ID A0A0Q9MYC4_9BACL Unreviewed; 1308 AA.
AC A0A0Q9MYC4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=ASL11_11615 {ECO:0000313|EMBL:KRE70929.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE70929.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE70929.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE70929.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRE70929.1}.
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DR EMBL; LMSD01000010; KRE70929.1; -; Genomic_DNA.
DR RefSeq; WP_056613666.1; NZ_LMSD01000010.1.
DR STRING; 1736398.ASL11_11615; -.
DR OrthoDB; 9809277at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
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; 2.
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}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:KRE70929.1}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1308
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006379058"
FT DOMAIN 355..688
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 1127..1187
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1188..1251
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1254..1308
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 888..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 612
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1308 AA; 141616 MW; 2691E51C3F14B1F0 CRC64;
MRKKFVRIAL ILLVAALVIP SSLLTKVTKA ATTETITLYH ETFASGQGKA TRAGSANLSQ
VTGKTFTGND DGKALYVSNR VNNWDGADFK FSDIGLENGQ TYTVTATVYV DADVTVPSGA
QAGFQTVNGY QNTIYVNYEA GKALTLTKEF TVDTSKDSAL RINSNTAGAG VPFYLGDILV
TKNVAAGPVV ETPRLPAVDF PTITFEDQTN GGFAGRKGTE TLTVISDANH TEGGTSALKV
EGRTETWHGP SLRVEKYVDK GFEYKITAWV KLISPGSSQL QLSTQVGNAS ASYNTVDKKT
ISTEDGWVKF EGNYRYNTVP DEFLSIYVES SSSKDASFYI DDISFVESSA PISVQTNLTP
IKDAYRNDFL IGNAVSAADL DGVRLQLLKL HNNVVTAENA MKPDQTYNAN KEFDFATEDA
LVTKIQAAGL KLHGHVLVWH QQTPTWLTTT TDSLPLGRVE ALANLKTHIQ TVMEHYGNKV
ISWDVVNEAM NDNPSNPSNW HGALRQSPWK AAIGDDYVEQ AFLAAKEVLD AHPTWDIKLY
YNDYNEDNQN KAQAIYSMVK EINDRYALTH PGKLLIDGVG MQAHYNLNTK PDNVKLSLEK
FISLGVQVSI SELDITAGSN SRLTEKEANA QGSLYAQIFQ IFKAHAAHIE RVTFWGLNDA
TSWRASQNPQ LFNSDLQAKP AYFGVIDPAA FLAAHPPESV AQANQSTAKF ATPTIDGMAD
DAAWSQAPDM AINRYQQAWQ GASGVAKALW DDQNLYVLIQ VSNAELDKSS ANAYEQDSVE
IFLDENNAKT SSYEADDGQY RINFGNEQSF NPASKSAGVE SKTHVSGTNY TVEVKIPLKT
ITPEDNTKLG FDVQINDAKN GARQSVAAWN DTTGTGFQDT SVYGVLNLTG KVSNPSDGGD
PDPGSGTGSG SGTVPSTSTD TGSSGGTITP ELKTENGRTI AAISGDTLKK ALEQAAPTAN
VQKQIVIEVP KQANATSYEV QLPTQSLRGQ DNFELSVKTA DATIQIPSNM LSGVTENAEQ
VSLRVAKVSK DNMDTATREQ IGNRPVIELT LAAGDKVIAW NNPNAPVTVA IPYLPTEEEL
SDTDHIIIWY IDGQGKATPV PNGRYNAASG TVVFQTTHFS TYAVASVFKT FGDLQYVPWA
KQAIDTMASR DVIHGTDENS FSPEASIKRA DFIALLVRSL ELHTTSNDVA MFSDVPKTAY
YYNELVIAKA LGITTGFEDN TFKPDSPISR QDMMVLTTRA MAAADKQVQV GGTLDAYPDA
ASMSSYAKDS AAALVKSGIV NGKNDKLAPI DELTRAEGAV ILYRIWQK
//
