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Database: UniProt
Entry: A0A255T961_9BACT
LinkDB: A0A255T961_9BACT
Original site: A0A255T961_9BACT 
ID   A0A255T961_9BACT        Unreviewed;       392 AA.
AC   A0A255T961;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=CIL02_06945 {ECO:0000313|EMBL:OYP61176.1};
OS   Prevotella sp. P3-122.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024223 {ECO:0000313|EMBL:OYP61176.1, ECO:0000313|Proteomes:UP000215645};
RN   [1] {ECO:0000313|EMBL:OYP61176.1, ECO:0000313|Proteomes:UP000215645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P3-122 {ECO:0000313|EMBL:OYP61176.1,
RC   ECO:0000313|Proteomes:UP000215645};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-2017) 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}.
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:OYP61176.1}.
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DR   EMBL; NPJH01000037; OYP61176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255T961; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000215645; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215645};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..392
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013259619"
FT   DOMAIN          45..385
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
SQ   SEQUENCE   392 AA;  44788 MW;  299BDCC0095D9815 CRC64;
     MCGRGRLLYY SAIQGIQRMK SSIIILSLVL AALSATAQQT ETAVADTTYG YKDAYKDYFS
     IGVSLSARNV RSAEQMDIVR RNFNSVTAEN AMKPGVIHPK ENVWRWDDAD SIANWCRRNG
     VKMRGHCLCW HEQFSNWMFT GSLGNEVTKE VFYQRLRNHI HTVVGRYKDV VYAWDVLNEA
     IADGDGDRLP DDNGEPSPYR QSRLFKLCGE ELVRKVFEFA HEADPDAKLF YNDYNAAVPS
     KRDHIYNMVK KMKDDGVPID GIGMQGHYNA WWPSAEDVEA AISKFSEIVD EVQVTELDIR
     TTNEMGGQLQ FSQGNAGGVP QHIAEMQERQ YANIFRIVRK WRNVVTNVTF WNLSDADSWL
     GAGNSPLPFD TDYKPKSIYY TIRDFNPAND RR
//
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