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Unsaturated glucuronyl hydrolase (UGL) (EC 3.2.1.179) (Glycosaminoglycan hydrolase) (Glycuronidase) (Unsaturated uronic acid hydrolase)

 UGL_BACGL               Reviewed;         377 AA.
Q9RC92;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 64.
RecName: Full=Unsaturated glucuronyl hydrolase;
Short=UGL;
EC=3.2.1.179 {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
AltName: Full=Glycosaminoglycan hydrolase;
AltName: Full=Glycuronidase;
AltName: Full=Unsaturated uronic acid hydrolase;
Name=ugl;
Bacillus sp. (strain GL1).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=84635;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, FUNCTION,
CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10441389; DOI=10.1006/abbi.1999.1305;
Hashimoto W., Kobayashi E., Nankai H., Sato N., Miya T., Kawai S.,
Murata K.;
"Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme
prerequisite for metabolism of unsaturated oligosaccharides produced
by polysaccharide lyases.";
Arch. Biochem. Biophys. 368:367-374(1999).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE
SITE, AND MUTAGENESIS OF HIS-339; GLY-342 AND ILE-344.
PubMed=21147778; DOI=10.1074/jbc.M110.182618;
Nakamichi Y., Maruyama Y., Mikami B., Hashimoto W., Murata K.;
"Structural determinants in streptococcal unsaturated glucuronyl
hydrolase for recognition of glycosaminoglycan sulfate groups.";
J. Biol. Chem. 286:6262-6271(2011).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS OF ASP-88 AND
ASP-149.
PubMed=15148314; DOI=10.1074/jbc.M403288200;
Itoh T., Akao S., Hashimoto W., Mikami B., Murata K.;
"Crystal structure of unsaturated glucuronyl hydrolase, responsible
for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8
A resolution.";
J. Biol. Chem. 279:31804-31812(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF APOENZYME AND IN COMPLEXES
WITH SUBSTRATES, AND REACTION MECHANISM.
PubMed=16630576; DOI=10.1016/j.bbrc.2006.03.141;
Itoh T., Hashimoto W., Mikami B., Murata K.;
"Substrate recognition by unsaturated glucuronyl hydrolase from
Bacillus sp. GL1.";
Biochem. Biophys. Res. Commun. 344:253-262(2006).
[5]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-88
IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF ASP-88, AND REACTION
MECHANISM.
PubMed=16893885; DOI=10.1074/jbc.M604975200;
Itoh T., Hashimoto W., Mikami B., Murata K.;
"Crystal structure of unsaturated glucuronyl hydrolase complexed with
substrate: molecular insights into its catalytic reaction mechanism.";
J. Biol. Chem. 281:29807-29816(2006).
-!- FUNCTION: Catalyzes the hydrolysis of oligosaccharides with
unsaturated glucuronyl residues at the non-reducing terminal, to a
sugar or an amino sugar, and an unsaturated D-glucuronic acid
(GlcA), which is nonenzymatically converted immediately to alpha-
keto acid. {ECO:0000269|PubMed:10441389,
ECO:0000269|PubMed:21147778}.
-!- CATALYTIC ACTIVITY: Beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-
Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp + H(2)O = 5-dehydro-4-
deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-
Glcp. {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778}.
-!- ENZYME REGULATION: Partially inhibited by divalent metal ions such
as calcium, copper, iron and mercury.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.381 mM for unsaturated chondroitin disaccharidee (delta0S)
{ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
KM=18.6 mM for unsaturated chondroitin disaccharide sulfated at
C-6 position of GalNAc residue (delta6S)
{ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
KM=90 uM for gellan lyase product (at 30 degrees Celsius and pH
6.5) {ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
KM=200 uM for chondroitin lyase product (at 30 degrees Celsius
and pH 6.5) {ECO:0000269|PubMed:10441389,
ECO:0000269|PubMed:21147778};
KM=226 uM for hyaluronate lyase product (at 30 degrees Celsius
and pH 6.5) {ECO:0000269|PubMed:10441389,
ECO:0000269|PubMed:21147778};
Note=kcat is 14.1 sec(-1) with unsaturated chondroitin
(delta0S). kcat is 54.9 sec(-1) with unsaturated chondroitin
disaccharide sulfated at C-6 position of GalNAc residue
(delta6S). {ECO:0000269|PubMed:21147778};
pH dependence:
Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:10441389,
ECO:0000269|PubMed:21147778};
Temperature dependence:
Optimum temperature is 45 degrees Celsius.
{ECO:0000269|PubMed:10441389, ECO:0000269|PubMed:21147778};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10441389,
ECO:0000269|PubMed:16893885}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 88 family.
{ECO:0000305}.
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EMBL; AB019619; BAA84216.1; -; Genomic_DNA.
PDB; 1VD5; X-ray; 1.80 A; A=1-377.
PDB; 2AHF; X-ray; 1.52 A; A/B=1-377.
PDB; 2AHG; X-ray; 1.90 A; A/B=1-377.
PDB; 2D5J; X-ray; 1.60 A; A/B=1-377.
PDB; 2FUZ; X-ray; 1.80 A; A=1-377.
PDB; 2FV0; X-ray; 1.91 A; A/B=1-377.
PDB; 2FV1; X-ray; 1.73 A; A/B=1-377.
PDBsum; 1VD5; -.
PDBsum; 2AHF; -.
PDBsum; 2AHG; -.
PDBsum; 2D5J; -.
PDBsum; 2FUZ; -.
PDBsum; 2FV0; -.
PDBsum; 2FV1; -.
ProteinModelPortal; Q9RC92; -.
SMR; Q9RC92; -.
CAZy; GH88; Glycoside Hydrolase Family 88.
KEGG; ag:BAA84216; -.
KO; K20831; -.
BioCyc; MetaCyc:MONOMER-16269; -.
BRENDA; 3.2.1.179; 691.
EvolutionaryTrace; Q9RC92; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
Gene3D; 1.50.10.10; -; 1.
InterPro; IPR008928; 6-hairpin_glycosidase_sf.
InterPro; IPR012341; 6hp_glycosidase-like_sf.
InterPro; IPR010905; Glyco_hydro_88.
Pfam; PF07470; Glyco_hydro_88; 1.
SUPFAM; SSF48208; SSF48208; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Cytoplasm;
Direct protein sequencing; Glycosidase; Hydrolase;
Polysaccharide degradation.
CHAIN 1 377 Unsaturated glucuronyl hydrolase.
/FTId=PRO_0000171596.
ACT_SITE 88 88 Nucleophile.
{ECO:0000269|PubMed:21147778}.
ACT_SITE 149 149 Proton donor.
{ECO:0000269|PubMed:21147778}.
MUTAGEN 88 88 D->N: No activity, but no significant
conformational change.
{ECO:0000269|PubMed:15148314,
ECO:0000269|PubMed:16893885}.
MUTAGEN 149 149 D->N: Large decrease in activity, but no
significant conformational change.
{ECO:0000269|PubMed:15148314}.
MUTAGEN 339 339 H->S: Shows higher affinity for
unsaturated chondroitin disaccharide
sulfated at C-6 position of GalNAc
residue (delta6S).
{ECO:0000269|PubMed:21147778}.
MUTAGEN 342 342 G->S: Shows higher affinity for
unsaturated chondroitin disaccharide
sulfated at C-6 position of GalNAc
residue (delta6S).
{ECO:0000269|PubMed:21147778}.
MUTAGEN 344 344 I->K: Shows higher affinity for
unsaturated chondroitin disaccharide
sulfated at C-6 position of GalNAc
residue (delta6S).
{ECO:0000269|PubMed:21147778}.
HELIX 3 20 {ECO:0000244|PDB:2AHF}.
STRAND 24 39 {ECO:0000244|PDB:2AHF}.
HELIX 44 58 {ECO:0000244|PDB:2AHF}.
HELIX 61 78 {ECO:0000244|PDB:2AHF}.
TURN 79 83 {ECO:0000244|PDB:2AHF}.
STRAND 85 87 {ECO:0000244|PDB:2D5J}.
HELIX 89 94 {ECO:0000244|PDB:2AHF}.
HELIX 97 104 {ECO:0000244|PDB:2AHF}.
HELIX 107 121 {ECO:0000244|PDB:2AHF}.
TURN 126 129 {ECO:0000244|PDB:2AHF}.
STRAND 134 136 {ECO:0000244|PDB:2AHF}.
TURN 140 144 {ECO:0000244|PDB:2AHF}.
STRAND 145 147 {ECO:0000244|PDB:2AHF}.
HELIX 148 153 {ECO:0000244|PDB:2AHF}.
HELIX 154 164 {ECO:0000244|PDB:2AHF}.
HELIX 168 183 {ECO:0000244|PDB:2AHF}.
STRAND 193 197 {ECO:0000244|PDB:2AHF}.
TURN 199 201 {ECO:0000244|PDB:2AHF}.
STRAND 204 208 {ECO:0000244|PDB:2AHF}.
STRAND 210 214 {ECO:0000244|PDB:2AHF}.
HELIX 220 237 {ECO:0000244|PDB:2AHF}.
HELIX 240 254 {ECO:0000244|PDB:2AHF}.
STRAND 264 266 {ECO:0000244|PDB:2AHF}.
HELIX 279 294 {ECO:0000244|PDB:2AHF}.
HELIX 301 320 {ECO:0000244|PDB:2AHF}.
STRAND 332 334 {ECO:0000244|PDB:2AHF}.
TURN 340 343 {ECO:0000244|PDB:2AHF}.
STRAND 344 348 {ECO:0000244|PDB:2AHF}.
HELIX 351 366 {ECO:0000244|PDB:2AHF}.
STRAND 371 373 {ECO:0000244|PDB:2FUZ}.
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


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