ID A0A1R1EKF7_9BACL Unreviewed; 1350 AA.
AC A0A1R1EKF7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=BK138_22975 {ECO:0000313|EMBL:OMF52301.1};
OS Paenibacillus rhizosphaerae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=297318 {ECO:0000313|EMBL:OMF52301.1, ECO:0000313|Proteomes:UP000187172};
RN [1] {ECO:0000313|EMBL:OMF52301.1, ECO:0000313|Proteomes:UP000187172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0378 {ECO:0000313|EMBL:OMF52301.1,
RC ECO:0000313|Proteomes:UP000187172};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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:OMF52301.1}.
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DR EMBL; MRTP01000007; OMF52301.1; -; Genomic_DNA.
DR RefSeq; WP_076173123.1; NZ_MRTP01000007.1.
DR STRING; 297318.BK138_22975; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000187172; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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|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|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000187172};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:OMF52301.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1350
FT /note="Beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012661143"
FT DOMAIN 366..703
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 1169..1232
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1233..1293
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1296..1350
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 883..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 627
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10061"
SQ SEQUENCE 1350 AA; 144353 MW; E73A225955F542D0 CRC64;
MSKWMKQAFS AVIAAALIMP SGWLASDVSA DAESPDAGTV TVVYHETFAN GTGKAVQSGG
ANLAHVSGKV FDGNEDGGAL YVNNRTHDYD AADFNYTDLG IKNGKTYTIT VKGYVDAEAT
VPDDAQAYLQ TVDKSYGWLA GAAFKAGEDF TLTKEFTLDT SSGDTRLRVQ SNSAGATVPF
YLGDILITEK ADSGGGGNEE LPRDPALPFS TITFEDQTPG GFEGRSGTEK LTVTDEANHT
PDGAYALKVE GRTATWHGPS LRVEKYVDKG AEYKISAWVK LINPASSQIQ LSTQIGSDGS
ANYATLAPKT ISTDDGWVQF EGTYRYNSVG GEYLTLYVES SSNAEASFYI DDISFEKTGS
TPVEIQKDLV PLKNAYQNDF LIGNAISAED LEGVRLELLT MHHNVATAGN AMKPDALQPT
KGSFTFTAAD AMVDKVRAAG MQMHGHVLVW HQQSPAWMNT AQDAQGNTVP LSREEALVNL
RTHIRTVMEH FGDKVISWDV VNEAMNDNPP NPADWEASLR KSPWYNAIGP DYVEQAFLAA
REVLDDHPDW DIKLYYNDYN EDNQNKAQAI YNMVKAMNDR YAEAHPGKKL VDGVGMQGHY
NVNTNPENVK LSLEKFISLG VEVSISELDI QAGSNYELPE KLANAQGYLY AQLMKIFKDH
AADISRVTFW GMDDGTSWRA SSNPLLFDKN LQAKPAYYGV IDPDKFITEH PPESGNANQS
IAAYGTPVID GTVDAVWNQA AAMPVNRYQM AWQGATGTAK ALWDDHNLYV LIQVSDTQLD
KSSANAWEQD SVEVFLDENN AKTTFYQDDD GQFRINFDNE TSFNPPKIAD GFESATKAAG
TNYTVEMKIP LKTVTPANQL KLGFDAQVND AKDGARQSVA AWNDTTGNGY QDPSVFGVLT
LTGKPANPGD NGSGNEGGGG NNGGNGGSNG NGGNSGSGNG SNSSGNNSNG GGSPQTGITI
STDGAVTIKP EAKIQDGRAV STISADNLKK ALEQAAVPAN GKKLIVIEAA NPPGTGSVEV
QLPAQSLSGK ESFELLLKTG SAVLRIPSGM LSNQTDLSGQ VSVRIGTAST DHLNLTAADR
ERIGSRPVIE LSLAAGGRTL EWSNPAAPVT VEIPYKPTAE ELSHPDQIVV WYVDGQGQAT
PIPNGRYDAA TRTVVFHTNH FSTYAVAYAS TAFADLQNVP WAKPAIDAMA ARGVIHGMSE
GRFSPEAIIK RADFVALLVR ALELQGTGIP KTAFSDVDPI AYNRSELNTA NELGIAVGLP
DRTFKPDSPI TRQEMMVLTA RALTAAGKTV EGSGSLSAYA DAASIAGYAK DSAAALVKAG
IVTGSNGKIT PQGPLTRAEA AVILYRIWKL
//