ID Q023N8_SOLUE Unreviewed; 1039 AA.
AC Q023N8;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
DE Flags: Precursor;
GN OrderedLocusNames=Acid_2816 {ECO:0000313|EMBL:ABJ83802.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ83802.1};
RN [1] {ECO:0000313|EMBL:ABJ83802.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ83802.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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; CP000473; ABJ83802.1; -; Genomic_DNA.
DR AlphaFoldDB; Q023N8; -.
DR STRING; 234267.Acid_2816; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR KEGG; sus:Acid_2816; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_292852_0_0_0; -.
DR InParanoid; Q023N8; -.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08023; GH16_laminarinase_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR017803; CHP03437_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR NCBIfam; TIGR03437; Soli_cterm; 1.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF01833; TIG; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174};
KW Glycosidase {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}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1039
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004163809"
FT DOMAIN 250..536
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 753..1039
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
SQ SEQUENCE 1039 AA; 111593 MW; 0368CD65C936C004 CRC64;
MVECVLPSLA VLAALLSASV AFADPSPLIP GDPLACFTRV DGAATVTNVT VAGMPFTRAL
HVKTGTVASN ANAWDIRPRC FSTQAAKVND VVAVTFWMRA IAAPGNLGLT SFVLERNDSP
YTKSVTYTAA AGTDWKKLEV PFTMAETYAS NAYNFSFWVT FANQEIEIGG LAILDYGPGV
PFSSLGLTTW PYDERAPDAP WRAAAAGRID RYRKGDIVVI ARDDSGRTIP GAQIHARMKR
HAFGFGTAVA GDVIQRTDTT GQNYRDAIKK LFNKVVTENA LKWPTFESNG RQQADYMLPW
FAANGIEMVR GHNVIWPAAT YLPADVQAML KATPVNADAL RARIDKHIAD VMGYTKGKVT
EWDVLNEAYT NKDLQAVLGD SEMASWFVQA RTADPAIKLY INDYNILEAG GYDIQHINGY
QQIIRNLLAA GAPVDGIGLQ SHFDSNLTPP SRVIELLDQF ATFGRDLQVT EFDVSVADEQ
VQADYTRDFL TACFSHPAIK GFMMWGFWEG AHWKPQGAMI RRDWSTKPNY GVWNDLLYTQ
WWTDVRGATA ADGTWRTRGF LGDYDIEVTV NGATKTYPLR VSSNTEPVYL NTGKTPARAI
AAKGIVNGAS FAGGPIAPGE IVTIFGSGFG PGDTRVLFDG VAGQLIYALA GQVSAIVPSG
VTGTTQVRVE YQGVATEPVQ MTVAAAAPGI FMCPNKPGVA LVINASAGNV ISCNADFVPP
GSGSVITFFV TGEGGLRGGT SFGNIALASR CVADFAGAIY PGVTQINTCV PDAAPRDPAV
PMVFIAGGVA SPPASINLQT AWTLLWSDDF NGAAGTSPDP ARWTYDLGGG GWGNAELETY
TNTTDNVYHD GAGNLVIRAV KTGSGYTSAR IKTQGKFSVT YGKVEARIKI PYGQGIWPAF
WMLGADIDQV GWPACGEIDI MENIGKEPAT IHGTVHGPGY SGNSGIGAPF SLAAGGRFAD
DFHVYGIEWS PQSVAFFLDG TQYFEVTPAR LPAGKNWVYQ HPFFLILNVA TGGTWPGNPD
ATTTFPQQML VDWVHVSQR
//
