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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei70 – 701Proton donorBy similarity
    Active sitei128 – 1281NucleophileBy similarity

    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

    BioCyciBHAL272558:GJC5-2189-MONOMER.
    MetaCyc: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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701E → A: Activity is 0.01% of wild type. 1 Publication
    Mutagenesisi128 – 1281D → A: Activity is 0.4% of wild type. 1 Publication
    Mutagenesisi198 – 1981Y → F: Has high levels of glycosynthase activity. Reduced hydrolase activity. 1 Publication
    Mutagenesisi263 – 2631D → A: Activity is 0.02% of wild type. Has glycosynthase activity. 3 Publications
    Mutagenesisi263 – 2631D → C or N: Has high levels of glycosynthase activity. Reduced hydrolase activity. 3 Publications
    Mutagenesisi263 – 2631D → G, L, P, S, T or V: Has glycosynthase activity. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 388388Reducing end xylose-releasing exo-oligoxylanasePRO_0000397235Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272558.BH2105.

    Structurei

    Secondary structure

    1
    388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Helixi17 – 204Combined sources
    Helixi25 – 4016Combined sources
    Turni44 – 463Combined sources
    Beta strandi49 – 524Combined sources
    Turni53 – 553Combined sources
    Beta strandi56 – 594Combined sources
    Turni62 – 654Combined sources
    Beta strandi66 – 683Combined sources
    Helixi69 – 8113Combined sources
    Helixi85 – 9814Combined sources
    Beta strandi102 – 1043Combined sources
    Turni105 – 1084Combined sources
    Beta strandi112 – 1143Combined sources
    Helixi127 – 14418Combined sources
    Helixi154 – 16714Combined sources
    Beta strandi170 – 1734Combined sources
    Turni180 – 1823Combined sources
    Beta strandi192 – 1943Combined sources
    Helixi196 – 1983Combined sources
    Helixi201 – 21010Combined sources
    Helixi213 – 2153Combined sources
    Helixi216 – 23318Combined sources
    Turni236 – 2383Combined sources
    Beta strandi243 – 2464Combined sources
    Beta strandi249 – 2513Combined sources
    Beta strandi258 – 2614Combined sources
    Helixi262 – 2654Combined sources
    Helixi266 – 27813Combined sources
    Helixi282 – 29514Combined sources
    Helixi300 – 3023Combined sources
    Beta strandi304 – 3063Combined sources
    Beta strandi312 – 3165Combined sources
    Helixi320 – 32910Combined sources
    Helixi330 – 3334Combined sources
    Helixi340 – 3489Combined sources
    Helixi359 – 37214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 6-381.
    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.
    OrthoDBiEOG62G5M5.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21K → E AA sequence (PubMed:15491996).Curated

    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
    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. Positions 6-381.
    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.
    OrthoDBiEOG62G5M5.

    Enzyme and pathway databases

    BioCyciBHAL272558:GJC5-2189-MONOMER.
    MetaCyc: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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    2. "A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase."
      Honda Y., Kitaoka M.
      J. Biol. Chem. 279:55097-55103(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-70; ASP-128 AND ASP-263.
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    3. "Partial ORF identical to Xylanase Y from B. halodurans C-125."
      Martinez M.A., Baigori M.D., Sineriz F.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-376.
      Strain: MIR32Imported.
    4. "The first glycosynthase derived from an inverting glycoside hydrolase."
      Honda Y., Kitaoka M.
      J. Biol. Chem. 281:1426-1431(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-263.
    5. "Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase."
      Honda Y., Fushinobu S., Hidaka M., Wakagi T., Shoun H., Taniguchi H., Kitaoka M.
      Glycobiology 18:325-330(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-198 AND ASP-263.
    6. "Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125."
      Fushinobu S., Hidaka M., Honda Y., Wakagi T., Shoun H., Kitaoka M.
      J. Biol. Chem. 280:17180-17186(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).

    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: January 20, 2016
    This is version 97 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.