ID   A0A099D7C2_9ACTN        Unreviewed;       362 AA.
AC   A0A099D7C2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=CDG81_12445 {ECO:0000313|EMBL:ASU78961.1}, IL38_12525
GN   {ECO:0000313|EMBL:KGI81295.1};
OS   Actinopolyspora erythraea.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC   Actinopolysporaceae; Actinopolyspora.
OX   NCBI_TaxID=414996 {ECO:0000313|EMBL:ASU78961.1, ECO:0000313|Proteomes:UP000215043};
RN   [1] {ECO:0000313|EMBL:KGI81295.1, ECO:0000313|Proteomes:UP000029737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM90600 {ECO:0000313|EMBL:KGI81295.1,
RC   ECO:0000313|Proteomes:UP000029737};
RX   PubMed=25250723;
RA   Chen D., Feng J., Huang L., Zhang Q., Wu J., Zhu X., Duan Y., Xu Z.;
RT   "Identification and Characterization of a New Erythromycin Biosynthetic
RT   Gene Cluster in Actinopolyspora erythraea YIM90600, a Novel Erythronolide-
RT   Producing Halophilic Actinomycete Isolated from Salt Field.";
RL   PLoS ONE 9:E108129-E108129(2014).
RN   [2] {ECO:0000313|EMBL:ASU78961.1, ECO:0000313|Proteomes:UP000215043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90600 {ECO:0000313|EMBL:ASU78961.1,
RC   ECO:0000313|Proteomes:UP000215043};
RA   Yin M., Tang S.;
RT   "The complete genome sequence of moderately halophilic actinomycete
RT   Actinopolyspora erythraea YIM 90600, the producer of novel erythromycin,
RT   novel actinopolysporins A-C and tubercidin.";
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}.
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DR   EMBL; CP022752; ASU78961.1; -; Genomic_DNA.
DR   EMBL; JPMV01000020; KGI81295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099D7C2; -.
DR   KEGG; aey:CDG81_12445; -.
DR   eggNOG; COG3693; Bacteria.
DR   HOGENOM; CLU_020161_6_0_11; -.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000029737; Unassembled WGS sequence.
DR   Proteomes; UP000215043; Chromosome.
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:ASU78961.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174}; Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ASU78961.1}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..362
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001944188"
FT   DOMAIN          50..361
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          31..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  39759 MW;  922B88874C7CA08F CRC64;
     MPRTRGKHGR LGRLGAVLAA SAGLFASQAA PALAAPEPPE REASGTAAPA PARTPLKDLT
     DNHVGSAVDA SALANEADYR SVLTSEFSSV TAENAMKWSV VEPNRGQYDW SGADSVVNYA
     QQNGKSVRGH TLLWHKQRPG WLDNLSASEL RSAVKDHITT VVNRYEGEIR AWDVVNEVFD
     SDGTRRDSIF QRKLGDGWIA DAFRWAHQAD PSAELYINDY NTGWVNDKSN AIHDLVSSLR
     QQGVPIHGVG FQTHLSIDYS FPGGFQSNLQ RFADLGVDVA ITEADVRMTL PATDSELTTQ
     ADYYERIWNA CEAVSRCVEF TTWGYTDRHS WVPNTFDGQG AACLFDDSLN PKPAYNRLNP
     ST
//