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   25-MAY-2022, entry version 77.
DE   RecName: Full=Reducing end xylose-releasing exo-oligoxylanase {ECO:0000303|PubMed:17586675};
DE            Short=RexA {ECO:0000303|PubMed:17586675};
DE            EC=3.2.1.156;
GN   Name=xylA {ECO:0000312|EMBL:AAO67498.1}; OrderedLocusNames=BAD_0300;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1] {ECO:0000312|EMBL:AAO67498.1}
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., McCleary B.V.,
RA   Voragen A.G.;
RT   "Cloning and characterization of arabinoxylan arabinofuranohydrolase-D3
RT   (AXHd3) from Bifidobacterium adolescentis DSM20083.";
RL   Appl. Microbiol. Biotechnol. 67:641-647(2005).
RN   [2] {ECO:0000312|EMBL:BAF39081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
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 from the
CC       reducing end. Has low activity on birchwood xylan, oat spelt xylan and
CC       arabinoxylan. {ECO:0000269|PubMed:17586675}.
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:17586675};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. Stable between pH 4.0 and 10.0 for 120 minutes.
CC         {ECO:0000269|PubMed:17586675};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Stable up to 40 degrees
CC         Celsius. {ECO:0000269|PubMed:17586675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000255}.
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DR   EMBL; AY233379; AAO67498.1; -; Genomic_DNA.
DR   EMBL; AP009256; BAF39081.1; -; Genomic_DNA.
DR   RefSeq; WP_004220042.1; NC_008618.1.
DR   AlphaFoldDB; A1A048; -.
DR   SMR; A1A048; -.
DR   STRING; 1680.BADO_0309; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   PRIDE; A1A048; -.
DR   EnsemblBacteria; BAF39081; BAF39081; BAD_0300.
DR   KEGG; bad:BAD_0300; -.
DR   HOGENOM; CLU_037722_0_0_11; -.
DR   OMA; FDRLWKW; -.
DR   BRENDA; 3.2.1.156; 842.
DR   Proteomes; UP000008702; 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   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Xylan degradation.
FT   CHAIN           1..379
FT                   /note="Reducing end xylose-releasing exo-oligoxylanase"
FT                   /id="PRO_0000397236"
FT   ACT_SITE        66
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0S2UQQ5"
FT   ACT_SITE        259
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0S2UQQ5"
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