ID A0A1Y1ZMG3_9PLEO Unreviewed; 425 AA.
AC A0A1Y1ZMG3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BCR34DRAFT_624825 {ECO:0000313|EMBL:ORY11443.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY11443.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY11443.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY11443.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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|RuleBase:RU361174};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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:ORY11443.1}.
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DR EMBL; MCFA01000061; ORY11443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1ZMG3; -.
DR STRING; 1231657.A0A1Y1ZMG3; -.
DR OrthoDB; 548101at2759; -.
DR Proteomes; UP000193144; Unassembled WGS sequence.
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; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PS00591; GH10_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000193144};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ORY11443.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..425
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012124073"
FT DOMAIN 25..343
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 389..425
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 425 AA; 44588 MW; 9CE7B406D45DE3D9 CRC64;
MAFVTALTVL LAATGSSATP FNRRATDGLN IRAVAAGKQY FGSATDNGEL SNSAYLSGLS
NTADFGQITP GNSMKWDSIE PSRGSFSYSG GDTIQQLAVK NGQKLRCHTL VWHSQLPNWV
SNGGFDNATL ISVMKNHITN EMTHYKGKCF HWDVVNEALN EDGTFRSSVF YNTIGPAFIP
IAFATAASVD PDAKLYYNDY NTENAGSKST GAQNIVKLIK QYGAKIDGVG FQSHFIVGST
PSQSAQVSNM NAFVSLGVEV AITELDIRTN TPATSSAVAQ QAKDYAATIG ACKAVAKCVG
VTIWDYTDKY SWIPGVFSGQ GSALPWDDNL NKKTDIYNAI LNAWGSAPTG GATSSAASSA
TVAPPASTSA VRSTTTSAAP AATSSAAGPV VAKWGQCGGV NWNGGTVCES GSSCTKFNDY
YSQCI
//
