ID A0A0F8UQW9_9EURO Unreviewed; 793 AA.
AC A0A0F8UQW9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
DE AltName: Full=1,4-beta-D-xylan xylohydrolase xlnD {ECO:0000256|ARBA:ARBA00041684};
DE AltName: Full=Beta-xylosidase A {ECO:0000256|ARBA:ARBA00042744};
DE AltName: Full=Beta-xylosidase xlnD {ECO:0000256|ARBA:ARBA00041545};
DE AltName: Full=Xylobiase xlnD {ECO:0000256|ARBA:ARBA00041508};
GN ORFNames=ARAM_000563 {ECO:0000313|EMBL:KKK13216.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK13216.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK13216.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK13216.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) 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:0000256|ARBA:ARBA00025331}.
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 Evidence={ECO:0000256|ARBA:ARBA00024574};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK13216.1}.
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DR EMBL; JZBS01003859; KKK13216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8UQW9; -.
DR STRING; 308745.A0A0F8UQW9; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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:SF13; EXO-1,4-BETA-XYLOSIDASE XLND; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..793
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002528656"
FT DOMAIN 694..764
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 793 AA; 86465 MW; 45772A52642F191B CRC64;
MHVPTSAVAL AAALLVPLAL AQANTSYVDY NTSPNPDLFP LTFKLLKTSF PDCNNGPLSQ
TRVCDKTARP HDRAAALLSL LTLEELVNNT GNTGLGVPRL GLPNYQVWEE ALHGVARADW
SSSGEYSWAT SFPMPILTMA ALNRTLVNQI ASIISTQLRA YSNIGRGGLD VYAPNINTFR
HPVWGRGQET PGEDAYCLTS AYAYEYITGL QGGVDPEHLK IVATAKHYAG YDIENWENHS
RLANDMQITQ QELSEYYTPQ FLVAARDARV HSVMCSYNAV NGVPSCSNSF FLQTLLRDTF
GFVEDGYVSG DCGAVYNVFN PHGYAANESG AAADSIRAGT DIDCGTSYQS RFEDAFEDGL
LSRSDIERGV IRLYSNLVRL GYFDGEDQEY RGISWTDVLK TDAWNISYEA AVEGIVLLKN
DDTLPLSPHI RSIALIGPWA NATVELQGNY YGPAPYLISP LSAFQSSGLK IHYAEGTAIK
SDSQEGFHAA LAAARNADAI VFAGGIDETI EGEAMDRESI AWPGNQLELI QQLSQLQKPL
IVLQMGGGQV DSSSLKDSKH VNALIWGGYP GQSGGQALFD IITGKRAPAG RLVSTQYPAE
YALQFPAIDM NLRPSGHNPG QTYMWYTGTP VYEFGHGLFY TTFHEGHAGS SDRGTYDITD
ILSQPYTGYM YAEQRPLLHF TARITNTGRR TSDYTAMVFA NTTAGPLPHP NKWLIGFDRL
AALNPGASTT LTIPVTIDSV ARTDEQGNRV LYPGRYELAL NNERSVVLSF TLAGDEAVLL
KWPLANQGIP PAS
//