UGL_BACGL
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 03-AUG-2022, entry version 76.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 = 5-dehydro-4-deoxy-D-glucuronate + beta-D-Glc-
CC (1->4)-alpha-L-Rha-(1->3)-D-Glc; 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 PDBsum; 1VD5; -.
DR PDBsum; 2AHF; -.
DR PDBsum; 2AHG; -.
DR PDBsum; 2D5J; -.
DR PDBsum; 2FUZ; -.
DR PDBsum; 2FV0; -.
DR PDBsum; 2FV1; -.
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:MON-16269; -.
DR BRENDA; 3.2.1.179; 691.
DR EvolutionaryTrace; Q9RC92; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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..94
FT /evidence="ECO:0007829|PDB:2AHF"
FT HELIX 97..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
