ID A0A1R3UQJ9_9ACTN Unreviewed; 376 AA.
AC A0A1R3UQJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BQ8420_20565 {ECO:0000313|EMBL:SIO89051.1};
OS Nocardiopsis sp. JB363.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1434837 {ECO:0000313|EMBL:SIO89051.1, ECO:0000313|Proteomes:UP000195722};
RN [1] {ECO:0000313|EMBL:SIO89051.1, ECO:0000313|Proteomes:UP000195722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB363 {ECO:0000313|EMBL:SIO89051.1,
RC ECO:0000313|Proteomes:UP000195722};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; FRFF01000133; SIO89051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3UQJ9; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000195722; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000195722};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000313|EMBL:SIO89051.1}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..361
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 376 AA; 41860 MW; 88F86FB01E083553 CRC64;
MRKTTERRRR TATRGRGVLL AAGAVCVVIF VVAAVLALVL PGPAEEPGSD LPGLAESHGI
KLGVAVAVDP LRDDSDYQDI VTDHYTSVTA ENTMKWEHVQ PERHEFDWSG PDTMVDFAED
HGLDMRGHTL LWHNQQPEWL AQGFYDSDEL REVMREHMEA LVGRYQGRID SWDVINEPFE
DGGPELRDNL WYQTLGEDYI AEGLRMAHEV DPDAKLYINE FGIEGGGDKA DALYELASGL
LEEGVPLHGI GFQGHFVHGD VPEDLAENMR RFADLGLDVE ISELDVRIAE PVTDEAISAQ
AEEYRRAVEA CLDVSRCVGV SVWGVTDAHS WIPEWFPGYD SALPFDEDYQ GKPALGGMVE
ALRRDRRSPG RPAPGR
//
