BXLB_ASPTN
ID BXLB_ASPTN Reviewed; 765 AA.
AC Q0CB82;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Probable exo-1,4-beta-xylosidase bxlB;
DE EC=3.2.1.37;
DE AltName: Full=1,4-beta-D-xylan xylohydrolase bxlB;
DE AltName: Full=Beta-xylosidase bxlB;
DE AltName: Full=Xylobiase bxlB;
DE Flags: Precursor;
GN Name=bxlB; ORFNames=ATEG_09052;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Xylan 1,4-beta-xylosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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; CH476607; EAU30189.1; -; Genomic_DNA.
DR RefSeq; XP_001217674.1; XM_001217673.1.
DR AlphaFoldDB; Q0CB82; -.
DR SMR; Q0CB82; -.
DR STRING; 341663.Q0CB82; -.
DR EnsemblFungi; EAU30189; EAU30189; ATEG_09052.
DR GeneID; 4354040; -.
DR VEuPathDB; FungiDB:ATEG_09052; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; DKVAMTD; -.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42721; PTHR42721; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..765
FT /note="Probable exo-1,4-beta-xylosidase bxlB"
FT /id="PRO_0000394090"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 765 AA; 82764 MW; 7B6D1E85A3EFEA87 CRC64;
MYSSNSRRAA SILACIVSLT QLGFAQSPFP DCENGPLSKN AVCDTTLDPV TRAQALLAAM
TLEEKINNTQ YNSPGVPRLG LPAYNWWSEA LHGVAGSPGV HFADSGNFSY ATSFPSPITL
GAAFDDDLVK QIATVIGTEG RAFGNAGHAG LDYWTPNINP YRDPRWGRGQ ETPGEDPFHT
SRYVYHLIDG LQDGIGPEKP KIVATCKHFA GYDIEDWEGN ERYAFDAVIS DQDMAEYYFP
PFKTCTRDAK VDAVMCSYNS VNGIPTCADP WLLQTVLREH WEWEGVGHWV TSDCGAIDNI
YKDHKYVADG AHAAAVAVNA GTDLDCGSVY PQFLGSAISQ GLLGNRTLDR ALTRLYSSLV
KLGYFDPAAD QPYRSIGWSD VATPDAEQLA HTAAVEGTVL LKNDGTLPLK KNGTVAIVGP
YANATTQLQG NYEGTAKYIH TMLSAAAQQG YKVKYAPGTG INSNSTSGFE QALNAAKGSD
LVIYFGGIDH EVEAEALDRT SIAWPGNQLD LIQQLSDLKK PLVVVQFGGG QVDDSSLLSN
AGVNGLLWAG YPSQAGGAAV FDILTGKTAP AGRLPVTQYP EEYVDQVPMT DMNLRPGPSN
PGRTYRWYDK AVIPFGYGMH YTTFDVSWKR KNYGPYNTAA VKAENAVLET FSLQVKNTGK
VTSDYVALVF LTTTDAGPKP YPIKTLVGYQ RVKAIRPGER KVVDIDVTVG SVARTAANGD
LVLYPGSYKL QVDVEKDYPT AGFKIAGKEV VLDHFPQPPR NATKA
