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Chondroitin sulfate ABC exolyase (EC 4.2.2.21) (Chondroitin ABC exoeliminase) (Chondroitin ABC lyase II) (Chondroitin sulfate ABC lyase II) (ChS ABC lyase II) (Chondroitinase ABC II) (cABC II) (Exochondroitinase ABC)

 CABC2_BACTN             Reviewed;        1014 AA.
Q8A2I1;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
23-MAY-2018, entry version 94.
RecName: Full=Chondroitin sulfate ABC exolyase {ECO:0000250|UniProtKB:C5G6D7};
EC=4.2.2.21 {ECO:0000250|UniProtKB:C5G6D7};
AltName: Full=Chondroitin ABC exoeliminase {ECO:0000250|UniProtKB:C5G6D7};
AltName: Full=Chondroitin ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
AltName: Full=Chondroitin sulfate ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
Short=ChS ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
AltName: Full=Chondroitinase ABC II {ECO:0000250|UniProtKB:C5G6D7, ECO:0000312|EMBL:AAO78430.1};
Short=cABC II {ECO:0000250|UniProtKB:C5G6D7};
AltName: Full=Exochondroitinase ABC {ECO:0000250|UniProtKB:C5G6D7};
Flags: Precursor;
Name=chonabc {ECO:0000250|UniProtKB:C5G6D7};
OrderedLocusNames=BT_3324;
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
10582 / E50 / VPI-5482).
Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
Bacteroides.
NCBI_TaxID=226186;
[1] {ECO:0000312|EMBL:AAO78430.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
PubMed=12663928; DOI=10.1126/science.1080029;
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
[2] {ECO:0000305}
CATALYTIC ACTIVITY AS CHONDROITIN SULFATE ABC LYASE, AND SUBCELLULAR
LOCATION.
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482
{ECO:0000269|PubMed:6782076};
PubMed=6782076;
Salyers A.A., O'Brien M.;
"Cellular location of enzymes involved in chondroitin sulfate
breakdown by Bacteroides thetaiotaomicron.";
J. Bacteriol. 143:772-780(1980).
[3] {ECO:0000305}
FUNCTION, AND CATALYTIC ACTIVITY AS CHONDROITIN SULFATE ABC LYASE.
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482
{ECO:0000269|PubMed:6630153};
PubMed=6630153;
Linn S., Chan T., Lipeski L., Salyers A.A.;
"Isolation and characterization of two chondroitin lyases from
Bacteroides thetaiotaomicron.";
J. Bacteriol. 156:859-866(1983).
-!- FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in
an exolytic fashion degrading chondroitin sulfates and dermatan
sulfate to yield only disaccharide products. Has a preference for
chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely
low activity against hyaluronic acid. Is not active against
acharan sulfate, heparin or heparan sulfate.
{ECO:0000250|UniProtKB:C5G6D7, ECO:0000269|PubMed:6630153}.
-!- CATALYTIC ACTIVITY: Exolytic removal of Delta(4)-unsaturated
disaccharide residues from the non-reducing ends of both polymeric
chondroitin/dermatan sulfates and their oligosaccharide fragments.
{ECO:0000269|PubMed:6630153, ECO:0000269|PubMed:6782076}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Divalent metal cation. Requires divalent metal cation for
binding of dermatan sulfate substrate, whereas it is not necessary
for the binding of chondroitin sulfate substrates. Prefers Ca(2+)
or Mg(2+), binding 1 ion per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:C5G6D7}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6782076}.
-!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
{ECO:0000255}.
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EMBL; AE015928; AAO78430.1; -; Genomic_DNA.
RefSeq; NP_812236.1; NC_004663.1.
RefSeq; WP_011108769.1; NC_004663.1.
ProteinModelPortal; Q8A2I1; -.
SMR; Q8A2I1; -.
STRING; 226186.BT_3324; -.
CAZy; PL8; Polysaccharide Lyase Family 8.
PaxDb; Q8A2I1; -.
PRIDE; Q8A2I1; -.
EnsemblBacteria; AAO78430; AAO78430; BT_3324.
GeneID; 1075480; -.
KEGG; bth:BT_3324; -.
PATRIC; fig|226186.12.peg.3391; -.
eggNOG; ENOG4105TCD; Bacteria.
eggNOG; ENOG410Y18H; LUCA.
HOGENOM; HOG000105746; -.
InParanoid; Q8A2I1; -.
KO; K08961; -.
OMA; NAHYEYL; -.
OrthoDB; POG091H1YF1; -.
BioCyc; BTHE:G13PU-8291-MONOMER; -.
BRENDA; 4.2.2.21; 709.
EvolutionaryTrace; Q8A2I1; -.
Proteomes; UP000001414; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:InterPro.
GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0030341; F:chondroitin AC lyase activity; IDA:UniProtKB.
GO; GO:0033999; F:chondroitin B lyase activity; IDA:UniProtKB.
GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:InterPro.
GO; GO:0034001; F:chondroitin-sulfate-ABC exolyase activity; IEA:UniProtKB-EC.
GO; GO:0030340; F:hyaluronate lyase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0030207; P:chondroitin sulfate catabolic process; IDA:UniProtKB.
Gene3D; 1.50.10.100; -; 1.
Gene3D; 2.60.220.10; -; 1.
Gene3D; 2.70.98.10; -; 1.
InterPro; IPR008929; Chondroitin_lyas.
InterPro; IPR024200; Chondroitinase_ABC_I.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR014718; GH-type_carb-bd.
InterPro; IPR011071; Lyase_8-like_C.
InterPro; IPR003159; Lyase_8_central_dom.
InterPro; IPR015177; Lyase_catalyt.
InterPro; IPR015176; Lyase_N.
Pfam; PF02278; Lyase_8; 1.
Pfam; PF09093; Lyase_catalyt; 1.
Pfam; PF09092; Lyase_N; 1.
PIRSF; PIRSF034515; Chondroitinase; 1.
SUPFAM; SSF48230; SSF48230; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF49863; SSF49863; 1.
SUPFAM; SSF74650; SSF74650; 1.
1: Evidence at protein level;
Calcium; Carbohydrate metabolism; Complete proteome; Lyase;
Metal-binding; Periplasm; Reference proteome; Signal.
SIGNAL 1 14 {ECO:0000255}.
CHAIN 15 1014 Chondroitin sulfate ABC exolyase.
{ECO:0000255}.
/FTId=PRO_0000420124.
ACT_SITE 345 345 Proton acceptor.
{ECO:0000250|UniProtKB:C5G6D7}.
ACT_SITE 454 454 Proton acceptor.
{ECO:0000250|UniProtKB:C5G6D7}.
ACT_SITE 461 461 Proton donor.
{ECO:0000250|UniProtKB:C5G6D7}.
METAL 24 24 Calcium. {ECO:0000250|UniProtKB:C5G6D7}.
METAL 26 26 Calcium. {ECO:0000250|UniProtKB:C5G6D7}.
METAL 50 50 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:C5G6D7}.
METAL 53 53 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:C5G6D7}.
METAL 161 161 Calcium. {ECO:0000250|UniProtKB:C5G6D7}.
SITE 172 172 Important for catalytic activity against
all substrates.
{ECO:0000250|UniProtKB:C5G6D7}.
SITE 344 344 Important for catalytic activity against
dermatan sulfate substrate.
{ECO:0000250|UniProtKB:C5G6D7}.
SITE 514 514 Transition state stabilizer.
{ECO:0000250|UniProtKB:C5G6D7}.
SITE 628 628 Important for catalytic activity against
all substrates.
{ECO:0000250|UniProtKB:C5G6D7}.
SEQUENCE 1014 AA; 114839 MW; A58D5B0085F28355 CRC64;
MLILSFLCPA FLNAQIVTDE RMFSFEEPQL PACITGVQSQ LGISGAHYKD GKHSLEWTFE
PNGKLELRKD LKFEKKDPTG KDLYLSAFIV WIYNEQPQDA AIEFEFLKDG RKCASFPFGI
NFKGWRAAWV CYERDMQGTP EEGMNELRIV APNAKGRLFI DHLITATKVD ARQQTADLQV
PFVNAGTTNH WLVLYKHSLL KPDIELTPVS DRQRQEMKLL EKRFRDMIYT KGKVTEKEAE
TIRKKYDLYQ ITYKDGQVSG VPIFMVRASE AYERMIPDWD KDMLTKMGIE MRAYFDLMKR
IAVAYNNSEA GSPVREEMKR KFLAMYDHIT DQGVAYGSCW GNIHHYGYSV RGLYPAYFLM
KDVLREEGKL LEAERTLRWY AITNEVYPKP EGNGIDMDSF NTQTTGRIAS ILMMEDTPEK
LQYLKSFSRW IDYGCRPAPG LAGSFKVDGG AFHHRNNYPA YAVGGLDGAT NMIYLFSRTS
LAVSELAHRT VKDVLLAMRF YCNKLNFPLS MSGRHPDGQG KLVPMHYAMM AIAGTPDGKG
DFDKEMASAY LRLVSSDSSS AEQAPEYMPK VSNAQERKIA KRLVENGFRA ESDPQGNLSL
GYGCVSVQRR ENWSAVARGH SRYLWAAEHY LGHNLYGRYL AHGSLQILTA PPGQTVTPAT
SGWQQEGFDW NRIPGVTSIH LPLDLLKANV LNVDTFSGME EMLYSDEAFA GGLSQGKMNG
NFGMKLHEHD KYNGTHRARK SYHFIDGMIV CLGSDIENTN TDYPTETTIF QLAVTDKAAH
DYWKNNAGEG KVWMDHLGTG YYVPVPARFE KNFPQYSRMQ DTGKETKGDW VSLIIDHGKA
PKAGSYEYAI LPGTDRKTMT AFAKKPAYSV LQQDRNAHIL ESPSDRITSY VLFETPQSLL
PGGLLQRTDT SCLVMVRKES ADKVLLTVAQ PDLALYRGPS DEAFDKDGKR MERSIYSRPW
IDNESGEIPV TVTLKGRWKV AETPFCKVVS EDKKQTVLRF LCKDGASYEV ELEK


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