ID   A0A0M2PLG2_9BACI        Unreviewed;       340 AA.
AC   A0A0M2PLG2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=WQ54_05240 {ECO:0000313|EMBL:KKI93314.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI93314.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI93314.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI93314.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC         ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|RuleBase:RU361174}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKI93314.1}.
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DR   EMBL; LATZ01000005; KKI93314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2PLG2; -.
DR   PATRIC; fig|1455638.3.peg.1167; -.
DR   Proteomes; UP000034887; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174}.
FT   DOMAIN          18..336
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   340 AA;  39628 MW;  5A595151656C4F0F CRC64;
     MIFVLIGIGA IFFFTFISGK DPLKAEAEKN DFLIGSAVRY DPLMKEEDYR EKIKEEFNVI
     TIENEMKFST IHPEPYVYDF TEADAIVEFA NENNIKVRGH TLVHRSLPKW LTEGNYSKEE
     VREILKSHIK TVVTHYRGKV FAWDVVNEAF TEDGEYRDNF WLRKLGPEYI KLAFKWAHEA
     DPDALLFYND YDNEEVNKKS TAIYEHINNI KSKGVPVHGV GFQMHTTINN EYDFKSTQEN
     MKRLAKSNLQ VHITELDIKL QDRTELTFQE KLDKQSGIYG DILSTCLSAN NCKALVMWGF
     TDKHSWIPKQ TETDDYPLIF DRNYQPKPSY DVLNDILSSS
//