UCDH_STRP1
ID UCDH_STRP1 Reviewed; 399 AA.
AC Q9A0T3; Q48ZS8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Unsaturated chondroitin disaccharide hydrolase;
DE EC=3.2.1.180;
DE AltName: Full=Unsaturated glucuronyl hydrolase;
DE Short=SpyUGL;
GN Name=ugl; OrderedLocusNames=SPy_0632, M5005_Spy0522;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
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).
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}.
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};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for unsaturated chondroitin disaccharide sulfated at C-6
CC position of GalNAc residue {ECO:0000269|PubMed:19416976};
CC Note=kcat is 4 sec(-1) with unsaturated chondroitin disaccharide
CC sulfated at C-6 position of GalNAc residue.;
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 88 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004092; AAK33600.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ51140.1; -; Genomic_DNA.
DR RefSeq; NP_268879.1; NC_002737.2.
DR AlphaFoldDB; Q9A0T3; -.
DR SMR; Q9A0T3; -.
DR STRING; 1314.HKU360_00533; -.
DR CAZy; GH88; Glycoside Hydrolase Family 88.
DR PaxDb; Q9A0T3; -.
DR EnsemblBacteria; AAK33600; AAK33600; SPy_0632.
DR KEGG; spy:SPy_0632; -.
DR KEGG; spz:M5005_Spy0522; -.
DR PATRIC; fig|160490.10.peg.537; -.
DR HOGENOM; CLU_027158_1_1_9; -.
DR OMA; YWDLIFG; -.
DR BRENDA; 3.2.1.180; 5935.
DR Proteomes; UP000000750; 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 Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..399
FT /note="Unsaturated chondroitin disaccharide hydrolase"
FT /id="PRO_0000422018"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 46100 MW; 3FADBA02DE6A8411 CRC64;
MARPLKTIAL EPIKQPERFT KEDFLSQEDI TQALDLALKQ VRLNMDYFKE DFPTPATKDN
QYAIMDNTEW TNAFWTGCLW LAYEYSGDDA IKALAQANDL SFLDRVTRDI ELDHHDLGFL
YTPSCMAEWK LLKTPESREA ALKAADKLVQ RYQDKGGFIQ AWGELGKKED YRLIIDCLLN
IQLLFFASQE TGDNRYRDMA INHFYASANH VIRDDASAYH TFYFDPETGD PVKGVTRQGY
SDDSAWARGQ AWGIYGIPLT YRFLKEPELI QLFKGMTHYF LNRLPKDQVS YWDLIFGDGS
EQSRDSSATA IAVCGIHEML KTLPDHDPDK KTYEAAMHSM LRALIKDYAN KDLKPGAPLL
LHGVYSWHSG KGVDEGNIWG DYYYLEALLR FYKDWNPYW
