ID A0A1I6ST98_9ACTN Unreviewed; 473 AA.
AC A0A1I6ST98;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN05444716_104139 {ECO:0000313|EMBL:SFS80173.1};
OS Streptomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1176198 {ECO:0000313|EMBL:SFS80173.1, ECO:0000313|Proteomes:UP000198873};
RN [1] {ECO:0000313|Proteomes:UP000198873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7047 {ECO:0000313|Proteomes:UP000198873};
RA Varghese N., Submissions S.;
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; FPAB01000004; SFS80173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ST98; -.
DR STRING; 1176198.SAMN05444716_104139; -.
DR Proteomes; UP000198873; 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; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 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:UP000198873};
KW Xylan degradation {ECO:0000313|EMBL:SFS80173.1}.
FT DOMAIN 40..340
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 473 AA; 51019 MW; 878BC954EE10E8BA CRC64;
MGSYAISPPT ARRKFHGLLI ALIVGVLGVV SALVTPPSAH AAESTLGAAA AQSDRYFGVA
IASGRLNDSV YTSIANREFN SVTAENEMKI DATQPQRGQF NFTAGDRVYN WAVQNGKQVR
GHTLAWHSQQ PGWMQSLSGG ELRRAMTDHI TGVMTHYRGK IVEWDVVNEA FADGGSGARR
DSNLQRSGND WIEVAFRAAR AADPAAKLCY NDYNVENWNS AKTQAMYAMV RDFKQRGVPI
DCVGFQAHFN EGNPYNSNFR TTLQSFAALG VDVSVTELDI QGASPATFAN VTNDCLAVAR
CVGITVWGVR DSDSWRSHHT PLLFNNDGSK KPAYDAVLNA LNGGSSTPIP GGQIRGAGSE
RCLDVPNSST TDGTQVQLWD CHGGTNQQWT HTANGEFRVY GDKCLDAGGT SNGTRVQIYS
CWGGDNQKWR VNSDGSIVGV QSGLCLDATG SGNGAQLQLY SCWNGSNQRW TVT
//
