UCDH_STRR6
ID UCDH_STRR6 Reviewed; 396 AA.
AC Q8DR77;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Unsaturated chondroitin disaccharide hydrolase;
DE EC=3.2.1.180;
DE AltName: Full=Unsaturated glucuronyl hydrolase;
DE Short=SpnUGL;
GN Name=ugl; OrderedLocusNames=spr0292;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-255 / R6;
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=0.18 mM for unsaturated chondroitin disaccharide sulfated at C-6
CC position of GalNAc residue {ECO:0000269|PubMed:19416976};
CC Note=kcat is 1.3 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}.
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DR EMBL; AE007317; AAK99096.1; -; Genomic_DNA.
DR PIR; A95038; A95038.
DR PIR; D97908; D97908.
DR RefSeq; NP_357886.1; NC_003098.1.
DR RefSeq; WP_000592948.1; NC_003098.1.
DR AlphaFoldDB; Q8DR77; -.
DR SMR; Q8DR77; -.
DR STRING; 171101.spr0292; -.
DR CAZy; GH88; Glycoside Hydrolase Family 88.
DR EnsemblBacteria; AAK99096; AAK99096; spr0292.
DR GeneID; 60234090; -.
DR KEGG; spr:spr0292; -.
DR PATRIC; fig|171101.6.peg.329; -.
DR eggNOG; COG4225; Bacteria.
DR HOGENOM; CLU_027158_1_1_9; -.
DR OMA; YWDLIFG; -.
DR BRENDA; 3.2.1.180; 1960.
DR Proteomes; UP000000586; 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 Hydrolase; Reference proteome.
FT CHAIN 1..396
FT /note="Unsaturated chondroitin disaccharide hydrolase"
FT /id="PRO_0000422017"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 46079 MW; 25FDF8DBE7B69A5A CRC64;
MIKKVTIEKI KSPERFLEVP LLTKEEVGQA IDKVIRQLEL NLDYFKEDFP TPATFDNVYP
IMDNTEWTNG FWTGELWLAY EYSQQDAFKN IAHKNVLSFL DRVNKRVELD HHDLGFLYTP
SCMAEYKING DGEAREATLK AADKLIERYQ EKGGFIQAWG DLGKKEHYRL IIDCLLNIQL
LFFAYQETGD QKYYDIAESH FYASANNVIR DDASSFHTFY FDPETGQPFK GVTRQGYSDD
SCWARGQSWG VYGIPLTYRH LKDESCFDLF KGVTNYFLNR LPKDHVSYWD LIFNDGSDQS
RDSSATAIAV CGIHEMLKHL PEVDADKDIY KHAMHAMLRS LIEHYANDQF TPGGTSLLHG
VYSWHSGKGV DEGNIWGDYY YLEALIRFYK DWNLYW
