ID A0A318Z9R8_9EURO Unreviewed; 406 AA.
AC A0A318Z9R8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BP01DRAFT_383906 {ECO:0000313|EMBL:PYH44106.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH44106.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH44106.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH44106.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of
CC seed galactomannans and wood galactoglucomannans.
CC {ECO:0000256|ARBA:ARBA00002993}.
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 -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; KZ821239; PYH44106.1; -; Genomic_DNA.
DR RefSeq; XP_025430088.1; XM_025577460.1.
DR AlphaFoldDB; A0A318Z9R8; -.
DR STRING; 1450539.A0A318Z9R8; -.
DR GeneID; 37078689; -.
DR OrthoDB; 3055998at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000248349; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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-UniPathway.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR017853; GH.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {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 Reference proteome {ECO:0000313|Proteomes:UP000248349};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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..406
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016337975"
FT DOMAIN 27..337
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 370..406
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 406 AA; 42648 MW; A31DBEA980CCE479 CRC64;
MIKLAVTAAL AAIALPTCIS ALGLDQAAVA AGLTYFGTAT DNPELTDIPY VTQLNNTADF
GQITPGNSQK WDATEPSQGT FSFTEGDVIA DLAEANGQYL RCHTLVWYNQ LPSWVTSGTW
TNATLIAAMQ NHITTVVSHY KGRCLHWDVV NEALNDDGTY RTNIFYTTIG EAYIPLAFAA
AAAADPSAKL FYNDYNLEYG STKAASARAI VQLVQASGAK IDGVGFQGHF VVGTVPSQAS
LVSVLQSFTA LGVEVAYTEA DVRILLPTTA TTLAQQSSDF QALVGSCVAV DGCVGFTIWD
WTDKYSWVPS TFTGYGAALP WDEDLVKKPA YDGLLVGLGA SVSTTTTATT ASSTASGVTV
TATATATTTT TAAHWGQCGG SGWTGATVCA SGYTCTYVNA WYSQCL
//
