ID   XYN2_GEOSE              Reviewed;         330 AA.
AC   P45703;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Endo-1,4-beta-xylanase;
DE            Short=Xylanase;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase;
GN   Name=xynA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-7.
RC   STRAIN=No. 21;
RX   PubMed=8074507; DOI=10.1128/aem.60.7.2252-2258.1994;
RA   Baba T., Shinke R., Nanmori T.;
RT   "Identification and characterization of clustered genes for thermostable
RT   xylan-degrading enzymes, beta-xylosidase and xylanase, of Bacillus
RT   stearothermophilus 21.";
RL   Appl. Environ. Microbiol. 60:2252-2258(1994).
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: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By xylan and xylose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       Cytoplasmic xylanase subfamily. {ECO:0000305}.
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DR   EMBL; D28121; BAA05668.1; -; Genomic_DNA.
DR   PIR; I39760; I39760.
DR   AlphaFoldDB; P45703; -.
DR   SMR; P45703; -.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005737; C:cytoplasm; 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   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Xylan degradation.
FT   CHAIN           1..330
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /id="PRO_0000007969"
FT   DOMAIN          2..330
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   330 AA;  38473 MW;  0A2026B23502EB48 CRC64;
     MCSSIPSLRE VFANDFRIGA AVNPVTLEAQ QSLLIRHVNS LTAENHMKFE HLQPEEGRFT
     FDIAIKSSTS PFSSHGVRGH TLVWHNQTPS WVFQDSQGHF VGRDVLLERM KSHISTVVQR
     YKGKVYCWDV INEAVADEGS EWLRSSTWRQ IIGDDFIQQA FLYAHEADPE ALLFYNDYNE
     CFPEKREKIY TLVKSLRDKG IPIHGIGMQA HWSLNRPTLD EIRAAIERYA SLGVILHITE
     LDISMFEFDD HRKDLAAPTN EMVERQAERY EQIFSLFKEY RDVIQNVTFW GIADDHTWLD
     HFPVQGRKNW PLLFDEQHNP KPAFWRVVNI