BXLB_ASPCL
ID BXLB_ASPCL Reviewed; 771 AA.
AC A1CCL9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 65.
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=ACLA_062400;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAW12276.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DS027050; EAW12276.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001273702.1; XM_001273701.1.
DR AlphaFoldDB; A1CCL9; -.
DR SMR; A1CCL9; -.
DR STRING; 5057.CADACLAP00005715; -.
DR EnsemblFungi; EAW12276; EAW12276; ACLA_062400.
DR GeneID; 4705939; -.
DR KEGG; act:ACLA_062400; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR OrthoDB; 321444at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000006701; 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 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..771
FT /note="Probable exo-1,4-beta-xylosidase bxlB"
FT /id="PRO_0000394085"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
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 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 83355 MW; 4EA258993A6B26C1 CRC64;
MVGLTPQHYG NAIALMTYLA STALADNKFP DCTSGPLSKL AVCDTSRDVT TRAQSLVDAM
SFAEKVNNTQ YEAPGVPRLG LPAYNWWSEA LHGVAGAPGV HFADSGPFSY ATSFAQPILL
GASFDDELVK QVATVVGTEG RAFGNAGRAG LDYWTPNINP FRDPRWGRGQ ETPGEDPLHV
SRYVYHLVDG LQGGIGPARP QIAATCKHFA AYDMEDWNGV SRHEFDARVS TQDLAEFYLP
SFKSCVRDAQ VDAVMCSYNA LNGVPTCADP YLLQTLLREH WDWDQPGHWV VSDCGAIDDI
YIGHNYTKTG AEAAAVALNA GTDLDCGTVF PKHLGEAAEQ GLYTNQTLDR ALVRLYSSLV
KLGYFDPAEK QPYGSIGWKD VDTPAAEQLA HKAAVEGIVL LKNDQTLPLK AKGTLALIGP
YANATKQMQG NYQGPPKYIR TLEWAATQHG YQVQYSPGTA INNSSTAGFA AALAAAKDAD
VVLYAGGIDN TIESETLDRT TITWPGNQLS LISELSNLHK PLIVIQFGGG QVDDTPLLTN
PHVNALLWAG YPSQEGGAAI FDILTGKAAP AGRLPITQYP AAYTAQVPMT EMGLRAGGDN
PGRTYRWYDK AVVPFGFGLH YTSFEVSWDR GRLGPYNTAA LVNRAPGGSH VDRALFDTFR
VQVQNTGTVT SDYVALLFVK TEDAGPEPYP LKTLVGYTRV QQVKPGERRS VEIEVTLGAM
ARTAANGDLV LYPGKYTLQV DVGERGYPTA RVSVHGKEVV LDHFPQPPEG R
