UCDH_STRA3
ID UCDH_STRA3 Reviewed; 398 AA.
AC Q8E372;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Unsaturated chondroitin disaccharide hydrolase;
DE EC=3.2.1.180;
DE AltName: Full=Unsaturated glucuronyl hydrolase;
DE Short=SagUGL;
GN OrderedLocusNames=gbs1889;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP ACTIVE SITE, INDUCTION, AND MUTAGENESIS OF ASP-115; ASP-175 AND ARG-236.
RC STRAIN=NEM316;
RX PubMed=19416976; DOI=10.1074/jbc.m109.005660;
RA Maruyama Y., Nakamichi Y., Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Substrate specificity of streptococcal unsaturated glucuronyl hydrolases
RT for sulfated glycosaminoglycan.";
RL J. Biol. Chem. 284:18059-18069(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-155 IN
RP COMPLEX WITH N-ACETYL-D-GALACTOSAMINE 6-SULFATE, FUNCTION, CATALYTIC
RP ACTIVITY, AND MUTAGENESIS OF SER-365; SER-368 AND LYS-370.
RC STRAIN=NEM316;
RX PubMed=21147778; DOI=10.1074/jbc.m110.182618;
RA Nakamichi Y., Maruyama Y., Mikami B., Hashimoto W., Murata K.;
RT "Structural determinants in streptococcal unsaturated glucuronyl hydrolase
RT for recognition of glycosaminoglycan sulfate groups.";
RL J. Biol. Chem. 286:6262-6271(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ASN-155.
RC STRAIN=NEM316;
RA Nakamichi Y., Maruyama Y., Mikami B., Hashimoto W., Murata K.;
RT "Crystal structure of unsaturated glucuronyl hydrolase mutant D115N from
RT Streptcoccus agalactiae.";
RL Submitted (SEP-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of unsaturated hyaluronate and
CC chondroitin disaccharides. Also degrades unsaturated heparin
CC disaccharides. Releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-
CC deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides,
CC hyaluronan disaccharides and heparin disaccharides and cleaves both
CC glycosidic (1->3) and (1->4) bonds. Prefers sulfated glycosaminoglycans
CC compared to unsulfated glycosaminoglycans. Probably required for
CC mammalian cells invasion through the degradation of extracellular
CC sulfated glycosaminoglycans such as chondroitin and hyaluronan.
CC {ECO:0000269|PubMed:19416976, ECO:0000269|PubMed:21147778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-4-deoxy-Delta(4)-GlcpA-(1->3)-beta-D-GalpNAc6S + H2O =
CC 5-dehydro-4-deoxy-D-glucuronate + N-acetyl-beta-D-galactosamine 6-
CC sulfate; Xref=Rhea:RHEA:31647, ChEBI:CHEBI:15377, ChEBI:CHEBI:17117,
CC ChEBI:CHEBI:63267, ChEBI:CHEBI:63270; EC=3.2.1.180;
CC Evidence={ECO:0000269|PubMed:19416976, ECO:0000269|PubMed:21147778};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.27 mM for unsaturated chondroitin disaccharidee (delta0S)
CC {ECO:0000269|PubMed:19416976, ECO:0000269|PubMed:21147778};
CC KM=0.1 mM for unsaturated chondroitin disaccharide sulfated at C-6
CC position of GalNAc residue (delta6S) {ECO:0000269|PubMed:19416976,
CC ECO:0000269|PubMed:21147778};
CC KM=0.54 mM for unsaturated chondroitin disaccharide sulfated at C-6
CC position of GalNAc residue (delta6S) {ECO:0000269|PubMed:19416976};
CC Note=kcat is 2.69 sec(-1) with unsaturated chondroitin (delta0S)
CC (PubMed:21147778). kcat is 24 sec(-1) with unsaturated chondroitin
CC disaccharide sulfated at C-6 position of GalNAc residue (delta6S)
CC (PubMed:19416976). kcat is 10.2 sec(-1) with unsaturated chondroitin
CC disaccharide sulfated at C-6 position of GalNAc residue (delta6S)
CC (PubMed:21147778). {ECO:0000269|PubMed:19416976,
CC ECO:0000269|PubMed:21147778};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:19416976};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19416976};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19416976,
CC ECO:0000269|PubMed:21147778}.
CC -!- INDUCTION: Constitutively expressed. Expression level increases in the
CC presence of glycosaminoglycan. {ECO:0000269|PubMed:19416976}.
CC -!- MISCELLANEOUS: Ser-365 and Ser-368 bind the sulfated group in the
CC substrate and determine the preference for sulfated glycosaminoglycans
CC compared to unsulfated glycosaminoglycans.
CC {ECO:0000305|PubMed:21147778}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 88 family. {ECO:0000305}.
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DR EMBL; AL766854; CAD47548.1; -; Genomic_DNA.
DR RefSeq; WP_000975716.1; NC_004368.1.
DR PDB; 3ANI; X-ray; 2.50 A; A=1-398.
DR PDB; 3ANJ; X-ray; 1.95 A; A=1-398.
DR PDB; 3ANK; X-ray; 2.02 A; A=1-398.
DR PDB; 3VXD; X-ray; 2.00 A; A/B/C/D=1-398.
DR PDB; 3WUX; X-ray; 1.79 A; A=1-398.
DR PDBsum; 3ANI; -.
DR PDBsum; 3ANJ; -.
DR PDBsum; 3ANK; -.
DR PDBsum; 3VXD; -.
DR PDBsum; 3WUX; -.
DR AlphaFoldDB; Q8E372; -.
DR SMR; Q8E372; -.
DR STRING; 211110.gbs1889; -.
DR CAZy; GH88; Glycoside Hydrolase Family 88.
DR EnsemblBacteria; CAD47548; CAD47548; CAD47548.
DR KEGG; san:gbs1889; -.
DR eggNOG; COG4225; Bacteria.
DR HOGENOM; CLU_027158_1_1_9; -.
DR OMA; YWDLIFG; -.
DR BioCyc; MetaCyc:MON-16268; -.
DR BRENDA; 3.2.1.180; 5917.
DR EvolutionaryTrace; Q8E372; -.
DR Proteomes; UP000000823; Chromosome.
DR GO; GO:0052757; F:chondroitin hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102212; F:unsaturated chondroitin disaccharide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010905; Glyco_hydro_88.
DR Pfam; PF07470; Glyco_hydro_88; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Virulence.
FT CHAIN 1..398
FT /note="Unsaturated chondroitin disaccharide hydrolase"
FT /id="PRO_0000422016"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19416976"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:19416976"
FT BINDING 115
FT /ligand="substrate"
FT BINDING 175
FT /ligand="substrate"
FT BINDING 233
FT /ligand="substrate"
FT BINDING 235
FT /ligand="substrate"
FT BINDING 247
FT /ligand="substrate"
FT BINDING 251
FT /ligand="substrate"
FT BINDING 365
FT /ligand="substrate"
FT BINDING 368
FT /ligand="substrate"
FT MUTAGEN 115
FT /note="D->N: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:19416976"
FT MUTAGEN 175
FT /note="D->N: Large decrease in activity."
FT /evidence="ECO:0000269|PubMed:19416976"
FT MUTAGEN 236
FT /note="R->A,H: Able to degrade unsaturated chondroitin
FT disaccharide sulfated at C-6 position of GalNAc residue
FT (delta6S) but abolishes ability to degrade unsaturated
FT chondroitin disaccharide sulfated at C-4 position of GalNAc
FT residue (delta4S)."
FT /evidence="ECO:0000269|PubMed:19416976"
FT MUTAGEN 365
FT /note="S->H: Prefers unsulfated glycosaminoglycans compared
FT to sulfated glycosaminoglycans."
FT /evidence="ECO:0000269|PubMed:21147778"
FT MUTAGEN 368
FT /note="S->G: Affects preference for sulfated
FT glycosaminoglycans compared to sulfated
FT glycosaminoglycans."
FT /evidence="ECO:0000269|PubMed:21147778"
FT MUTAGEN 370
FT /note="K->I: Prefers unsulfated glycosaminoglycans compared
FT to sulfated glycosaminoglycans."
FT /evidence="ECO:0000269|PubMed:21147778"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 26..47
FT /evidence="ECO:0007829|PDB:3WUX"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:3WUX"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:3ANI"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3ANJ"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:3WUX"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:3WUX"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3WUX"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3ANJ"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:3WUX"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:3WUX"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3WUX"
FT TURN 366..369
FT /evidence="ECO:0007829|PDB:3WUX"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3WUX"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:3WUX"
SQ SEQUENCE 398 AA; 46587 MW; 6554A85BE6A0E15D CRC64;
MMKIKPVKVE SIENPKRFLN SRLLTKIEVE EAIEKALKQL YINIDYFGEE YPTPATFNNI
YKVMDNTEWT NGFWTGCLWL AYEYNQDKKL KNIAHKNVLS FLNRINNRIA LDHHDLGFLY
TPSCTAEYRI NGDVKALEAT IKAADKLMER YQEKGGFIQA WGELGYKEHY RLIIDCLLNI
QLLFFAYEQT GDEKYRQVAV NHFYASANNV VRDDSSAFHT FYFDPETGEP LKGVTRQGYS
DESSWARGQA WGIYGIPLSY RKMKDYQQII LFKGMTNYFL NRLPEDKVSY WDLIFTDGSG
QPRDTSATAT AVCGIHEMLK YLPEVDPDKE TYKYAMHTML RSLIEQYSNN ELIAGRPLLL
HGVYSWHSGK GVDEGNIWGD YYYLEALIRF YKDWELYW
