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Protein

Reducing end xylose-releasing exo-oligoxylanase

Gene

BH2105

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes xylooligosaccharides with a degree of polymerization of greater than or equal to 3, releasing xylose from the reducing end. Only hydrolyzes the beta anomers of xylooligosaccharides, with inversion of anomeric configuration. Hydrolyzes the glucose and xylose-based trisaccharides where xylose is located at the -1 subsite, GXX, XXG and GXG. Does not hydrolyze xylan, chitosan, lichenan, curdlan or carboxymethylcellulose.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides.1 Publication

Kineticsi

  1. KM=2.4 mM for X3 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  2. KM=5.0 mM for X4 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  3. KM=4.4 mM for X5 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  4. KM=18.5 mM for X6 (in 50 mM sodium phosphate, pH 7.1, 40 degrees Celsius)2 Publications
  5. KM=4.3 mM for X3 (in 0.1 M MOPS, pH 7.0, 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 6.2-7.3. Stable between pH 5.0 and 9.8 for 30 min at 30 degrees Celsius.2 Publications

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius. Stable up to 40 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei70Proton donorBy similarity1
    Active sitei128NucleophileBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17885.
    BRENDAi3.2.1.156. 661.

    Protein family/group databases

    CAZyiGH8. Glycoside Hydrolase Family 8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Reducing end xylose-releasing exo-oligoxylanase1 Publication (EC:3.2.1.156)
    Short name:
    Rex1 Publication
    Gene namesi
    Ordered Locus Names:BH2105
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001258 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70E → A: Activity is 0.01% of wild type. 1 Publication1
    Mutagenesisi128D → A: Activity is 0.4% of wild type. 1 Publication1
    Mutagenesisi198Y → F: Has high levels of glycosynthase activity. Reduced hydrolase activity. 1 Publication1
    Mutagenesisi263D → A: Activity is 0.02% of wild type. Has glycosynthase activity. 3 Publications1
    Mutagenesisi263D → C or N: Has high levels of glycosynthase activity. Reduced hydrolase activity. 3 Publications1
    Mutagenesisi263D → G, L, P, S, T or V: Has glycosynthase activity. 3 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003972351 – 388Reducing end xylose-releasing exo-oligoxylanaseAdd BLAST388

    Interactioni

    Protein-protein interaction databases

    STRINGi272558.BH2105.

    Structurei

    Secondary structure

    1388
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi8 – 11Combined sources4
    Helixi17 – 20Combined sources4
    Helixi25 – 40Combined sources16
    Turni44 – 46Combined sources3
    Beta strandi49 – 52Combined sources4
    Turni53 – 55Combined sources3
    Beta strandi56 – 59Combined sources4
    Turni62 – 65Combined sources4
    Beta strandi66 – 68Combined sources3
    Helixi69 – 81Combined sources13
    Helixi85 – 98Combined sources14
    Beta strandi102 – 104Combined sources3
    Turni105 – 108Combined sources4
    Beta strandi112 – 114Combined sources3
    Helixi127 – 144Combined sources18
    Helixi154 – 167Combined sources14
    Beta strandi170 – 173Combined sources4
    Turni180 – 182Combined sources3
    Beta strandi192 – 194Combined sources3
    Helixi196 – 198Combined sources3
    Helixi201 – 210Combined sources10
    Helixi213 – 215Combined sources3
    Helixi216 – 233Combined sources18
    Turni236 – 238Combined sources3
    Beta strandi243 – 246Combined sources4
    Beta strandi249 – 251Combined sources3
    Beta strandi258 – 261Combined sources4
    Helixi262 – 265Combined sources4
    Helixi266 – 278Combined sources13
    Helixi282 – 295Combined sources14
    Helixi300 – 302Combined sources3
    Beta strandi304 – 306Combined sources3
    Beta strandi312 – 316Combined sources5
    Helixi320 – 329Combined sources10
    Helixi330 – 333Combined sources4
    Helixi340 – 348Combined sources9
    Helixi359 – 372Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WU4X-ray1.35A1-388[»]
    1WU5X-ray2.20A1-388[»]
    1WU6X-ray1.45A1-388[»]
    2DROX-ray1.70A1-388[»]
    2DRQX-ray2.10A1-388[»]
    2DRRX-ray1.60A1-388[»]
    2DRSX-ray2.10A1-388[»]
    3A3VX-ray1.39A1-388[»]
    ProteinModelPortaliQ9KB30.
    SMRiQ9KB30.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KB30.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 8 (cellulase D) family.Sequence analysis

    Phylogenomic databases

    eggNOGiENOG4105EK5. Bacteria.
    COG3405. LUCA.
    HOGENOMiHOG000112672.
    KOiK15531.
    OMAiSYGMMMA.
    OrthoDBiPOG091H07QZ.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR002037. Glyco_hydro_8.
    [Graphical view]
    PfamiPF01270. Glyco_hydro_8. 1 hit.
    [Graphical view]
    PRINTSiPR00735. GLHYDRLASE8.
    SUPFAMiSSF48208. SSF48208. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9KB30-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKTTEGAFY TREYRNLFKE FGYSEAEIQE RVKDTWEQLF GDNPETKIYY
    60 70 80 90 100
    EVGDDLGYLL DTGNLDVRTE GMSYGMMMAV QMDRKDIFDR IWNWTMKNMY
    110 120 130 140 150
    MTEGVHAGYF AWSCQPDGTK NSWGPAPDGE EYFALALFFA SHRWGDGDEQ
    160 170 180 190 200
    PFNYSEQARK LLHTCVHNGE GGPGHPMWNR DNKLIKFIPE VEFSDPSYHL
    210 220 230 240 250
    PHFYELFSLW ANEEDRVFWK EAAEASREYL KIACHPETGL APEYAYYDGT
    260 270 280 290 300
    PNDEKGYGHF FSDSYRVAAN IGLDAEWFGG SEWSAEEINK IQAFFADKEP
    310 320 330 340 350
    EDYRRYKIDG EPFEEKSLHP VGLIATNAMG SLASVDGPYA KANVDLFWNT
    360 370 380
    PVRTGNRRYY DNCLYLFAML ALSGNFKIWF PEGQEEEH
    Length:388
    Mass (Da):45,010
    Last modified:October 1, 2000 - v1
    Checksum:iC1EBA5B4A98C0E28
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti2K → E AA sequence (PubMed:15491996).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000004 Genomic DNA. Translation: BAB05824.1.
    AY137373 Genomic DNA. Translation: AAN16076.1.
    PIRiA83913.
    RefSeqiWP_010898262.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB05824; BAB05824; BAB05824.
    KEGGibha:BH2105.
    PATRICi18941366. VBIBacHal18977_2196.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000004 Genomic DNA. Translation: BAB05824.1.
    AY137373 Genomic DNA. Translation: AAN16076.1.
    PIRiA83913.
    RefSeqiWP_010898262.1. NC_002570.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1WU4X-ray1.35A1-388[»]
    1WU5X-ray2.20A1-388[»]
    1WU6X-ray1.45A1-388[»]
    2DROX-ray1.70A1-388[»]
    2DRQX-ray2.10A1-388[»]
    2DRRX-ray1.60A1-388[»]
    2DRSX-ray2.10A1-388[»]
    3A3VX-ray1.39A1-388[»]
    ProteinModelPortaliQ9KB30.
    SMRiQ9KB30.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi272558.BH2105.

    Protein family/group databases

    CAZyiGH8. Glycoside Hydrolase Family 8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB05824; BAB05824; BAB05824.
    KEGGibha:BH2105.
    PATRICi18941366. VBIBacHal18977_2196.

    Phylogenomic databases

    eggNOGiENOG4105EK5. Bacteria.
    COG3405. LUCA.
    HOGENOMiHOG000112672.
    KOiK15531.
    OMAiSYGMMMA.
    OrthoDBiPOG091H07QZ.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17885.
    BRENDAi3.2.1.156. 661.

    Miscellaneous databases

    EvolutionaryTraceiQ9KB30.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR002037. Glyco_hydro_8.
    [Graphical view]
    PfamiPF01270. Glyco_hydro_8. 1 hit.
    [Graphical view]
    PRINTSiPR00735. GLHYDRLASE8.
    SUPFAMiSSF48208. SSF48208. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiREOX_BACHD
    AccessioniPrimary (citable) accession number: Q9KB30
    Secondary accession number(s): Q8GLI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 10, 2010
    Last sequence update: October 1, 2000
    Last modified: November 2, 2016
    This is version 100 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, Complete proteome, Direct protein sequencing, Reference proteome

    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.