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Protein

Unsaturated glucuronyl hydrolase

Gene

ugl

Organism
Bacillus sp. (strain GL1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O = 5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp.2 Publications

Enzyme regulationi

Partially inhibited by divalent metal ions such as calcium, copper, iron and mercury.

Kineticsi

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).1 Publication

Manual assertion based on experiment ini

  1. KM=0.381 mM for unsaturated chondroitin disaccharidee (delta0S)2 Publications
  2. KM=18.6 mM for unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S)2 Publications
  3. KM=90 µM for gellan lyase product (at 30 degrees Celsius and pH 6.5)2 Publications
  4. KM=200 µM for chondroitin lyase product (at 30 degrees Celsius and pH 6.5)2 Publications
  5. KM=226 µM for hyaluronate lyase product (at 30 degrees Celsius and pH 6.5)2 Publications

    pH dependencei

    Optimum pH is 6.0-6.5.2 Publications

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei88Nucleophile1 Publication1
    Active sitei149Proton donor1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16269.
    BRENDAi3.2.1.179. 691.

    Protein family/group databases

    CAZyiGH88. Glycoside Hydrolase Family 88.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unsaturated glucuronyl hydrolase (EC:3.2.1.179)
    Short name:
    UGL
    Alternative name(s):
    Glycosaminoglycan hydrolase
    Glycuronidase
    Unsaturated uronic acid hydrolase
    Gene namesi
    Name:ugl
    OrganismiBacillus sp. (strain GL1)
    Taxonomic identifieri84635 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi88D → N: No activity, but no significant conformational change. 2 Publications1
    Mutagenesisi149D → N: Large decrease in activity, but no significant conformational change. 1 Publication1
    Mutagenesisi339H → S: Shows higher affinity for unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S). 1 Publication1
    Mutagenesisi342G → S: Shows higher affinity for unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S). 1 Publication1
    Mutagenesisi344I → K: Shows higher affinity for unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S). 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001715961 – 377Unsaturated glucuronyl hydrolaseAdd BLAST377

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1377
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 20Combined sources18
    Beta strandi24 – 39Combined sources16
    Helixi44 – 58Combined sources15
    Helixi61 – 78Combined sources18
    Turni79 – 83Combined sources5
    Beta strandi85 – 87Combined sources3
    Helixi89 – 94Combined sources6
    Helixi97 – 104Combined sources8
    Helixi107 – 121Combined sources15
    Turni126 – 129Combined sources4
    Beta strandi134 – 136Combined sources3
    Turni140 – 144Combined sources5
    Beta strandi145 – 147Combined sources3
    Helixi148 – 153Combined sources6
    Helixi154 – 164Combined sources11
    Helixi168 – 183Combined sources16
    Beta strandi193 – 197Combined sources5
    Turni199 – 201Combined sources3
    Beta strandi204 – 208Combined sources5
    Beta strandi210 – 214Combined sources5
    Helixi220 – 237Combined sources18
    Helixi240 – 254Combined sources15
    Beta strandi264 – 266Combined sources3
    Helixi279 – 294Combined sources16
    Helixi301 – 320Combined sources20
    Beta strandi332 – 334Combined sources3
    Turni340 – 343Combined sources4
    Beta strandi344 – 348Combined sources5
    Helixi351 – 366Combined sources16
    Beta strandi371 – 373Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VD5X-ray1.80A1-377[»]
    2AHFX-ray1.52A/B1-377[»]
    2AHGX-ray1.90A/B1-377[»]
    2D5JX-ray1.60A/B1-377[»]
    2FUZX-ray1.80A1-377[»]
    2FV0X-ray1.91A/B1-377[»]
    2FV1X-ray1.73A/B1-377[»]
    ProteinModelPortaliQ9RC92.
    SMRiQ9RC92.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9RC92.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 88 family.Curated

    Phylogenomic databases

    KOiK20831.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR010905. Glyco_hydro_88.
    [Graphical view]
    PfamiPF07470. Glyco_hydro_88. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9RC92-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MWQQAIGDAL GITARNLKKF GDRFPHVSDG SNKYVLNDNT DWTDGFWSGI
    60 70 80 90 100
    LWLCYEYTGD EQYREGAVRT VASFRERLDR FENLDHHDIG FLYSLSAKAQ
    110 120 130 140 150
    WIVEKDESAR KLALDAADVL MRRWRADAGI IQAWGPKGDP ENGGRIIIDC
    160 170 180 190 200
    LLNLPLLLWA GEQTGDPEYR RVAEAHALKS RRFLVRGDDS SYHTFYFDPE
    210 220 230 240 250
    NGNAIRGGTH QGNTDGSTWT RGQAWGIYGF ALNSRYLGNA DLLETAKRMA
    260 270 280 290 300
    RHFLARVPED GVVYWDFEVP QEPSSYRDSS ASAITACGLL EIASQLDESD
    310 320 330 340 350
    PERQRFIDAA KTTVTALRDG YAERDDGEAE GFIRRGSYHV RGGISPDDYT
    360 370
    IWGDYYYLEA LLRLERGVTG YWYERGR
    Length:377
    Mass (Da):42,861
    Last modified:May 1, 2000 - v1
    Checksum:i430593BDE9216680
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB019619 Genomic DNA. Translation: BAA84216.1.

    Genome annotation databases

    KEGGiag:BAA84216.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB019619 Genomic DNA. Translation: BAA84216.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VD5X-ray1.80A1-377[»]
    2AHFX-ray1.52A/B1-377[»]
    2AHGX-ray1.90A/B1-377[»]
    2D5JX-ray1.60A/B1-377[»]
    2FUZX-ray1.80A1-377[»]
    2FV0X-ray1.91A/B1-377[»]
    2FV1X-ray1.73A/B1-377[»]
    ProteinModelPortaliQ9RC92.
    SMRiQ9RC92.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH88. Glycoside Hydrolase Family 88.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAA84216.

    Phylogenomic databases

    KOiK20831.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16269.
    BRENDAi3.2.1.179. 691.

    Miscellaneous databases

    EvolutionaryTraceiQ9RC92.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR010905. Glyco_hydro_88.
    [Graphical view]
    PfamiPF07470. Glyco_hydro_88. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiUGL_BACGL
    AccessioniPrimary (citable) accession number: Q9RC92
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: May 1, 2000
    Last modified: November 30, 2016
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.