobacterium heparinum
and its complex with a disaccharide product at 1.7 A resolution.";
J. Mol. Biol. 294:1257-1269(1999).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11327856; DOI=10.1021/bi0024254;
Huang W., Boju L., Tkalec A.L., Su H., Yang H.O., Gunay N.S.,
Linhardt R.J., Kim Y.S., Matte A., Cygler M.;
"Active site of chondroitin AC lyase revealed by the structure of
enzyme-oligosaccharide complexes and mutagenesis.";
Biochemistry 40:2359-2372(2001).
-!- FUNCTION: Cleaves the glycosaminoglycan, dermatan sulfate.
-!- CATALYTIC ACTIVITY: Eliminative cleavage of dermatan sulfate
containing (1->4)-beta-D-hexosaminyl and (1->3)-beta-D-
glucurosonyl or (1->3)-alpha-L-iduronosyl linkages to
disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups
to yield a 4,5-unsaturated dermatan-sulfate disaccharide (Delta-
UA-GalNAc-4S).
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U27584; AAC83384.1; -; Genomic_DNA.
EMBL; CP001681; ACU03011.1; -; Genomic_DNA.
RefSeq; WP_012780957.1; NZ_AQGK01000003.1.
PDB; 1DBG; X-ray; 1.70 A; A=1-506.
PDB; 1DBO; X-ray; 1.70 A; A=1-506.
PDB; 1OFL; X-ray; 1.70 A; A=27-506.
PDB; 1OFM; X-ray; 1.80 A; A=27-506.
PDBsum; 1DBG; -.
PDBsum; 1DBO; -.
PDBsum; 1OFL; -.
PDBsum; 1OFM; -.
SMR; Q46079; -.
STRING; 485917.Phep_0789; -.
DrugBank; DB04492; 2-(Acetylamino)-2-Deoxy-4-O-Sulfo-Alpha-D-Galactopyranose.
DrugBank; DB03863; 2-O-Methyl Fucose.
DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid.
DrugBank; DB04515; 6-Deoxy-2-O-Methyl-Alpha-L-Galactopyranose.
DrugBank; DB01872; Acetylgalactosamine-4-Sulfate.
DrugBank; DB03389; alpha-D-Xylopyranose.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB03088; Pyroglutamic Acid.
CAZy; PL6; Polysaccharide Lyase Family 6.
PRIDE; Q46079; -.
EnsemblBacteria; ACU03011; ACU03011; Phep_0789.
KEGG; phe:Phep_0789; -.
KO; K19053; -.
OMA; RNDIGRC; -.
OrthoDB; POG091H03H8; -.
BioCyc; MetaCyc:MONOMER-15800; -.
BioCyc; PHEP485917:G1GFH-804-MONOMER; -.
BRENDA; 4.2.2.19; 2286.
SABIO-RK; Q46079; -.
EvolutionaryTrace; Q46079; -.
Proteomes; UP000000852; Chromosome.
GO; GO:0033999; F:chondroitin B lyase activity; IEA:UniProtKB-EC.
Gene3D; 2.160.20.10; -; 1.
InterPro; IPR012334; Pectin_lyas_fold.
InterPro; IPR011050; Pectin_lyase_fold/virulence.
SUPFAM; SSF51126; SSF51126; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Glycoprotein; Lyase;
Pyrrolidone carboxylic acid; Reference proteome; Signal.
SIGNAL 1 25
CHAIN 26 506 Chondroitinase-B.
/FTId=PRO_0000024928.
ACT_SITE 250 250
ACT_SITE 272 272
ACT_SITE 333 333
MOD_RES 26 26 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:10600383}.
CARBOHYD 234 234 O-linked (Man...) serine.
MUTAGEN 250 250 K->A: Complete loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 272 272 H->A: Partial loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 333 333 E->A: Partial loss of activity.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 363 363 R->A: No effect.
{ECO:0000269|PubMed:12063249}.
MUTAGEN 364 364 R->A: Partial loss of activity and
altered product profile.
{ECO:0000269|PubMed:12063249}.
CONFLICT 195 195 A -> G (in Ref. 1; AAC83384).
{ECO:0000305}.
HELIX 31 40 {ECO:0000244|PDB:1DBG}.
STRAND 46 49 {ECO:0000244|PDB:1DBG}.
STRAND 51 55 {ECO:0000244|PDB:1DBG}.
STRAND 58 61 {ECO:0000244|PDB:1DBG}.
STRAND 71 77 {ECO:0000244|PDB:1DBG}.
STRAND 80 86 {ECO:0000244|PDB:1DBG}.
STRAND 88 91 {ECO:0000244|PDB:1DBG}.
STRAND 93 100 {ECO:0000244|PDB:1DBG}.
STRAND 102 106 {ECO:0000244|PDB:1DBG}.
TURN 110 112 {ECO:0000244|PDB:1DBG}.
STRAND 120 123 {ECO:0000244|PDB:1DBG}.
STRAND 125 127 {ECO:0000244|PDB:1DBG}.
STRAND 129 132 {ECO:0000244|PDB:1DBG}.
STRAND 134 137 {ECO:0000244|PDB:1DBG}.
STRAND 145 148 {ECO:0000244|PDB:1DBG}.
STRAND 161 164 {ECO:0000244|PDB:1DBG}.
STRAND 166 168 {ECO:0000244|PDB:1DBG}.
STRAND 172 174 {ECO:0000244|PDB:1DBG}.
STRAND 176 179 {ECO:0000244|PDB:1DBG}.
STRAND 199 202 {ECO:0000244|PDB:1DBG}.
STRAND 204 207 {ECO:0000244|PDB:1DBG}.
STRAND 211 213 {ECO:0000244|PDB:1DBG}.
STRAND 217 220 {ECO:0000244|PDB:1DBG}.
STRAND 231 234 {ECO:0000244|PDB:1DBG}.
STRAND 236 240 {ECO:0000244|PDB:1DBG}.
STRAND 242 253 {ECO:0000244|PDB:1DBG}.
STRAND 255 258 {ECO:0000244|PDB:1DBG}.
STRAND 260 263 {ECO:0000244|PDB:1DBG}.
STRAND 265 272 {ECO:0000244|PDB:1DBG}.
STRAND 277 280 {ECO:0000244|PDB:1DBG}.
STRAND 282 285 {ECO:0000244|PDB:1DBG}.
STRAND 287 290 {ECO:0000244|PDB:1DBG}.
STRAND 295 297 {ECO:0000244|PDB:1DBG}.
STRAND 299 301 {ECO:0000244|PDB:1DBG}.
STRAND 303 306 {ECO:0000244|PDB:1DBG}.
STRAND 308 314 {ECO:0000244|PDB:1DBG}.
TURN 316 319 {ECO:0000244|PDB:1DBG}.
STRAND 320 325 {ECO:0000244|PDB:1DBG}.
STRAND 338 344 {ECO:0000244|PDB:1DBG}.
STRAND 346 349 {ECO:0000244|PDB:1DBG}.
STRAND 351 358 {ECO:0000244|PDB:1DBG}.
HELIX 361 370 {ECO:0000244|PDB:1DBG}.
STRAND 380 385 {ECO:0000244|PDB:1DBG}.
STRAND 387 389 {ECO:0000244|PDB:1DBG}.
STRAND 398 400 {ECO:0000244|PDB:1DBG}.
STRAND 408 413 {ECO:0000244|PDB:1DBG}.
STRAND 415 419 {ECO:0000244|PDB:1DBG}.
STRAND 422 424 {ECO:0000244|PDB:1DBG}.
HELIX 431 433 {ECO:0000244|PDB:1DBO}.
HELIX 452 458 {ECO:0000244|PDB:1DBG}.
HELIX 467 469 {ECO:0000244|PDB:1DBG}.
HELIX 482 485 {ECO:0000244|PDB:1DBG}.
HELIX 490 502 {ECO:0000244|PDB:1DBG}.
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


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