ID D9S9N9_FIBSS Unreviewed; 467 AA.
AC D9S9N9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN OrderedLocusNames=FSU_1195 {ECO:0000313|EMBL:ADL24722.1};
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL24722.1, ECO:0000313|Proteomes:UP000000517};
RN [1] {ECO:0000313|Proteomes:UP000000517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) 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; CP002158; ADL24722.1; -; Genomic_DNA.
DR RefSeq; WP_014545521.1; NC_017448.1.
DR AlphaFoldDB; D9S9N9; -.
DR STRING; 59374.FSU_1195; -.
DR GeneID; 34755112; -.
DR KEGG; fsc:FSU_1195; -.
DR PATRIC; fig|59374.8.peg.1156; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_020161_6_0_0; -.
DR OrthoDB; 9815836at2; -.
DR Proteomes; UP000000517; 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; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF18962; Por_Secre_tail; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:ADL24722.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..467
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003128038"
FT DOMAIN 51..353
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 467 AA; 52410 MW; E1F7B9D7CCD26D28 CRC64;
MKKHRISKFI LSAAFLGAGF MNAQAADETI RELAKERGRF IGTILNSEWF NDAIEPEFEE
IHKTQFNVVV AENEMKFDAT EPKEDEFNFE KGDKMVKYAQ ANGLRVRGHA LAWHSQVANW
VNDYKGQKEK LLAVLKNHIT KVVGHWKGKI AEWDVVNEAV NDDYNADWRS TNSVWYEGIG
AEFLDSAFVW AHEADPDAEL CYNDYSIEWG LREGSKASFV VEQIKRWKAN NIPITCVGTQ
THIEIAHETT PQNVRALAKA LAELGVTLNI TELDIGFSKG SAGKLTEADY AKQGHLYRQF
MDVFLEEPNM GEFVIWGLTD AHSWLDEQQG KTEGLLYDKQ YNPKPAYDSV MASLKAHPAS
EVKTPYPESV LNPPKDCGTG NCDDPIAIKT LAKLNNISIH LAGRTLFVTG LALKTATKVD
IFDMQGHLVF SAKNVKGNIE LSSTPEGLYV IQIRQGVTRL TKRITIK
//
