ID A0A1Q9PS80_9BACI Unreviewed; 329 AA.
AC A0A1Q9PS80;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BTR25_16430 {ECO:0000313|EMBL:OLS37204.1};
OS Bacillus sp. MRMR6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1928617 {ECO:0000313|EMBL:OLS37204.1, ECO:0000313|Proteomes:UP000185615};
RN [1] {ECO:0000313|EMBL:OLS37204.1, ECO:0000313|Proteomes:UP000185615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRMR6 {ECO:0000313|EMBL:OLS37204.1,
RC ECO:0000313|Proteomes:UP000185615};
RA Thomas J.M., Ghebrendrias N., Rawat M.;
RT "Mendota Genome Annoucement.";
RL Submitted (DEC-2016) 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:OLS37204.1}.
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DR EMBL; MSLS01000018; OLS37204.1; -; Genomic_DNA.
DR RefSeq; WP_075689129.1; NZ_MSLS01000018.1.
DR AlphaFoldDB; A0A1Q9PS80; -.
DR STRING; 1928617.BTR25_16430; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000185615; 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:OLS37204.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000185615};
KW Xylan degradation {ECO:0000313|EMBL:OLS37204.1}.
FT DOMAIN 5..329
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
SQ SEQUENCE 329 AA; 38675 MW; ACCE6D78F6C65896 CRC64;
MVKTTVEIPS LSKVYVEYFN IGAAVNLRTI ESQKDLLKKH FNSITAENDM KFIEIQPAEG
QFTFEKADQL AAFAKDNGMK MRGHTLVWHN QTPDWVFQNA DRETLLQRMK DHITTVMKRY
KGTIFCWDVV NEAVTDEGPE LYRSTKWLEI IGEDYIEKAF EFAHEADPEA LLFYNDYNES
NPEKREKIYK LVKSLVDKGV PIHGVGLQAH WNLVNPSLED IRTAIERYVS LGLKLHLTEL
DVSVFNFEDK RTDLTEPTSE LLKWQAERYD QVFQLLRQYR DHVTSVTFWG AADDYTWLSD
FPVRGRKNWP FLFDEKHQPK DSFWKVVQY
//
