CABC2_BACTN
ID CABC2_BACTN Reviewed; 1014 AA.
AC Q8A2I1;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Chondroitin sulfate ABC exolyase {ECO:0000250|UniProtKB:C5G6D7};
DE EC=4.2.2.21 {ECO:0000250|UniProtKB:C5G6D7};
DE AltName: Full=Chondroitin ABC exoeliminase {ECO:0000250|UniProtKB:C5G6D7};
DE AltName: Full=Chondroitin ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
DE AltName: Full=Chondroitin sulfate ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
DE Short=ChS ABC lyase II {ECO:0000250|UniProtKB:C5G6D7};
DE AltName: Full=Chondroitinase ABC II {ECO:0000250|UniProtKB:C5G6D7, ECO:0000312|EMBL:AAO78430.1};
DE Short=cABC II {ECO:0000250|UniProtKB:C5G6D7};
DE AltName: Full=Exochondroitinase ABC {ECO:0000250|UniProtKB:C5G6D7};
DE Flags: Precursor;
GN Name=chonabc {ECO:0000250|UniProtKB:C5G6D7}; OrderedLocusNames=BT_3324;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1] {ECO:0000312|EMBL:AAO78430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000305}
RP CATALYTIC ACTIVITY AS CHONDROITIN SULFATE ABC LYASE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000269|PubMed:6782076};
RX PubMed=6782076; DOI=10.1128/jb.143.2.772-780.1980;
RA Salyers A.A., O'Brien M.;
RT "Cellular location of enzymes involved in chondroitin sulfate breakdown by
RT Bacteroides thetaiotaomicron.";
RL J. Bacteriol. 143:772-780(1980).
RN [3] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY AS CHONDROITIN SULFATE ABC LYASE.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000269|PubMed:6630153};
RX PubMed=6630153; DOI=10.1128/jb.156.2.859-866.1983;
RA Linn S., Chan T., Lipeski L., Salyers A.A.;
RT "Isolation and characterization of two chondroitin lyases from Bacteroides
RT thetaiotaomicron.";
RL J. Bacteriol. 156:859-866(1983).
CC -!- FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an
CC exolytic fashion degrading chondroitin sulfates and dermatan sulfate to
CC yield only disaccharide products. Has a preference for chondroitin 4-
CC sulfate over chondroitin 6-sulfate. Has extremely low activity against
CC hyaluronic acid. Is not active against acharan sulfate, heparin or
CC heparan sulfate. {ECO:0000250|UniProtKB:C5G6D7,
CC ECO:0000269|PubMed:6630153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic removal of Delta(4)-unsaturated disaccharide residues
CC from the non-reducing ends of both polymeric chondroitin/dermatan
CC sulfates and their oligosaccharide fragments.; EC=4.2.2.21;
CC Evidence={ECO:0000269|PubMed:6630153, ECO:0000269|PubMed:6782076};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Divalent metal cation. Requires divalent metal cation for binding
CC of dermatan sulfate substrate, whereas it is not necessary for the
CC binding of chondroitin sulfate substrates. Prefers Ca(2+) or Mg(2+),
CC binding 1 ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:C5G6D7}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:6782076}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000255}.
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DR EMBL; AE015928; AAO78430.1; -; Genomic_DNA.
DR RefSeq; NP_812236.1; NC_004663.1.
DR AlphaFoldDB; Q8A2I1; -.
DR SMR; Q8A2I1; -.
DR STRING; 226186.BT_3324; -.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR PaxDb; Q8A2I1; -.
DR PRIDE; Q8A2I1; -.
DR EnsemblBacteria; AAO78430; AAO78430; BT_3324.
DR KEGG; bth:BT_3324; -.
DR PATRIC; fig|226186.12.peg.3391; -.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_011258_0_0_10; -.
DR InParanoid; Q8A2I1; -.
DR OMA; VCYERDM; -.
DR BRENDA; 4.2.2.21; 709.
DR EvolutionaryTrace; Q8A2I1; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IBA:GO_Central.
DR GO; GO:0030341; F:chondroitin AC lyase activity; IDA:UniProtKB.
DR GO; GO:0033999; F:chondroitin B lyase activity; IDA:UniProtKB.
DR GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:InterPro.
DR GO; GO:0034001; F:chondroitin-sulfate-ABC exolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030340; F:hyaluronate lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030207; P:chondroitin sulfate catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR039174; Chondroitin_ABC_lyase.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR024200; Chondroitinase_ABC_I.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR InterPro; IPR015177; Lyase_catalyt.
DR InterPro; IPR015176; Lyase_N.
DR PANTHER; PTHR37322; PTHR37322; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF09093; Lyase_catalyt; 1.
DR Pfam; PF09092; Lyase_N; 1.
DR PIRSF; PIRSF034515; Chondroitinase; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Lyase; Metal-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..1014
FT /note="Chondroitin sulfate ABC exolyase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420124"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT SITE 172
FT /note="Important for catalytic activity against all
FT substrates"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT SITE 344
FT /note="Important for catalytic activity against dermatan
FT sulfate substrate"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT SITE 514
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
FT SITE 628
FT /note="Important for catalytic activity against all
FT substrates"
FT /evidence="ECO:0000250|UniProtKB:C5G6D7"
SQ 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
