REOX_ALKHC
ID REOX_ALKHC Reviewed; 388 AA.
AC Q9KB30; Q8GLI2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Reducing end xylose-releasing exo-oligoxylanase {ECO:0000303|PubMed:15491996};
DE Short=Rex {ECO:0000303|PubMed:15491996};
DE EC=3.2.1.156;
GN OrderedLocusNames=BH2105;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1] {ECO:0000312|EMBL:BAB05824.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF GLU-70; ASP-128 AND ASP-263.
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=15491996; DOI=10.1074/jbc.m409832200;
RA Honda Y., Kitaoka M.;
RT "A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is
RT a reducing end xylose-releasing exo-oligoxylanase.";
RL J. Biol. Chem. 279:55097-55103(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN16076.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-376.
RC STRAIN=MIR32 {ECO:0000312|EMBL:AAN16076.1};
RA Martinez M.A., Baigori M.D., Sineriz F.;
RT "Partial ORF identical to Xylanase Y from B. halodurans C-125.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-263.
RX PubMed=16301312; DOI=10.1074/jbc.m511202200;
RA Honda Y., Kitaoka M.;
RT "The first glycosynthase derived from an inverting glycoside hydrolase.";
RL J. Biol. Chem. 281:1426-1431(2006).
RN [5] {ECO:0000305}
RP MUTAGENESIS OF TYR-198 AND ASP-263.
RX PubMed=18263897; DOI=10.1093/glycob/cwn011;
RA Honda Y., Fushinobu S., Hidaka M., Wakagi T., Shoun H., Taniguchi H.,
RA Kitaoka M.;
RT "Alternative strategy for converting an inverting glycoside hydrolase into
RT a glycosynthase.";
RL Glycobiology 18:325-330(2008).
RN [6] {ECO:0000312|PDB:1WU4}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
RX PubMed=15718242; DOI=10.1074/jbc.m413693200;
RA Fushinobu S., Hidaka M., Honda Y., Wakagi T., Shoun H., Kitaoka M.;
RT "Structural basis for the specificity of the reducing end xylose-releasing
RT exo-oligoxylanase from Bacillus halodurans C-125.";
RL J. Biol. Chem. 280:17180-17186(2005).
CC -!- FUNCTION: Hydrolyzes xylooligosaccharides with a degree of
CC polymerization of greater than or equal to 3, releasing xylose from the
CC reducing end. Only hydrolyzes the beta anomers of xylooligosaccharides,
CC with inversion of anomeric configuration. Hydrolyzes the glucose and
CC xylose-based trisaccharides where xylose is located at the -1 subsite,
CC GXX, XXG and GXG. Does not hydrolyze xylan, chitosan, lichenan, curdlan
CC or carboxymethylcellulose. {ECO:0000269|PubMed:15491996}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylose residues from the reducing
CC end of oligosaccharides.; EC=3.2.1.156;
CC Evidence={ECO:0000269|PubMed:15491996};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for X3 (in 50 mM sodium phosphate, pH 7.1, 40 degrees
CC Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC KM=5.0 mM for X4 (in 50 mM sodium phosphate, pH 7.1, 40 degrees
CC Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC KM=4.4 mM for X5 (in 50 mM sodium phosphate, pH 7.1, 40 degrees
CC Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC KM=18.5 mM for X6 (in 50 mM sodium phosphate, pH 7.1, 40 degrees
CC Celsius) {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC KM=4.3 mM for X3 (in 0.1 M MOPS, pH 7.0, 30 degrees Celsius)
CC {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC pH dependence:
CC Optimum pH is 6.2-7.3. Stable between pH 5.0 and 9.8 for 30 min at 30
CC degrees Celsius. {ECO:0000269|PubMed:15491996,
CC ECO:0000269|PubMed:16301312};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Stable up to 40 degrees
CC Celsius. {ECO:0000269|PubMed:15491996, ECO:0000269|PubMed:16301312};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000004; BAB05824.1; -; Genomic_DNA.
DR EMBL; AY137373; AAN16076.1; -; Genomic_DNA.
DR PIR; A83913; A83913.
DR RefSeq; WP_010898262.1; NC_002570.2.
DR PDB; 1WU4; X-ray; 1.35 A; A=1-388.
DR PDB; 1WU5; X-ray; 2.20 A; A=1-388.
DR PDB; 1WU6; X-ray; 1.45 A; A=1-388.
DR PDB; 2DRO; X-ray; 1.70 A; A=1-388.
DR PDB; 2DRQ; X-ray; 2.10 A; A=1-388.
DR PDB; 2DRR; X-ray; 1.60 A; A=1-388.
DR PDB; 2DRS; X-ray; 2.10 A; A=1-388.
DR PDB; 3A3V; X-ray; 1.39 A; A=1-388.
DR PDBsum; 1WU4; -.
DR PDBsum; 1WU5; -.
DR PDBsum; 1WU6; -.
DR PDBsum; 2DRO; -.
DR PDBsum; 2DRQ; -.
DR PDBsum; 2DRR; -.
DR PDBsum; 2DRS; -.
DR PDBsum; 3A3V; -.
DR AlphaFoldDB; Q9KB30; -.
DR SMR; Q9KB30; -.
DR STRING; 272558.10174724; -.
DR DrugBank; DB03389; alpha-D-Xylopyranose.
DR CAZy; GH8; Glycoside Hydrolase Family 8.
DR EnsemblBacteria; BAB05824; BAB05824; BAB05824.
DR KEGG; bha:BH2105; -.
DR eggNOG; COG3405; Bacteria.
DR HOGENOM; CLU_037722_0_0_9; -.
DR OMA; FDRLWKW; -.
DR OrthoDB; 636673at2; -.
DR BioCyc; MetaCyc:MON-17885; -.
DR BRENDA; 3.2.1.156; 661.
DR EvolutionaryTrace; Q9KB30; -.
DR Proteomes; UP000001258; Chromosome.
DR GO; GO:0033951; F:oligosaccharide reducing-end xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002037; Glyco_hydro_8.
DR Pfam; PF01270; Glyco_hydro_8; 1.
DR PRINTS; PR00735; GLHYDRLASE8.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Xylan degradation.
FT CHAIN 1..388
FT /note="Reducing end xylose-releasing exo-oligoxylanase"
FT /id="PRO_0000397235"
FT ACT_SITE 70
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A0S2UQQ5"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0S2UQQ5"
FT MUTAGEN 70
FT /note="E->A: Activity is 0.01% of wild type."
FT /evidence="ECO:0000269|PubMed:15491996"
FT MUTAGEN 128
FT /note="D->A: Activity is 0.4% of wild type."
FT /evidence="ECO:0000269|PubMed:15491996"
FT MUTAGEN 198
FT /note="Y->F: Has high levels of glycosynthase activity.
FT Reduced hydrolase activity."
FT /evidence="ECO:0000269|PubMed:18263897"
FT MUTAGEN 263
FT /note="D->A: Activity is 0.02% of wild type. Has
FT glycosynthase activity."
FT /evidence="ECO:0000269|PubMed:15491996,
FT ECO:0000269|PubMed:16301312, ECO:0000269|PubMed:18263897"
FT MUTAGEN 263
FT /note="D->C,N: Has high levels of glycosynthase activity.
FT Reduced hydrolase activity."
FT /evidence="ECO:0000269|PubMed:15491996,
FT ECO:0000269|PubMed:16301312, ECO:0000269|PubMed:18263897"
FT MUTAGEN 263
FT /note="D->G,L,P,S,T,V: Has glycosynthase activity."
FT /evidence="ECO:0000269|PubMed:15491996,
FT ECO:0000269|PubMed:16301312, ECO:0000269|PubMed:18263897"
FT CONFLICT 2
FT /note="K -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:1WU4"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3A3V"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1WU4"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1WU4"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1WU5"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1WU4"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:1WU4"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1WU4"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:1WU4"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:1WU4"
SQ SEQUENCE 388 AA; 45010 MW; C1EBA5B4A98C0E28 CRC64;
MKKTTEGAFY TREYRNLFKE FGYSEAEIQE RVKDTWEQLF GDNPETKIYY EVGDDLGYLL
DTGNLDVRTE GMSYGMMMAV QMDRKDIFDR IWNWTMKNMY MTEGVHAGYF AWSCQPDGTK
NSWGPAPDGE EYFALALFFA SHRWGDGDEQ PFNYSEQARK LLHTCVHNGE GGPGHPMWNR
DNKLIKFIPE VEFSDPSYHL PHFYELFSLW ANEEDRVFWK EAAEASREYL KIACHPETGL
APEYAYYDGT PNDEKGYGHF FSDSYRVAAN IGLDAEWFGG SEWSAEEINK IQAFFADKEP
EDYRRYKIDG EPFEEKSLHP VGLIATNAMG SLASVDGPYA KANVDLFWNT PVRTGNRRYY
DNCLYLFAML ALSGNFKIWF PEGQEEEH
