ID   A0A0X3VN36_9ACTN        Unreviewed;       453 AA.
AC   A0A0X3VN36;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=ADL12_02680 {ECO:0000313|EMBL:KUL46179.1};
OS   Streptomyces regalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL46179.1, ECO:0000313|Proteomes:UP000053923};
RN   [1] {ECO:0000313|Proteomes:UP000053923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (OCT-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|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:KUL46179.1}.
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DR   EMBL; LLZG01000007; KUL46179.1; -; Genomic_DNA.
DR   RefSeq; WP_062698031.1; NZ_LLZG01000007.1.
DR   AlphaFoldDB; A0A0X3VN36; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000053923; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
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; PF00553; CBM_2; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00637; CBD_II; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00591; GH10_1; 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|ARBA:ARBA00023295, 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:UP000053923};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:KUL46179.1}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..453
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007056075"
FT   DOMAIN          34..344
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          351..453
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   453 AA;  47760 MW;  A61618584586A76F CRC64;
     MRSLRTGLSL GSLLTGVATV AALLLTAPAA HAADTPLRDL AAAQGKVMGT AVTGSKLTGT
     YGDIVGREFN AMTPGNAMKW GSVEPTRSSF NWAEADQIVA FAEAHGQQVR GHTLVWHSQN
     PGWLTNGSWT SAELSQLMND HIATEVGRYK GRLATWDVVN EPFNEDGTYR QTLWYNGLGA
     DYIAQALTAA RAADPSAKLY INDYNVEGVN AKSTALYNLV KSLKERGVPI DGVGLQAHLI
     LGQVPSTMQQ NIQRFADLGV DVAITELDIR MQLPSDSAKL TQQAADYKAV MNACLAVSRC
     VGVTVWGFTD SDSWIPGTFP GQGAATPYDE NYVPKPAYHA IAESLGGGTT TPPPTDACTA
     TYSVASQWNT GFTGQVRIAC SGAALSAWKV SWTYGAGQQL TQAWNASCTQ SGATVTCSNA
     SYNGTVPDGG SVTFGFNASW SGSNPAPTVA LAE
//