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 28-MAR-2018, entry version 63. 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 OS 11814 / 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., 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] {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., 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] {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 CC from the reducing end. Has low activity on birchwood xylan, oat CC spelt xylan and arabinoxylan. {ECO:0000269|PubMed:17586675}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-D-xylose residues CC from the reducing end of oligosaccharides. CC {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 CC minutes. {ECO:0000269|PubMed:17586675}; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. Stable up to 40 CC degrees Celsius. {ECO:0000269|PubMed:17586675}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) CC family. {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 ProteinModelPortal; A1A048; -. DR SMR; A1A048; -. DR STRING; 367928.BAD_0300; -. DR CAZy; GH8; Glycoside Hydrolase Family 8. DR EnsemblBacteria; BAF39081; BAF39081; BAD_0300. DR GeneID; 4556993; -. DR KEGG; bad:BAD_0300; -. DR eggNOG; ENOG4105EK5; Bacteria. DR eggNOG; COG3405; LUCA. DR HOGENOM; HOG000112672; -. DR KO; K15531; -. DR OMA; FDRLWKW; -. DR OrthoDB; POG091H07QZ; -. 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; Complete proteome; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Xylan degradation. FT CHAIN 1 379 Reducing end xylose-releasing exo- FT oligoxylanase. FT /FTId=PRO_0000397236. FT ACT_SITE 66 66 Proton donor. FT {ECO:0000250|UniProtKB:A3DC29}. FT ACT_SITE 124 124 Nucleophile. FT {ECO:0000250|UniProtKB:A3DC29}. 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 //