ID   UGL_BACGL               Reviewed;         377 AA.
AC   Q9RC92;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=Unsaturated glucuronyl hydrolase;
DE            Short=UGL;
DE            EC=3.2.1.179 {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
DE   AltName: Full=Glycosaminoglycan hydrolase;
DE   AltName: Full=Glycuronidase;
DE   AltName: Full=Unsaturated uronic acid hydrolase;
GN   Name=ugl;
OS   Bacillus sp. (strain GL1).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=84635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=10441389; DOI=10.1006/abbi.1999.1305;
RA   Hashimoto W., Kobayashi E., Nankai H., Sato N., Miya T., Kawai S.,
RA   Murata K.;
RT   "Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme
RT   prerequisite for metabolism of unsaturated oligosaccharides produced by
RT   polysaccharide lyases.";
RL   Arch. Biochem. Biophys. 368:367-374(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP   AND MUTAGENESIS OF HIS-339; GLY-342 AND ILE-344.
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   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS OF ASP-88 AND
RP   ASP-149.
RX   PubMed=15148314; DOI=10.1074/jbc.m403288200;
RA   Itoh T., Akao S., Hashimoto W., Mikami B., Murata K.;
RT   "Crystal structure of unsaturated glucuronyl hydrolase, responsible for the
RT   degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A
RT   resolution.";
RL   J. Biol. Chem. 279:31804-31812(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP   SUBSTRATES, AND REACTION MECHANISM.
RX   PubMed=16630576; DOI=10.1016/j.bbrc.2006.03.141;
RA   Itoh T., Hashimoto W., Mikami B., Murata K.;
RT   "Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus
RT   sp. GL1.";
RL   Biochem. Biophys. Res. Commun. 344:253-262(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-88 IN
RP   COMPLEX WITH SUBSTRATE, MUTAGENESIS OF ASP-88, AND REACTION MECHANISM.
RX   PubMed=16893885; DOI=10.1074/jbc.m604975200;
RA   Itoh T., Hashimoto W., Mikami B., Murata K.;
RT   "Crystal structure of unsaturated glucuronyl hydrolase complexed with
RT   substrate: molecular insights into its catalytic reaction mechanism.";
RL   J. Biol. Chem. 281:29807-29816(2006).
CC   -!- FUNCTION: Catalyzes the hydrolysis of oligosaccharides with unsaturated
CC       glucuronyl residues at the non-reducing terminal, to a sugar or an
CC       amino sugar, and an unsaturated D-glucuronic acid (GlcA), which is
CC       nonenzymatically converted immediately to alpha-keto acid.
CC       {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Delta(4)-GlcA-(1->4)-beta-D-Glc-(1->4)-alpha-L-Rha-
CC         (1->3)-D-Glc + H2O = beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc + 5-
CC         dehydro-4-deoxy-D-glucuronate; Xref=Rhea:RHEA:31635,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17117, ChEBI:CHEBI:134389,
CC         ChEBI:CHEBI:134390; EC=3.2.1.179;
CC         Evidence={ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC   -!- ACTIVITY REGULATION: Partially inhibited by divalent metal ions such as
CC       calcium, copper, iron and mercury.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.381 mM for unsaturated chondroitin disaccharidee (delta0S)
CC         {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC         KM=18.6 mM for unsaturated chondroitin disaccharide sulfated at C-6
CC         position of GalNAc residue (delta6S) {ECO:0000269|PubMed:10441389,
CC         ECO:0000269|PubMed:21147778};
CC         KM=90 uM for gellan lyase product (at 30 degrees Celsius and pH 6.5)
CC         {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC         KM=200 uM for chondroitin lyase product (at 30 degrees Celsius and pH
CC         6.5) {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC         KM=226 uM for hyaluronate lyase product (at 30 degrees Celsius and pH
CC         6.5) {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC         Note=kcat is 14.1 sec(-1) with unsaturated chondroitin (delta0S).
CC         kcat is 54.9 sec(-1) with unsaturated chondroitin disaccharide
CC         sulfated at C-6 position of GalNAc residue (delta6S).
CC         {ECO:0000269|PubMed:21147778};
CC       pH dependence:
CC         Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:10441389,
CC         ECO:0000269|PubMed:21147778};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10441389,
CC       ECO:0000269|PubMed:16893885}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 88 family. {ECO:0000305}.
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DR   EMBL; AB019619; BAA84216.1; -; Genomic_DNA.
DR   PDB; 1VD5; X-ray; 1.80 A; A=1-377.
DR   PDB; 2AHF; X-ray; 1.52 A; A/B=1-377.
DR   PDB; 2AHG; X-ray; 1.90 A; A/B=1-377.
DR   PDB; 2D5J; X-ray; 1.60 A; A/B=1-377.
DR   PDB; 2FUZ; X-ray; 1.80 A; A=1-377.
DR   PDB; 2FV0; X-ray; 1.91 A; A/B=1-377.
DR   PDB; 2FV1; X-ray; 1.73 A; A/B=1-377.
DR   AlphaFoldDB; Q9RC92; -.
DR   SMR; Q9RC92; -.
DR   DrugBank; DB04447; 1,4-Dithiothreitol.
DR   CAZy; GH88; Glycoside Hydrolase Family 88.
DR   KEGG; ag:BAA84216; -.
DR   BioCyc; MetaCyc:MONOMER-16269; -.
DR   BRENDA; 3.2.1.179; 691.
DR   EvolutionaryTrace; Q9RC92; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052757; F:chondroitin hydrolase activity; IEA:TreeGrafter.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:TreeGrafter.
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   InterPro; IPR052369; UG_Glycosaminoglycan_Hydrolase.
DR   PANTHER; PTHR36845; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G05090)-RELATED; 1.
DR   PANTHER; PTHR36845:SF1; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G05090)-RELATED; 1.
DR   Pfam; PF07470; Glyco_hydro_88; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PDBsum; 1VD5; -.
DR   PDBsum; 2AHF; -.
DR   PDBsum; 2AHG; -.
DR   PDBsum; 2D5J; -.
DR   PDBsum; 2FUZ; -.
DR   PDBsum; 2FV0; -.
DR   PDBsum; 2FV1; -.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cytoplasm;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..377
FT                   /note="Unsaturated glucuronyl hydrolase"
FT                   /id="PRO_0000171596"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:21147778"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:21147778"
FT   MUTAGEN         88
FT                   /note="D->N: No activity, but no significant conformational
FT                   change."
FT                   /evidence="ECO:0000269|PubMed:15148314,
FT                   ECO:0000269|PubMed:16893885"
FT   MUTAGEN         149
FT                   /note="D->N: Large decrease in activity, but no significant
FT                   conformational change."
FT                   /evidence="ECO:0000269|PubMed:15148314"
FT   MUTAGEN         339
FT                   /note="H->S: Shows higher affinity for unsaturated
FT                   chondroitin disaccharide sulfated at C-6 position of GalNAc
FT                   residue (delta6S)."
FT                   /evidence="ECO:0000269|PubMed:21147778"
FT   MUTAGEN         342
FT                   /note="G->S: Shows higher affinity for unsaturated
FT                   chondroitin disaccharide sulfated at C-6 position of GalNAc
FT                   residue (delta6S)."
FT                   /evidence="ECO:0000269|PubMed:21147778"
FT   MUTAGEN         344
FT                   /note="I->K: Shows higher affinity for unsaturated
FT                   chondroitin disaccharide sulfated at C-6 position of GalNAc
FT                   residue (delta6S)."
FT                   /evidence="ECO:0000269|PubMed:21147778"
FT   HELIX           3..20
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          24..39
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           44..58
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           61..78
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   TURN            79..83
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:2D5J"
FT   HELIX           89..93
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           94..98
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           99..104
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           107..121
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   TURN            140..144
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           148..153
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           168..183
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          210..214
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           220..237
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           240..254
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           279..294
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           301..320
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   TURN            340..343
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          344..348
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   HELIX           351..366
FT                   /evidence="ECO:0007829|PDB:2AHF"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:2FUZ"
SQ   SEQUENCE   377 AA;  42861 MW;  430593BDE9216680 CRC64;
     MWQQAIGDAL GITARNLKKF GDRFPHVSDG SNKYVLNDNT DWTDGFWSGI LWLCYEYTGD
     EQYREGAVRT VASFRERLDR FENLDHHDIG FLYSLSAKAQ WIVEKDESAR KLALDAADVL
     MRRWRADAGI IQAWGPKGDP ENGGRIIIDC LLNLPLLLWA GEQTGDPEYR RVAEAHALKS
     RRFLVRGDDS SYHTFYFDPE NGNAIRGGTH QGNTDGSTWT RGQAWGIYGF ALNSRYLGNA
     DLLETAKRMA RHFLARVPED GVVYWDFEVP QEPSSYRDSS ASAITACGLL EIASQLDESD
     PERQRFIDAA KTTVTALRDG YAERDDGEAE GFIRRGSYHV RGGISPDDYT IWGDYYYLEA
     LLRLERGVTG YWYERGR
//