ID A0A1I7IIJ3_9CLOT Unreviewed; 596 AA.
AC A0A1I7IIJ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN04487886_11212 {ECO:0000313|EMBL:SFU72754.1};
OS Clostridium sp. DSM 8431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1761781 {ECO:0000313|EMBL:SFU72754.1, ECO:0000313|Proteomes:UP000198524};
RN [1] {ECO:0000313|EMBL:SFU72754.1, ECO:0000313|Proteomes:UP000198524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8431 {ECO:0000313|EMBL:SFU72754.1,
RC ECO:0000313|Proteomes:UP000198524};
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|RuleBase:RU361174}.
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DR EMBL; FPBY01000121; SFU72754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7IIJ3; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000198524; 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 CDD; cd14256; Dockerin_I; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; PF00404; Dockerin_1; 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; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
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:SFU72754.1};
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:UP000198524};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SFU72754.1}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..596
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011499674"
FT DOMAIN 177..527
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 535..596
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
SQ SEQUENCE 596 AA; 67098 MW; AB550C331AE261D5 CRC64;
MKKLTSLVMA FITAICFTLL IPFSASAADI KGTDGYTYKT YDFSEMSFLL ARGTEYSISG
TNLNATFTGL WKEIQFQLPE TLDMSKCPSV TFSGNCTNGK TCFKLYNTDN EELAVQYDFK
NNGECTFTTD SKLTNKMVDH VGIMSKESNQ ISVTINSVKF KYDDRDPYLD NSISADDNLL
TNYGQAFDHV GAAVSAAKFA NPSVVKYLQI EHNSVTPGNE MKPDAIMNST DTISVDEAKS
LGYYIPEGYS ESTVPKLDFT TVDSMLKTAS DNGFSFRAHT LVWHQQTPDR FFRDGYSDNG
AYVSKDTMNK RMEFYIRSVM DHVYTGQYSK AVYAWDVVNE YLHANNSGWL NIYGGVNTNP
DFVKQAFNIA YDELEKYGVQ DKVKLFYNDY NTYDEVSNVI TLINNINADK KVCAGIGMQS
HIGLYPSNVS HYLNALQKFV NEGFEVQITE LDATCNNFDT QAKYYYDLMT GVMKIKKESD
ESETLGKITA LIFWGIADDD SWRSAQRPLL YSDYYTAKPA YSKVLQAYKE SGYVPKVMYG
DVNGDRVIDL SDYTLLRKYV NNGGKESNIV ITEKNADVNK DGNVNFFDLV ALKALI
//