ID G3FAQ8_9EURO Unreviewed; 384 AA.
AC G3FAQ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN Name=xyl1 {ECO:0000313|EMBL:AEN99940.1};
OS Chrysosporium lucknowense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Chrysosporium.
OX NCBI_TaxID=85845 {ECO:0000313|EMBL:AEN99940.1};
RN [1] {ECO:0000313|EMBL:AEN99940.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VKM F-3500-D {ECO:0000313|EMBL:AEN99940.1};
RA van Gool M.P., Bartels J., van Muiswinkel G., Hinz S., Schols H.,
RA Gruppen H.;
RT "Xylanases from Chrysosporium lucknowense.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC ECO:0000256|RuleBase:RU361174};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR EMBL; JF508853; AEN99940.1; -; Genomic_DNA.
DR AlphaFoldDB; G3FAQ8; -.
DR SMR; G3FAQ8; -.
DR CLAE; XYN10A_MYCTH; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF76; ENDO-1,4-BETA-XYLANASE C; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00236; fCBD; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:AEN99940.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..384
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003443522"
FT DOMAIN 17..53
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT DOMAIN 78..383
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT REGION 55..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 41285 MW; 485765C7B7B444B8 CRC64;
MRTLTFVLAA APVAVLAQSP LWGQCGGQGW TGPTTCVSGA VCQFVNDWYS QCVPGSSNPP
TGTTSSTTGS TPAPTGGGGS GTGLHDKFKA KGKLYFGTEI DHYHLNNNAL TNIVKKDFGQ
VTHENSLKWD ATEPSRNQFN FANADAVVNF AQANGKLIRG HTLLWHSQLP QWVQNINDRN
TLTQVIENHV TTLVTRYKGK ILHWDVVNEI FAEDGSLRDS VFSRVLGEDF VGIAFRAARA
ADPNAKLYIN DYNLDIANYA KVTRGMVEKV NKWIAQGIPI DGIGTQCHLA GPGGWNTAAG
VPDALKALAA ANVKEIAITE LDIAGASAND YLTVMNACLQ VSKCVGITVW GVSDKDSWRS
SSNPLLFDSN YQPKAAYNAL INAL
//
