XYNB_TALFU
ID XYNB_TALFU Reviewed; 282 AA.
AC Q8J0K5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Endo-1,4-beta-xylanase B;
DE Short=Xylanase B;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase B;
DE Flags: Precursor;
GN Name=xynB;
OS Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium
OS funiculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=28572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-49; 135-153
RP AND 162-170.
RC STRAIN=IMI 134756;
RX PubMed=12664153; DOI=10.1007/s00253-002-1184-4;
RA Alcocer M.J., Furniss C.S.M., Kroon P.A., Campbell M., Archer D.B.;
RT "Comparison of modular and non-modular xylanases as carrier proteins for
RT the efficient secretion of heterologous proteins from Penicillium
RT funiculosum.";
RL Appl. Microbiol. Biotechnol. 60:726-732(2003).
RN [2]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15450181; DOI=10.1016/j.bbapap.2004.06.010;
RA Brutus A., Villard C., Durand A., Tahir T., Furniss C., Puigserver A.,
RA Juge N., Giardina T.;
RT "The inhibition specificity of recombinant Penicillium funiculosum xylanase
RT B towards wheat proteinaceous inhibitors.";
RL Biochim. Biophys. Acta 1701:121-128(2004).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=IMI 134756;
RX AGRICOLA=IND43674834;
RA Furniss C.S.M., Williamson G., Kroon P.A.;
RT "The substrate specificity and susceptibility to wheat inhibitor proteins
RT of Penicillium funiculosum xylanases from a commercial enzyme
RT preparation.";
RL J. Sci. Food Agric. 85:574-582(2005).
CC -!- FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:15450181,
CC ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Significantly inhibited by the wheat xylanase
CC inhibiting protein I (XIP-I) and the proteinaceous endoxylanase
CC Triticum aestivum xylanase inhibitors I (TAXI-I), but not TAXI-II.
CC {ECO:0000269|PubMed:15450181, ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 mg/ml for birchwood xylan {ECO:0000269|PubMed:15450181,
CC ECO:0000269|Ref.3};
CC KM=29 mg/ml for insoluble fractions of wheat arabinoxylans
CC {ECO:0000269|PubMed:15450181, ECO:0000269|Ref.3};
CC Vmax=506 umol/min/mg enzyme toward birchwood xylan
CC {ECO:0000269|PubMed:15450181, ECO:0000269|Ref.3};
CC Vmax=1080 umol/min/mg enzyme toward insoluble fractions of wheat
CC arabinoxylans {ECO:0000269|PubMed:15450181, ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 3.7-4.7 for birchwood xylan.
CC {ECO:0000269|PubMed:15450181, ECO:0000269|Ref.3};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; AJ489605; CAD33900.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8J0K5; -.
DR SMR; Q8J0K5; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11B_PENFN; -.
DR BRENDA; 3.2.1.8; 4616.
DR UniPathway; UPA00114; -.
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; 2.60.120.180; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:12664153"
FT CHAIN 40..282
FT /note="Endo-1,4-beta-xylanase B"
FT /id="PRO_5000068593"
FT DOMAIN 40..219
FT /note="GH11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 246..282
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 214..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 206
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 282 AA; 29475 MW; 1ABD021D46A8F614 CRC64;
MGISSILLSA LIAGGALALP AAEPVSFDIR DENITLARRA EAINYNQDYI ASGANVQYSP
NMAAGSFSIN YNTQGDFVVG LGWQPGDANP ITYSGSFSAS GVGILAVYGW STNPLVEYYV
MEVHDGYQTA GTHKGTVTTD GGTYDIWEHQ QVNQPSILGT STFNQYISIR QSPRTSGTVT
VQNHFNAWAQ AGMNLGTLNY QVMAVESWSG SGSGQISLSK GTGGGSTTTT PTGPTSTSTA
PSSGGTGAAQ WGQCGGIGWT GPTTCVAPYT CKYENAYYSQ CQ
