CABC2_PROVU
ID CABC2_PROVU Reviewed; 990 AA.
AC C7S340;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Chondroitin sulfate ABC exolyase;
DE EC=4.2.2.21;
DE AltName: Full=Chondroitin ABC exoeliminase;
DE AltName: Full=Chondroitin ABC lyase II;
DE AltName: Full=Chondroitin sulfate ABC lyase II;
DE Short=ChS ABC lyase II;
DE AltName: Full=Chondroitinase ABC II;
DE Short=cABC II;
DE AltName: Full=Exochondroitinase ABC;
DE Flags: Fragment;
GN Name=ChABCII;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RA Tam K.-W., Wang Q., Li R.A., Chan Y.-S., Shum D.K.-Y.;
RT "Cloning, recombinant expression, characterization and mutagenesis of
RT chondroitin sulphate ABC exolyase from Proteus vulgaris.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=9083041; DOI=10.1074/jbc.272.14.9123;
RA Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K.,
RA Suzuki S.;
RT "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding
RT tetrasaccharides and an exoeliminase preferentially acting on
RT oligosaccharides.";
RL J. Biol. Chem. 272:9123-9130(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE RESIDUES, AND MUTAGENESIS OF HIS-343; HIS-452;
RP HIS-453; HIS-456; TYR-460; ARG-513 AND GLU-608.
RC STRAIN=ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636;
RX PubMed=18849565; DOI=10.1074/jbc.m806630200;
RA Prabhakar V., Capila I., Soundararajan V., Raman R., Sasisekharan R.;
RT "Recombinant expression, purification, and biochemical characterization of
RT chondroitinase ABC II from Proteus vulgaris.";
RL J. Biol. Chem. 284:974-982(2009).
CC -!- FUNCTION: Broad-specificity glycosaminoglycan lyase, which acts in an
CC exolytic fashion, and preferentially degrades the tetra- and
CC hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate
CC produced by the chondroitin sulfate ABC endolyase, to yield the
CC respective disaccharides. To a lesser extent, is also able to split off
CC disaccharide residues directly from polymeric chondroitin 4- and 6-
CC sulfate, dermatan sulfate, chondroitin, and hyaluronan. Is not active
CC against keratan sulfate, heparan sulfate, and heparin.
CC {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041}.
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:18849565, ECO:0000269|PubMed:9083041};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+), whereas Ni(2+), Fe(2+), and
CC Cu(2+) have little or no effect on activity.
CC {ECO:0000269|PubMed:9083041}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for chondroitin 6-sulfate tetrasaccharide
CC {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
CC KM=80 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC KM=9.8 uM for chondroitin 6-sulfate {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC KM=16.1 uM for chondroitin 4-sulfate {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC KM=19.2 uM for dermatan sulfate {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC Vmax=155 umol/min/mg enzyme with chondroitin 6-sulfate
CC tetrasaccharide as substrate {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC Vmax=34 umol/min/mg enzyme with chondroitin 6-sulfate as substrate
CC {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18849565,
CC ECO:0000269|PubMed:9083041};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius (PubMed:9083041). Optimum
CC temperature is 37 degrees Celsius (PubMed:18849565).
CC {ECO:0000269|PubMed:18849565, ECO:0000269|PubMed:9083041};
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
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DR EMBL; EF988659; ABU46331.1; -; Genomic_DNA.
DR AlphaFoldDB; C7S340; -.
DR SMR; C7S340; -.
DR STRING; 585.DR95_2845; -.
DR eggNOG; ENOG502Z8J1; Bacteria.
DR BioCyc; MetaCyc:MON-15789; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IEA:InterPro.
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; IPR004103; Lyase_8_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; PF02884; Lyase_8_C; 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 Carbohydrate metabolism; Lyase.
FT CHAIN <1..990
FT /note="Chondroitin sulfate ABC exolyase"
FT /id="PRO_0000413627"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:18849565"
FT ACT_SITE 460
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT SITE 513
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT SITE 608
FT /note="Important for catalytic activity"
FT MUTAGEN 343
FT /note="H->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 452
FT /note="H->A: Slight decrease in substrate affinity, but
FT greatly reduced (100-fold) catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 453
FT /note="H->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 456
FT /note="H->A: 3-fold decrease in catalytic efficiency with
FT both chondroitin 6-sulfate and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 460
FT /note="Y->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 513
FT /note="R->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT MUTAGEN 608
FT /note="E->A: Loss of activity on both chondroitin 6-sulfate
FT and dermatan sulfate."
FT /evidence="ECO:0000269|PubMed:18849565"
FT NON_TER 1
SQ SEQUENCE 990 AA; 111744 MW; 7AA786306AAADF08 CRC64;
LPTLSHEAFG DIYLFEGELP NTLTTSNNNQ LSLSKQHAKD GEQSLKWQYQ PQATLTLNNI
VNYQDDKNTA TPLTFMMWIY NEKPQSSPLT LAFKQNNKIA LSFNAELNFT GWRGIAVPFR
DMQGSATGQL DQLVITAPNQ AGTLFFDQII MSVPLDNRWA VPDYQTPYVN NAVNTMVSKN
WSALLMYDQM FQAHYPTLNF DTEFRDDQTE MASIYQRFEY YQGIRSDKKI TPDMLDKHLA
LWEKLVLTQH ADGSITGKAL DHPNRQHFMK VEGVFSEGTQ KALLDANMLR DVGKTLLQTA
IYLRSDSLSA TDRKKLEERY LLGTRYVLEQ GFTRGSGYQI ITHVGYQTRE LFDAWFIGRH
VLAKNNLLAP TQQAMMWYNA TGRIFEKNNE IVDANVDILN TQLQWMIKSL LMLPDYQQRQ
QALAQLQSWL NKTILSSKGV AGGFKSDGSI FHHSQHYPAY AKDAFGGLAP SVYALSDSPF
RLSTSAHERL KDVLLKMRIY TKETQIPVVL SGRHPTGLHK IGIAPFKWMA LAGTPDGKQK
LDTTLSAAYA KLDNKTHFEG INAESEPVGA WAMNYASMAI QRRASTQSPQ QSWLAIARGF
SRYLVGNESY ENNNRYGRYL QYGQLEIIPA DLTQSGFSHA GWDWNRYPGT TTIHLPYNEL
EAKLNQLPAA GIEEMLLSTE SYSGANTLNN NSMFAMKLHG HSKYQQQSLR ANKSYFLFDN
RVIALGSGIE NDDKQHTTET TLFQFAVPKL QSVIINGKKV NQLDTQLTLN NADTLIDPTG
NLYKLTKGQT VKFSYQKQHS LDDRNSKPTE QLFATAVISH GKAPSNENYE YAIAIEAQNN
KAPEYTVLQH NDQLHAVKDK ITQEEGYAFF EATKLKSADA TLLSSDAPVM VMAKIQNQQL
TLSIVNPDLN LYQGREKDQF DDKGNQIEVS VYSRHWLTAE SQSTNSTITV KGIWKLTTPQ
PGVIIKHHNN NTLITTTTIQ ATPTVINLVK
