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 08-NOV-2023, entry version 82. 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; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; 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}. 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; 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 PaxDb; 1680-BADO_0309; -. 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; Six-hairpin glycosidases; 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 //