ID   XYNB_TALPU              Reviewed;         208 AA.
AC   Q96W72; Q12666;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 85.
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 purpureogenus (Soft rot fungus) (Penicillium purpureogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1266744;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9099888; DOI=10.1016/s0378-1119(96)00762-7;
RA   Diaz R., Sapag A., Peirano A., Steiner J., Eyzaguirre J.;
RT   "Cloning, sequencing and expression of the cDNA of endoxylanase B from
RT   Penicillium purpurogenum.";
RL   Gene 187:247-251(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, CATALYTIC
RP   ACTIVITY, AND INDUCTION.
RX   PubMed=12137954; DOI=10.1016/s0378-1119(02)00720-5;
RA   Chavez R., Schachter K., Navarro C., Peirano A., Aguirre C., Bull P.,
RA   Eyzaguirre J.;
RT   "Differences in expression of two endoxylanase genes (xynA and xynB) from
RT   Penicillium purpurogenum.";
RL   Gene 293:161-168(2002).
RN   [3]
RP   SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=7640003; DOI=10.1016/0168-1656(95)00057-w;
RA   Belancic A., Scarpa J., Peirano A., Diaz R., Steiner J., Eyzaguirre J.;
RT   "Penicillium purpurogenum produces several xylanases: purification and
RT   properties of two of the enzymes.";
RL   J. Biotechnol. 41:71-79(1995).
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. {ECO:0000269|PubMed:7640003}.
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:12137954,
CC         ECO:0000269|PubMed:7640003};
CC   -!- ACTIVITY REGULATION: N-bromosuccinimide completely inhibits the
CC       catalytic activity. {ECO:0000269|PubMed:7640003}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.5. {ECO:0000269|PubMed:7640003};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:7640003};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12137954}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; Z50050; CAA90390.1; -; mRNA.
DR   EMBL; AF359553; AAK50762.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96W72; -.
DR   SMR; Q96W72; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11B_PENPU; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..208
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000429662"
FT   DOMAIN          17..207
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CONFLICT        13..19
FT                   /note="TTLAAPA -> RHSPPLS (in Ref. 1; CAA90390)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="H -> Y (in Ref. 1; CAA90390)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178..179
FT                   /note="KH -> ND (in Ref. 1; CAA90390)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  21869 MW;  6DC554A2CA97C6D3 CRC64;
     MKVTAAFAGL LATTLAAPAT ELVTRSINYV QNYNGNLGAF SYNEGAGTFS MYWQQGVSND
     FVVGLGRSTG SSNPITYSAS YSASGGSYLA VYGWVNSPQA EYHVVEAYGN YNPCSSGSAT
     NLGTVSSDGG TYQVCTDTRV NQPSITGTST FTQFFSVRQG SRTSGTVTIA NHFNFWAKHG
     FGNSNFNYQV VAVEAWSGTG TASVTVSA