ID A0A089JX92_9BACL Unreviewed; 1333 AA.
AC A0A089JX92;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=R50912_08945 {ECO:0000313|EMBL:AIQ40140.1};
OS Paenibacillus sp. FSL R5-0912.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ40140.1, ECO:0000313|Proteomes:UP000029512};
RN [1] {ECO:0000313|EMBL:AIQ40140.1, ECO:0000313|Proteomes:UP000029512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ40140.1,
RC ECO:0000313|Proteomes:UP000029512};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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|ARBA:ARBA00000681,
CC ECO:0000256|RuleBase:RU361174};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR EMBL; CP009282; AIQ40140.1; -; Genomic_DNA.
DR RefSeq; WP_042233988.1; NZ_CP009282.1.
DR KEGG; paeq:R50912_08945; -.
DR HOGENOM; CLU_001408_1_0_9; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000029512; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00005; CBM9_like_1; 1.
DR Gene3D; 2.60.40.1190; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR031158; GH10_AS.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF06452; CBM9_1; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS00591; GH10_1; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51272; SLH; 3.
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:UP000029512};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:AIQ40140.1}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1333
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001844876"
FT DOMAIN 357..694
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 1152..1212
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1213..1276
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1279..1333
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 894..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 618
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1333 AA; 143160 MW; 306B1A6873957E26 CRC64;
MKRIIKQVSL VLLAAVLLLP AGGYIPAAQA AEAPAMVYHE TFGGGIGKAV QSGGASLSAV
TGVPFDGNAD GAALYVSNRV NNWDAVDFKF SDVGLKNGQT YTVTAVVYVD ANVALPSGAN
AALQTVDDYT NDAAVPYKAG ESVILTKKFT VDTSKKDYAL RINSNEAGAA VPFYLGDILF
TEEGAPGGGE EPVRDPALPF NTITFEDQTA GGFTGRAGTE LLTVTNEENH TADGAYALKV
EGRTSTWHGP SLRVEKYVDK GSEYTLSAWV KLIDPASAQL QLSTQVGNDS GASYVALSPK
TISTADGWVK FEGSYRYNSV GGEYLTLYIE SSNNTAASFY IDDITFEHTG TGPVDIQRDL
VPLKAAYQND FLIGNALSAE DLEGVRLDLL KMHHNVATAG NAMKPDALQP TKGNFTFTAA
DAMVNKVLAE GMKMHGHVLV WYQQSPDWMN LTTDAAGNKV PLGRAEALTN LRTHIQGVME
HFGGRVISWD VVNEAMNDNP SNPSNWQAAL RQAPWQDAIG ADYVEQAFLA AREVLDDHPE
WDIKLYYNDY NDDNQNKAQA IYSMVKEIND RYALAHPGKL LIDGVGMQAH YNINTNPDNV
KLSLEKFISL GVEVSITELD IQAGSDNKQT EKELVDQGYL YARLMDIYKT HAANIARVTF
WGMDDRTSWR ASSSPLLFDR DLQAKPAYYG VIDPAKYMAE HQPNTTEAKV SEAVYGTPVI
DGTADAIWSL APEMAVNRYQ MAWQGASGTA RALWDDQNLY VLVQVSDAQL DKSNTNVWEQ
DSVEVFLDEN LGRTTFYQDD DGQFRVNYDN EASFSPADIS AGFVSATKVA GTSYTLEMKI
PFKKITPAGG TKVGFDTQIN DAKSGVRQSV AAWNDTTGNG YQDTSVYGVL TLKSRDEQPE
PTTAPTPTPA ATTEPTAEPT ATPTPTPAPV SGGTNYVNST PTPKPVNLDS KDGVVTIRPE
VKNQGGEAKA AVTGDILRKA LEQAVPAADG MKQIVIDLPK QTGAASYEVE LPLQSLKGQA
NFVLVIKTDH ATLSIPSGQL AGITANTEYI SIRVKASPAA SPDAAAGSRP VVELKLSAGG
REMAWSNADM PITVSIPYKP AVEELGYSDS LLVRYLREDG HRTAVVNSRY DAANGSLVFQ
TSEFGTFAAA YAPLTFTDLG NLSWAKQAVA AMAARDLVQG TSSDNFSPAV PMSRADLTAS
LLKVLELKAT AESGAGFSDV GNHAEHFKEL AAAKQLGIVT GYADNSFKPD STISRQEMMV
IAARALKSAG IAAHGSGTLD AYADAERISA YAKDSLEALL KYGVVNGKNG RLAPDDTLTR
AEAAVILYRI WKL
//
