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Chondroitinase-AC (EC 4.2.2.5) (Chondroitin sulfate AC lyase) (Chondroitin-AC eliminase) (Chondroitin-AC lyase)

 CSLA_PEDHD              Reviewed;         700 AA.
Q59288; C6Y215;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 104.
RecName: Full=Chondroitinase-AC;
EC=4.2.2.5;
AltName: Full=Chondroitin sulfate AC lyase;
AltName: Full=Chondroitin-AC eliminase;
AltName: Full=Chondroitin-AC lyase;
Flags: Precursor;
Name=cslA; Synonyms=chnAC; OrderedLocusNames=Phep_0786;
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]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=10329169; DOI=10.1006/jmbi.1999.2698;
Fethiere J., Eggimann B., Cygler M.;
"Crystal structure of chondroitin AC lyase, a representative of a
family of glycosaminoglycan degrading enzymes.";
J. Mol. Biol. 288:635-647(1999).
[4]
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).
-!- CATALYTIC ACTIVITY: Eliminative degradation of polysaccharides
containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl
linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-
enuronosyl groups.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion per subunit.;
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
{ECO:0000305}.
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EMBL; U27583; AAC83383.1; -; Genomic_DNA.
EMBL; CP001681; ACU03008.1; -; Genomic_DNA.
RefSeq; WP_012780954.1; NZ_AQGK01000003.1.
PDB; 1CB8; X-ray; 1.90 A; A=23-700.
PDB; 1HM2; X-ray; 2.00 A; A=1-700.
PDB; 1HM3; X-ray; 2.10 A; A=1-700.
PDB; 1HMU; X-ray; 2.00 A; A=1-700.
PDB; 1HMW; X-ray; 2.30 A; A=1-700.
PDBsum; 1CB8; -.
PDBsum; 1HM2; -.
PDBsum; 1HM3; -.
PDBsum; 1HMU; -.
PDBsum; 1HMW; -.
ProteinModelPortal; Q59288; -.
SMR; Q59288; -.
STRING; 485917.Phep_0786; -.
DrugBank; DB03863; 2-O-Methyl Fucose.
DrugBank; DB01872; Acetylgalactosamine-4-Sulfate.
DrugBank; DB03389; alpha-D-Xylopyranose.
DrugBank; DB02945; alpha-L-iduronic acid.
DrugBank; DB03879; alpha-L-methyl-fucose.
DrugBank; DB03156; D-Glucuronic Acid.
DrugBank; DB02186; N-Acetyl-D-Galactosamine 6-Sulfate.
CAZy; PL8; Polysaccharide Lyase Family 8.
PRIDE; Q59288; -.
EnsemblBacteria; ACU03008; ACU03008; Phep_0786.
KEGG; phe:Phep_0786; -.
eggNOG; ENOG4106AM8; Bacteria.
eggNOG; ENOG410XTFC; LUCA.
HOGENOM; HOG000105747; -.
KO; K19049; -.
OMA; RGDEYHN; -.
OrthoDB; POG091H03FL; -.
BioCyc; MetaCyc:MONOMER-15799; -.
BioCyc; PHEP485917:G1GFH-801-MONOMER; -.
BRENDA; 4.2.2.5; 2286.
EvolutionaryTrace; Q59288; -.
Proteomes; UP000000852; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0030341; F:chondroitin AC lyase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
Gene3D; 1.50.10.100; -; 1.
Gene3D; 2.60.220.10; -; 1.
Gene3D; 2.70.98.10; -; 1.
InterPro; IPR008929; Chondroitin_lyas.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR014718; GH-type_carb-bd.
InterPro; IPR038970; Lyase_8.
InterPro; IPR011071; Lyase_8-like_C.
InterPro; IPR012970; Lyase_8_alpha_N.
InterPro; IPR004103; Lyase_8_C.
InterPro; IPR003159; Lyase_8_central_dom.
PANTHER; PTHR38481; PTHR38481; 1.
Pfam; PF02278; Lyase_8; 1.
Pfam; PF02884; Lyase_8_C; 1.
Pfam; PF08124; Lyase_8_N; 1.
SUPFAM; SSF48230; SSF48230; 1.
SUPFAM; SSF49863; SSF49863; 1.
SUPFAM; SSF74650; SSF74650; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Glycoprotein; Lyase;
Metal-binding; Reference proteome; Signal.
SIGNAL 1 22
CHAIN 23 700 Chondroitinase-AC.
/FTId=PRO_0000024927.
ACT_SITE 225 225
ACT_SITE 234 234
ACT_SITE 288 288
METAL 405 405 Calcium.
METAL 407 407 Calcium.
METAL 416 416 Calcium.
METAL 417 417 Calcium; via carbonyl oxygen.
CARBOHYD 328 328 O-linked (Man...) serine.
CARBOHYD 455 455 O-linked (Man...) serine.
HELIX 27 39 {ECO:0000244|PDB:1CB8}.
HELIX 46 56 {ECO:0000244|PDB:1CB8}.
STRAND 73 75 {ECO:0000244|PDB:1CB8}.
HELIX 79 93 {ECO:0000244|PDB:1CB8}.
TURN 98 101 {ECO:0000244|PDB:1CB8}.
HELIX 103 119 {ECO:0000244|PDB:1CB8}.
HELIX 126 130 {ECO:0000244|PDB:1CB8}.
HELIX 132 143 {ECO:0000244|PDB:1CB8}.
HELIX 144 146 {ECO:0000244|PDB:1CB8}.
STRAND 147 149 {ECO:0000244|PDB:1CB8}.
HELIX 153 161 {ECO:0000244|PDB:1CB8}.
HELIX 168 170 {ECO:0000244|PDB:1CB8}.
HELIX 173 189 {ECO:0000244|PDB:1CB8}.
HELIX 193 204 {ECO:0000244|PDB:1CB8}.
STRAND 207 217 {ECO:0000244|PDB:1CB8}.
STRAND 225 227 {ECO:0000244|PDB:1CB8}.
TURN 231 233 {ECO:0000244|PDB:1CB8}.
HELIX 234 249 {ECO:0000244|PDB:1CB8}.
HELIX 258 270 {ECO:0000244|PDB:1CB8}.
HELIX 273 275 {ECO:0000244|PDB:1CB8}.
HELIX 283 285 {ECO:0000244|PDB:1CB8}.
HELIX 287 291 {ECO:0000244|PDB:1CB8}.
TURN 293 296 {ECO:0000244|PDB:1CB8}.
HELIX 299 301 {ECO:0000244|PDB:1CB8}.
HELIX 302 311 {ECO:0000244|PDB:1CB8}.
HELIX 313 315 {ECO:0000244|PDB:1CB8}.
HELIX 316 326 {ECO:0000244|PDB:1CB8}.
TURN 332 335 {ECO:0000244|PDB:1CB8}.
STRAND 339 343 {ECO:0000244|PDB:1CB8}.
TURN 344 347 {ECO:0000244|PDB:1CB8}.
STRAND 348 353 {ECO:0000244|PDB:1CB8}.
STRAND 356 361 {ECO:0000244|PDB:1CB8}.
TURN 381 384 {ECO:0000244|PDB:1CB8}.
STRAND 385 394 {ECO:0000244|PDB:1CB8}.
HELIX 395 397 {ECO:0000244|PDB:1CB8}.
HELIX 401 403 {ECO:0000244|PDB:1CB8}.
HELIX 406 408 {ECO:0000244|PDB:1HM2}.
STRAND 413 415 {ECO:0000244|PDB:1CB8}.
STRAND 425 427 {ECO:0000244|PDB:1CB8}.
STRAND 436 440 {ECO:0000244|PDB:1CB8}.
STRAND 445 453 {ECO:0000244|PDB:1CB8}.
STRAND 456 464 {ECO:0000244|PDB:1CB8}.
STRAND 469 478 {ECO:0000244|PDB:1CB8}.
STRAND 480 492 {ECO:0000244|PDB:1CB8}.
STRAND 497 499 {ECO:0000244|PDB:1CB8}.
STRAND 502 504 {ECO:0000244|PDB:1CB8}.
STRAND 509 514 {ECO:0000244|PDB:1CB8}.
STRAND 519 522 {ECO:0000244|PDB:1CB8}.
STRAND 525 528 {ECO:0000244|PDB:1CB8}.
STRAND 533 538 {ECO:0000244|PDB:1CB8}.
STRAND 541 546 {ECO:0000244|PDB:1CB8}.
TURN 547 549 {ECO:0000244|PDB:1CB8}.
STRAND 557 572 {ECO:0000244|PDB:1CB8}.
STRAND 574 584 {ECO:0000244|PDB:1CB8}.
HELIX 590 593 {ECO:0000244|PDB:1CB8}.
HELIX 596 598 {ECO:0000244|PDB:1CB8}.
STRAND 601 614 {ECO:0000244|PDB:1CB8}.
TURN 615 618 {ECO:0000244|PDB:1CB8}.
STRAND 619 632 {ECO:0000244|PDB:1CB8}.
STRAND 635 641 {ECO:0000244|PDB:1CB8}.
STRAND 643 648 {ECO:0000244|PDB:1CB8}.
STRAND 655 659 {ECO:0000244|PDB:1CB8}.
STRAND 666 674 {ECO:0000244|PDB:1CB8}.
TURN 675 677 {ECO:0000244|PDB:1CB8}.
STRAND 680 686 {ECO:0000244|PDB:1CB8}.
HELIX 690 692 {ECO:0000244|PDB:1CB8}.
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


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