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Database: UniProt
Entry: A0A1G4WDX8_9FIRM
LinkDB: A0A1G4WDX8_9FIRM
Original site: A0A1G4WDX8_9FIRM 
ID   A0A1G4WDX8_9FIRM        Unreviewed;       679 AA.
AC   A0A1G4WDX8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=SAMN02910339_02925 {ECO:0000313|EMBL:SCX21025.1};
OS   Lachnospiraceae bacterium YSD2013.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX21025.1, ECO:0000313|Proteomes:UP000199278};
RN   [1] {ECO:0000313|EMBL:SCX21025.1, ECO:0000313|Proteomes:UP000199278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSD2013 {ECO:0000313|EMBL:SCX21025.1,
RC   ECO:0000313|Proteomes:UP000199278};
RA   de Groot N.N.;
RL   Submitted (OCT-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|RuleBase:RU361174};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; FMTX01000043; SCX21025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4WDX8; -.
DR   STRING; 1520828.SAMN02910339_02925; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000199278; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   SUPFAM; SSF49785; Galactose-binding domain-like; 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:SCX21025.1};
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:UP000199278};
KW   Xylan degradation {ECO:0000313|EMBL:SCX21025.1}.
FT   DOMAIN          16..379
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   679 AA;  75836 MW;  7A84877AB221606E CRC64;
     MDFKLKDIYK DYFKIGVACE RINGRFTNHE IGNPAKEALM AEQFNSMTCA NELKPMYNMG
     FNSPDATEEF LPFVPNENAV EMLSFARANG LKVRGHVMVW HSQCPREIFA KGYNAVTIPT
     DPEKLKANPH LKFFEKLNPE CYVSREVLLK RIKSYIYNLV KWTYESGFAQ IIYAWDVVNE
     AIELADKTET GVRKSYWSEI IGPDYIYWAF RFARDAVDEI SAGYDYGKPL LFYNDYNEFD
     PEKKKAIIEN LGRSTSEHGS VFSEHLIDGI GMQGHLSDTN DIDLYYQAIM DYSALVDEVH
     ITELDVKCTS SGVNAFYYQA DFYKRLFEAI LKANKNGGKV TSVTVWGLTD DNSWIRGANP
     LLFNGDLSPK LACTALKYAV TGESLGEPEP VVLDLSDRFY DFEPVNGTNF DYAAVGFKNR
     GLFPIDLLKE GDGHSGNHCL ALETRFDGWS GILLDVSDFI GQTVKIGAWV KSPAKKVTLN
     VEHPNAPDKA ESFAAVDSSV DEWRYLEGEC TLPSDCHSVK VYFYTEEASE GTFSPIYVDD
     VSLHLIGLKE SFEGDTNIAA IRGMGHLPFL SVTDTEAVTP GTRSLRVSRQ EKDATVKFDI
     STYIGRDINI SLYVKTSDTT IRVGIDGCDP LGEFTSATGS FTHITVPASI PDGLRAAALF
     VETSGNADIF IDDLFITLS
//
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