ID A0A261PZC0_9BACT Unreviewed; 372 AA.
AC A0A261PZC0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BWI93_25240 {ECO:0000313|EMBL:OZI05477.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI05477.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI05477.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI05477.1,
RC ECO:0000313|Proteomes:UP000215802};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Draft genome of Siphonobacter sp. BAB-5385.";
RL Submitted (JUN-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:OZI05477.1}.
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DR EMBL; NMPS01000239; OZI05477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261PZC0; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000215802; 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 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 Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000215802};
KW Xylan degradation {ECO:0000313|EMBL:OZI05477.1}.
FT DOMAIN 30..370
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 372 AA; 42657 MW; F4981B2D7408C828 CRC64;
MRFKYTPLFL LGLTSLAMTH FKPETRPVMS VNLPSLKEVY KDYFLIGTAL NAGQIDEKNP
KEIQLVTEQF NAATPENIMK AEVIHPRWDQ YDFTYADKLV EFGKKNKLAI NAHTLIWHSQ
LPGFVRKIKS NDSLQLFFRN HIQTVAGRYR GKVQSWDVVN EALNEDGTLR KSIFLNRLGE
NYITEAFKLA QEASPETDLY YNDYNNEQPA KRAGCIAIIK KIQAAGVRID GVGIQGHWHA
GKIPLQHIEE SILQYSALGI KVAITELDIE VLKRDFQGAE VSQQMKNDKG LNPYPNALPD
SLQQKLASDY EALFKLFIKH KDKISRVTFW GVHDGQSWLN GWPVRGRTNY PLLFDRQYNP
KPAFYKVIQA NQ
//
