Reviewed, UniProtKB/Swiss-Prot Q9RC92 (UGL_BACGL)

Names and origin

Protein names

Recommended name:
    Unsaturated glucuronyl hydrolase
      Short name=UGL
    EC=3.2.1.-
Alternative name(s):
    Glycuronidase
    Unsaturated uronic acid hydrolase
    Glycosaminoglycan hydrolase

Gene names

Name:

ugl

Organism

Bacillus sp. (strain GL1)

Taxonomic identifier

84635 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Enzyme regulation	Partially inhibited by divalent metal ions such as calcium, copper, iron and mercury.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glycosyl hydrolase 88 family.
biophysicochemical properties	Kinetic parameters: At 30 degrees Celsius and pH 6.5. KM=90 µM for gellan lyase product KM=200 µM for chondroitin lyase product KM=226 µM for hyaluronate lyase product pH dependence: Optimum pH is 6.0-6.5. Temperature dependence: Optimum temperature is 45 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 377

377

Unsaturated glucuronyl hydrolase

PRO_0000171596

Sites

Active site

88

1

Nucleophile

Active site

149

1

Proton donor

Experimental info

Mutagenesis

88

1

D → N: Large decrease in activity, but no significant conformational change. Ref.2

Mutagenesis

149

1

D → N: Large decrease in activity, but no significant conformational change. Ref.2

Secondary structure

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377

Helix Strand Turn

Details...

Helix

3 – 20

18

Beta strand

24 – 39

16

Helix

44 – 58

15

Helix

61 – 80

20

Beta strand

85 – 87

3

Helix

89 – 94

6

Helix

97 – 104

8

Helix

107 – 120

14

Helix

121 – 123

3

Turn

126 – 128

3

Beta strand

129 – 131

3

Beta strand

134 – 136

3

Turn

140 – 144

5

Beta strand

145 – 147

3

Helix

148 – 153

6

Helix

154 – 164

11

Helix

168 – 183

16

Beta strand

193 – 197

5

Turn

199 – 201

3

Beta strand

204 – 208

5

Beta strand

210 – 214

5

Helix

220 – 237

18

Helix

240 – 254

15

Beta strand

264 – 266

3

Helix

279 – 294

16

Helix

301 – 320

20

Beta strand

332 – 334

3

Turn

340 – 343

4

Beta strand

344 – 348

5

Helix

351 – 366

16

Sequences

	Sequence		Length	Mass (Da)
	Q9RC92-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 430593BDE9216680	FASTA	377	42,861
	10 20 30 40 50 60 MWQQAIGDAL GITARNLKKF GDRFPHVSDG SNKYVLNDNT DWTDGFWSGI LWLCYEYTGD 70 80 90 100 110 120 EQYREGAVRT VASFRERLDR FENLDHHDIG FLYSLSAKAQ WIVEKDESAR KLALDAADVL 130 140 150 160 170 180 MRRWRADAGI IQAWGPKGDP ENGGRIIIDC LLNLPLLLWA GEQTGDPEYR RVAEAHALKS 190 200 210 220 230 240 RRFLVRGDDS SYHTFYFDPE NGNAIRGGTH QGNTDGSTWT RGQAWGIYGF ALNSRYLGNA 250 260 270 280 290 300 DLLETAKRMA RHFLARVPED GVVYWDFEVP QEPSSYRDSS ASAITACGLL EIASQLDESD 310 320 330 340 350 360 PERQRFIDAA KTTVTALRDG YAERDDGEAE GFIRRGSYHV RGGISPDDYT IWGDYYYLEA 370 LLRLERGVTG YWYERGR

References

[1]	"Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases." Hashimoto W., Kobayashi E., Nankai H., Sato N., Miya T., Kawai S., Murata K. Arch. Biochem. Biophys. 368:367-374(1999) [PubMed: 10441389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25, CHARACTERIZATION.
[2]	"Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution." Itoh T., Akao S., Hashimoto W., Mikami B., Murata K. J. Biol. Chem. 279:31804-31812(2004) [PubMed: 15148314] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF ASP-88 AND ASP-149.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB019619 Genomic DNA. Translation: BAA84216.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VD5	X-ray	1.80	A	1-377	[»]
2AHF	X-ray	1.52	A/B	1-377	[»]
2AHG	X-ray	1.90	A/B	1-377	[»]
2D5J	X-ray	1.60	A/B	1-377	[»]
2FUZ	X-ray	1.80	A	1-377	[»]
2FV0	X-ray	1.91	A/B	1-377	[»]
2FV1	X-ray	1.73	A/B	1-377	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH88. Glycoside Hydrolase Family 88.

Family and domain databases

InterPro

IPR012341. 6hp_glycosidase.
IPR010905. Glyco_hydro_88.
[Graphical view]

Gene3D

G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.

Pfam

PF07470. Glyco_hydro_88. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

UGL_BACGL

Accession

Primary (citable) accession number: Q9RC92

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)