ID   REOX_BIFAA              Reviewed;         379 AA.
AC   A1A048; Q5JB57;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   30-NOV-2010, entry version 23.
DE   RecName: Full=Reducing end xylose-releasing exo-oligoxylanase;
DE            Short=RexA;
DE            EC=3.2.1.156;
GN   Name=xylA; OrderedLocusNames=BAD_0300;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15650848; DOI=10.1007/s00253-004-1850-9;
RA   van den Broek L.A., Lloyd R.M., Beldman G., Verdoes J.C.,
RA   McCleary B.V., Voragen A.G.;
RT   "Cloning and characterization of arabinoxylan arabinofuranohydrolase-
RT   D3 (AXHd3) from Bifidobacterium adolescentis DSM20083.";
RL   Appl. Microbiol. Biotechnol. 67:641-647(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S.,
RA   Hirai S., Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17586675; DOI=10.1128/AEM.00722-07;
RA   Lagaert S., Van Campenhout S., Pollet A., Bourgois T.M., Delcour J.A.,
RA   Courtin C.M., Volckaert G.;
RT   "Recombinant expression and characterization of a reducing-end xylose-
RT   releasing exo-oligoxylanase from Bifidobacterium adolescentis.";
RL   Appl. Environ. Microbiol. 73:5374-5377(2007).
CC   -!- FUNCTION: Hydrolyzes xylooligosaccharides with a degree of
CC       polymerization of greater than or equal to 3, releasing xylose
CC       from the reducing end. Has low activity on birchwood xylan, oat
CC       spelt xylan and arabinoxylan.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-xylose residues
CC       from the reducing end of oligosaccharides.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. Stable between pH 4.0 and 10.0 for 120
CC         minutes;
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Stable up to 40
CC         degrees Celsius;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D)
CC       family.
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DR   EMBL; AY233379; AAO67498.1; -; Genomic_DNA.
DR   EMBL; AP009256; BAF39081.1; -; Genomic_DNA.
DR   RefSeq; YP_909163.1; NC_008618.1.
DR   ProteinModelPortal; A1A048; -.
DR   SMR; A1A048; 14-378.
DR   STRING; A1A048; -.
DR   GeneID; 4556993; -.
DR   GenomeReviews; AP009256_GR; BAD_0300.
DR   KEGG; bad:BAD_0300; -.
DR   NMPDR; fig|1680.3.peg.562; -.
DR   eggNOG; COG3405; -.
DR   HOGENOM; HBG424335; -.
DR   OMA; PSYHLPH; -.
DR   ProtClustDB; CLSK873228; -.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl ...; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR012341; 6hp_glycosidase.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   Gene3D; G3DSA:1.50.10.10; CelA/Cel48F_cat; 1.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Xylan degradation.
FT   CHAIN         1    379       Reducing end xylose-releasing exo-
FT                                oligoxylanase.
FT                                /FTId=PRO_0000397236.
FT   ACT_SITE     66     66       Proton donor (By similarity).
FT   ACT_SITE    124    124       Nucleophile (By similarity).
SQ   SEQUENCE   379 AA;  43785 MW;  C82283D2D1168A46 CRC64;
     MTNATDTNKT LGESMFAQCG YAQDAIDKRV SQVWHEIFEG PNKFYWENDE GLAYVMDTGN
     NDVRTEGMSY AMMIALQYDR KDVFDKLWGW VMRHMYMKDG HHAHYFAWSV APDGTPNSNG
     PAPDGEEYFA MDLFLASRRW GDGEDIYEYS AWGREILRYC VHKGERYDGE PMWNPDNKLI
     KFIPETEWSD PSYHLPHFYE VFAEEADEED RPFWHEAAAA SRRYLQAACD ERTGMNAEYA
     DYDGKPHVDE SNHWHFYSDA YRTAANIGLD AAWNGPQEVL CDRVAALQRF FLTHDRTSVY
     AIDGTAVDEV VLHPVGFLAA TAQGALAAVH SAQPDAEHNA REWVRMLWNT PMRTGTRRYY
     DNFLYAFAML ALSGKYRYE
//