BXLB_ASPOR
ID BXLB_ASPOR Reviewed; 797 AA.
AC Q2TYT2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=AO090103000120;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
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DR EMBL; AP007174; BAE65591.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2TYT2; -.
DR SMR; Q2TYT2; -.
DR STRING; 510516.Q2TYT2; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR EnsemblFungi; BAE65591; BAE65591; AO090103000120.
DR VEuPathDB; FungiDB:AO090103000120; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OMA; QCARDSN; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000006564; Chromosome 8.
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 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..797
FT /note="Probable exo-1,4-beta-xylosidase bxlB"
FT /id="PRO_0000394089"
FT ACT_SITE 312
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 797 AA; 86392 MW; 1ECC80EDDF734246 CRC64;
MPLICIVYFL QYLDKIAISY ASVTGLRESA NLHGNQFNWV STSTESIFPD CSTGPLSKNN
VCDTSLDPVS RAKSLVAAMT LEEKINNTKY DSSGAPRLGL PAYNWWNEAL HGVAEGHGVS
FSDSGNFSYA TSFPMPILLG AAFDDDLVKQ VATVISTEAR AFANGGHAGL DYWTPNINPF
RDPRWGRGQE TPGEDPLHLS RYVYHLVDGL QDGIGPERPK VVATCKHFAA YDLENWEGIE
RYAFDAVVSP QDLSEYYLPS FKTCTRDAKV DAVMCSYNSL NGIPTCADRW LLQTLLREHW
GWEQTGHWVT GDCGAIDNIY ADHHYVADGA HAAAAALNAG TDLDCGSVFP EYLGSALQQG
LYNNQTLNNA LIRLYSSLVK LGYFDPADDQ PYRSIGWNEV FTPAAEELAH KATVEGIVML
KNDGTLPLKS NGTVAIIGPF ANATTQLQGN YEGPPKYIRT LIWAAVHNGY KVKFSQGTDI
NSNSSAGFAE AISAAKEADT VIYAGGIDNT IEKESQDRTT IVWPGNQLDL IEQLSDLEKP
LIVVQFGGGQ VDDSSLLANA GVGALLWAGY PSQAGGAAVF DILTGKSAPA GRLPVTQYPA
SYVDEVPMTD MTLRPGSNNP GRTYRWYDKA VLPFGFGLHY TTFNVSWNHA EYGPYNTDSV
ASGTTNAPVD TELFDTFSIT VTNTGNVASD YIALLFLTAD GVGPEPYPIK TLVGYSRAKG
IEPGQSQQVK LDVSVGSVAR TAENGDLVLY PGSYKLEVDV GQDFPTATFT VSGKEKVLDE
FPEPQQNATS AVTRRGR
