ID A0A238Y9F0_9BACT Unreviewed; 364 AA.
AC A0A238Y9F0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=SAMN06269173_10534 {ECO:0000313|EMBL:SNR67371.1};
OS Hymenobacter mucosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411120 {ECO:0000313|EMBL:SNR67371.1, ECO:0000313|Proteomes:UP000198310};
RN [1] {ECO:0000313|EMBL:SNR67371.1, ECO:0000313|Proteomes:UP000198310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28041 {ECO:0000313|EMBL:SNR67371.1,
RC ECO:0000313|Proteomes:UP000198310};
RA Kim H.J., Triplett B.A.;
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}.
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DR EMBL; FZNS01000005; SNR67371.1; -; Genomic_DNA.
DR RefSeq; WP_055562180.1; NZ_FZNS01000005.1.
DR AlphaFoldDB; A0A238Y9F0; -.
DR Proteomes; UP000198310; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:SNR67371.1}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..364
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011305031"
FT DOMAIN 29..364
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 364 AA; 42265 MW; 804421C8805DC479 CRC64;
MKSTVFTFPK LALGALLVSC AGLLSSQHPA ADKGLKDYYK NYFPIGVAVG PQSIKGAEAE
LIKQQFNSVT PENAMKMGPI HPEENRYFWT DADAIVNFAQ ANKLRVRGHN LLWHEQTPKW
LFKDAQGKPV SKEVLLKRLH DHIFTVVKRY KGKIYAWDVV NEAIADNPSE FLRNSEWYQI
CGEDFIAKAF EYAHEADPKA VLFYNDYNTE RPEKRERVYK LLKKLVDAKV PIHAVGLQGH
WSLQEPTEAE LRKAIEQYSS LGLKVQITEL DVSVYPWEKE RREKRPGELD TYTPEVEQKQ
AAQYKMFFRV FRDYKNVLTG VTFWNVSDQY SWLDTYPVAG RKNYPLLFDQ NLKPKRAYQE
VVKF
//
