ID   XYNA_BACPU              Reviewed;         228 AA.
AC   P00694;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-MAY-2023, entry version 109.
DE   RecName: Full=Endo-1,4-beta-xylanase A;
DE            Short=Xylanase A;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase A;
DE   Flags: Precursor;
GN   Name=xynA;
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IPO;
RA   Fukusaki E., Panbangred W., Shinmyo A., Okada H.;
RT   "The complete nucleotide sequence of the xylanase gene (xynA) of Bacillus
RT   pumilus.";
RL   FEBS Lett. 171:197-201(1984).
RN   [2]
RP   SEQUENCE REVISION TO 103.
RA   Urabe I.;
RL   Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   MUTAGENESIS, AND ACTIVE SITES.
RX   PubMed=1359880; DOI=10.1042/bj2880117;
RA   Ko E.P., Akatsuka H., Moriyama H., Shinmyo A., Hata Y., Katsube Y.,
RA   Urabe I., Okada H.;
RT   "Site-directed mutagenesis at aspartate and glutamate residues of xylanase
RT   from Bacillus pumilus.";
RL   Biochem. J. 288:117-121(1992).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; X00660; CAA25278.1; -; Genomic_DNA.
DR   PIR; A00848; WWBSXP.
DR   RefSeq; WP_007500674.1; NZ_CP011109.1.
DR   AlphaFoldDB; P00694; -.
DR   SMR; P00694; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11C_BACPU; -.
DR   GeneID; 66363417; -.
DR   UniPathway; UPA00114; -.
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   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 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; Signal; Xylan degradation.
FT   SIGNAL          1..27
FT   CHAIN           28..228
FT                   /note="Endo-1,4-beta-xylanase A"
FT                   /id="PRO_0000007997"
FT   DOMAIN          29..222
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        120
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT   MUTAGEN         120
FT                   /note="E->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1359880"
FT   MUTAGEN         209
FT                   /note="E->D: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1359880"
SQ   SEQUENCE   228 AA;  25491 MW;  32EF9833E7B5E503 CRC64;
     MNLRKLRLLF VMCIGLTLIL TAVPAHARTI TNNEMGNHSG YDYELWKDYG NTSMTLNNGG
     AFSAGWNNIG NALFRKGKKF DSTRTHHQLG NISINYNASF NPGGNSYLCV YGWTQSPLAE
     YYIVDSWGTY RPTGAYKGSF YADGGTYDIY ETTRVNQPSI IGIATFKQYW SVRQTKRTSG
     TVSVSAHFRK WESLGMPMGK MYETAFTVEG YQSSGSANVM TNQLFIGN
//