ID   XYNB_ASPKW              Reviewed;         225 AA.
AC   P48824; G7XYK8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 92.
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   AltName: Full=Endo-1,4-beta-xylanase G1;
DE            Short=Xylanase G1;
DE   Flags: Precursor;
GN   Name=xlnB; Synonyms=xynB, xynG1; ORFNames=AKAW_10131;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RA   Ito K.;
RT   "Cloning of the third xylanase gene encoding xylanase B and
RT   characterization of the xylanase gene family of Aspergillus kawachii.";
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; D38070; BAA07264.1; -; Genomic_DNA.
DR   EMBL; DF126487; GAA92017.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48824; -.
DR   SMR; P48824; -.
DR   STRING; 40384.P48824; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   VEuPathDB; FungiDB:AKAW_10131; -.
DR   eggNOG; ENOG502RXA7; Eukaryota.
DR   InParanoid; P48824; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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; IPR018208; GH11_AS_1.
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; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..225
FT                   /note="Endo-1,4-beta-xylanase B"
FT                   /id="PRO_0000007989"
FT   DOMAIN          37..225
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   CONFLICT        100
FT                   /note="T -> N (in Ref. 1; BAA07264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139..144
FT                   /note="YKGTVT -> TRGNVS (in Ref. 1; BAA07264)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="T -> S (in Ref. 1; BAA07264)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   225 AA;  24182 MW;  2457FA9E0DFE1CB2 CRC64;
     MLTKNLLLCF AAAKAVLAVP HDSVVERSDA LHKLSERSTP SSTGENNGYY YSFWTDGGGD
     VTYTNGNAGS YSVEWSNVGN FVGGKGWNPG SAKDITYSGT FTPSGNGYLS VYGWTTDPLI
     EYYIVESYGD YNPGSGGTYK GTVTSDGSVY DIYTATRTNA PSIQGTATFT QYWSVRQNKR
     VGGTVTTSNH FNAWAKLGMN LGTHNYQILA TEGYQSSGSS SITIQ