ID A0A074XN10_AURPU Unreviewed; 805 AA.
AC A0A074XN10;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=xylan 1,4-beta-xylosidase {ECO:0000256|ARBA:ARBA00026107};
DE EC=3.2.1.37 {ECO:0000256|ARBA:ARBA00026107};
GN ORFNames=M438DRAFT_334904 {ECO:0000313|EMBL:KEQ85069.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ85069.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ85069.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ85069.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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}.
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DR EMBL; KL584981; KEQ85069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XN10; -.
DR STRING; 1043002.A0A074XN10; -.
DR HOGENOM; CLU_004542_5_3_1; -.
DR OrthoDB; 366914at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000030706; 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:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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:UP000030706};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..805
FT /note="xylan 1,4-beta-xylosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001703531"
FT DOMAIN 677..747
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 805 AA; 86816 MW; 0BC545E0E6176309 CRC64;
MAALLSLTAL ALLGGSVSAQ TFQGTAQGGF PDCVNGPLSN NTVCDKSADP IARARALVSA
FTVAEKLNLT GNNSPGVPRL GLPIYQWWNE ALHGVAESPG VTFNATGEFR YATSFPQPIT
MGAAFDDELI TAVAEIVSTE ARAFNNHGRA GLDFWTPNIN PYRDPRWGRG QETPGEDSFH
LSSYVHALIL GLQGGEDPEI RKVTATCKHF AGYDIESWNG NLRYQNDVQI SQRDLVEYYL
PSFRSCARDS NVGAFMCTYS ALNGVPTCAD PWLLNDVLRE HWGWTNEEQW VTSDCDSIQN
IYLPHNFSDT RQGAAAAALN AGTDLDCGTY YQHHLPQAYS EGLINQTTVD QSLLRLYTSL
VRTGYFDGPD AMYRNLTFSD VSTPHAQQVA LTAAEEGIVL LKNDGLLPLT VTNSTKIAVI
GDWANATQQM IGNYFGVPPY LHSPLYAAQQ SGAQIFNAGG PGGQGDPTTD HWLPMWTAAE
KADIIIYAGG LDISVEAEGM DRETIHWTGA QLDAIGELAS YGKPTIVAQM GDQLDNTPLL
QNSNISALLW GGYPGQDGGV ALFNIITGKT APAGRLPVTQ YPAHYVADIP MTDMTLRPNE
TTGSPGRTYK WYNGTAVFEF GYGMHYTNFT ADVSPMAASS YDIAALTSNC NETYKDKCAF
ESVSVNVHNT GSVSSDYVTL GFLAGQFGPS PYPKKSLVSY QRLHSIAGGA SATATLNLTL
GSLARIDDVG NTVLYPGDYA LMIDTMPEKT MVNFTLTGSP VTLDLWPQPP SGGPTIPPSD
YFYGGYGSRG EFPIAATTEV LEPEE
//
