ID A0A0M2PGU5_9BACI Unreviewed; 337 AA.
AC A0A0M2PGU5;
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_13375 {ECO:0000313|EMBL:KKI91704.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI91704.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI91704.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI91704.1,
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:KKI91704.1}.
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DR EMBL; LATZ01000021; KKI91704.1; -; Genomic_DNA.
DR RefSeq; WP_046517346.1; NZ_LATZ01000021.1.
DR AlphaFoldDB; A0A0M2PGU5; -.
DR PATRIC; fig|1455638.3.peg.2994; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000034887; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan 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, ECO:0000313|EMBL:KKI91704.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Xylan degradation {ECO:0000313|EMBL:KKI91704.1}.
FT DOMAIN 7..336
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 337 AA; 39333 MW; B715154D22E37858 CRC64;
MNQLQSKLNI PSFSDVYSDY FSIGAAINQR TIESSKQLLT RHFNSITAEN EMKPENLQPN
ENKFSFEKAD QFVAFAEEHN MKMRGHTLVW HNQTPDWMFK EQDGSDASRE LLLDRMKTHI
STVVGRYQGR IHSWDVVNEV IDDSEVLFLR KSNYLEIVGE DFIEKAFRFA HEADSKALLF
YNDYNECHPQ KRDKIYKLVK SLIEKQVPIH GIGMQGHWNL TSPSLDNIRA AIEKYASLGL
QIQLTELDVS VFDTTDGRTD LKEPTTEMIA LQEERYEQLF SMLREYRDVI SSVTFWGVAD
DYTWLDNFPV KGRKNWPLLF DVNQLPKQAL QKITSFR
//