ID A0A261Q9C3_9BACT Unreviewed; 352 AA.
AC A0A261Q9C3;
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_03980 {ECO:0000313|EMBL:OZI09426.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI09426.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI09426.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI09426.1,
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:OZI09426.1}.
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DR EMBL; NMPS01000042; OZI09426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261Q9C3; -.
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:OZI09426.1}.
FT DOMAIN 16..352
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 352 AA; 41020 MW; 41048E31D490536A CRC64;
MRKRSLLVLL LTTALVAPEK GLKDYYKDYF PIGVAVNPRM VQPGPEADLI KAQFNSMTPE
NAMKMGPIHP EENRYNWADA DAIADFAQQN NIKLRGHTLC WHNQTPRWLF TDAEGKTVSR
EVLLARLKRH ITDVMGRYKG KIYAWDVVNE AVPDTGTSLY RKSKFYEIIG EDYIEKAFEY
AHEADPTAQL FYNDYNTENA SKRERIYQIL KKLTDKKIPI HGVGLQGHWS IYEPTAQELQ
ASIDKFAGLG LKVQITELDL SVYAKEHERR QRRETDKSEF TETMREKQVA QYKMIFDVFR
KNRDKLTGIT FWNLSDRYSW LDNFPVPGRK DYPLLFDEKG QPKKAYEGVV KF
//
