ID A0A401HZ78_9BACL Unreviewed; 760 AA.
AC A0A401HZ78;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN ORFNames=PA598K_02609 {ECO:0000313|EMBL:GBF74273.1};
OS Paenibacillus sp. 598K.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1117987 {ECO:0000313|EMBL:GBF74273.1, ECO:0000313|Proteomes:UP000288287};
RN [1] {ECO:0000313|EMBL:GBF74273.1, ECO:0000313|Proteomes:UP000288287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=598K {ECO:0000313|EMBL:GBF74273.1,
RC ECO:0000313|Proteomes:UP000288287};
RA Mizushima D., Miyazaki T., Shiwa Y., Kimura K., Fujita N., Yoshikawa H.,
RA Kimura A., Kitamura S., Hara H., Funane K.;
RT "A novel intracellular dextranase derived from Paenibacillus sp. 598K with
RT an ability of degrading cycloisomaltooligosaccharides.";
RL Submitted (MAR-2018) 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|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:GBF74273.1}.
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DR EMBL; BFBX01000035; GBF74273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401HZ78; -.
DR OrthoDB; 9809277at2; -.
DR Proteomes; UP000288287; 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-KW.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490:SF90; ENDO-1,4-BETA-XYLANASE A; 1.
DR PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF07554; FIVAR; 2.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR PRINTS; PR00134; GLHYDRLASE10.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS51760; GH10_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361174}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361174};
KW Hydrolase {ECO:0000256|RuleBase:RU361174};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361174};
KW Reference proteome {ECO:0000313|Proteomes:UP000288287};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 78..475
FT /note="GH10"
FT /evidence="ECO:0000259|PROSITE:PS51760"
FT DOMAIN 697..760
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT COILED 657..687
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 760 AA; 83725 MW; 5237F98D3D40648F CRC64;
MGTFAMQASA NTEDTAPQTV VKRFEALDEN AFTPATYRLA KMEYVKVKAL LDDPNATSDE
INAALQTLDT RIAALKVRSG SESLWKTYQD YFEIGNIYSG AGNLNPNNPR GLLTSTHFNS
ISAENVMKPE SLSTGNAGTA GTFRIFEGSN HASDQMVREA QEKDITVHGH VLVWHGQTPS
WVNGGTSGNY TRTQARENME RYIKTVVEHF DTYYPGVVAS WDVVNEAFVD GAPSIPADAN
WKDYLRKGNQ SGWYKSYSRD MSENQDPSDF LYDAFVFSRK YTDAKLFYND FNLYQDGKSK
LVAMMTKELN ERYKKEYPND PRQLIEGVGM QSHNYIMDTP PSSVENGILN LLSAGVDIGI
SELDLFAWFP YNGEPTRDYM DLRDRGIEHI IASNGTEQER NYWINRGVTN GSEIEVIQAE
LFAEYFQIYK KYAAHIDRVT FWGLNDSQSW RRGHNPLLWN SDFSPKDAFF AVSNPEAYLG
IEQKGAYLTG PASVVSGTSF HVNFNISAVN DSDFQKIFGQ DLTIQFDPNV LTFVEAQSLT
EGLVVLDSKE VSPGKIRFLV AALGEDKVIP ANGNFLDLTF VAKPITAPVE TAVAVDNVIL
ANGQGQELQV PGSTLTFDVM VEPVDKAALH TLISSAQSKV DAAVEGTAHG QYITGSKALL
QAAIDKAQAV ADQAQATQQQ IDQAAADLTL AITAFESSRI SVDVNGDDKV SVGDLAIVAA
GYGKKSTDSD WDKFKAGDVN KDGIIDIHDL TTVARKILES
//
