ID   XG74_PAESP              Reviewed;        1027 AA.
AC   Q3MUH7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Xyloglucanase {ECO:0000312|EMBL:BAE44527.1};
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=xeg74 {ECO:0000312|EMBL:BAE44527.1};
OS   Paenibacillus sp.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=58172;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAE44527.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-52; 380-394 AND
RP   455-469, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=KM21 {ECO:0000312|EMBL:BAE44527.1};
RX   PubMed=16332739; DOI=10.1128/aem.71.12.7670-7678.2005;
RA   Yaoi K., Nakai T., Kameda Y., Hiyoshi A., Mitsuishi Y.;
RT   "Cloning and characterization of two xyloglucanases from Paenibacillus sp.
RT   strain KM21.";
RL   Appl. Environ. Microbiol. 71:7670-7678(2005).
CC   -!- FUNCTION: Hydrolyzes the glucosidic bonds of unbranched Glc residues in
CC       tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. May have
CC       a dual endo- and exo- mode of action towards xyloglucan, or may have an
CC       endo-processive mode of action. {ECO:0000269|PubMed:16332739}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0-6.5. Stable between pH 5.0 and 7.5.
CC         {ECO:0000269|PubMed:16332739};
CC       Temperature dependence:
CC         Optimum temperature is 60-70 degrees Celsius. Stable up to 55 degrees
CC         Celsius. {ECO:0000269|PubMed:16332739};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000269|PubMed:16332739}.
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DR   EMBL; AB212090; BAE44527.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MUH7; -.
DR   SMR; Q3MUH7; -.
DR   CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR   CAZy; GH74; Glycoside Hydrolase Family 74.
DR   PRIDE; Q3MUH7; -.
DR   KEGG; ag:BAE44527; -.
DR   BRENDA; 3.2.1.151; 6850.
DR   BRENDA; 3.2.1.155; 6850.
DR   SABIO-RK; Q3MUH7; -.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.710; -; 1.
DR   InterPro; IPR005102; Carbo-bd_X2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR001956; CBM3.
DR   InterPro; IPR036966; CBM3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF00942; CBM_3; 1.
DR   Pfam; PF03442; CBM_X2; 1.
DR   SMART; SM01067; CBM_3; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51172; CBM3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Repeat; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000269|PubMed:16332739"
FT   CHAIN           33..1027
FT                   /note="Xyloglucanase"
FT                   /evidence="ECO:0000269|PubMed:16332739"
FT                   /id="PRO_0000395872"
FT   REPEAT          134..143
FT                   /note="BNR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          185..196
FT                   /note="BNR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          252..262
FT                   /note="BNR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          357..367
FT                   /note="BNR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          537..545
FT                   /note="BNR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          717..727
FT                   /note="BNR 6"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          876..1027
FT                   /note="CBM3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT   ACT_SITE        70
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q70DK5"
FT   ACT_SITE        479
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70DK5"
SQ   SEQUENCE   1027 AA;  109165 MW;  982FB5898632D4F4 CRC64;
     MKTFLGKKLW MASLAVALAA GSFAALPEMT SAAPSEPYTW KNVVTGAGGG FVPGIIFNES
     EKDLIYARTD IGGAYRWNPA NESWIPLTDF VGWDDWNKNG VDALATDPVD PDRVYLAVGT
     YTNSWDKNNG AILRSTDRGD TWQTTTLPFK VGGNMPGRSM GERLVVDPND NRILYFGARS
     GNGLWRSSDY GATWSKVTSF PNPGTYVQDP ANEYGSDIVG LAWITFDKSS GQVGQATQTI
     YVGVADTAQS IYRSTDGGAT WTAVPGQPTG YLPHHGVLDA DGSLYITYSN GVGPYDGTKG
     DVWKLNTSTG AWTNISPIPS SSADNYFGYG GLAVDAQEPG TLMVATLNSW WPDAILFRSK
     DGGTTWTRIW EFDGYPNRKF RYTQNISAAP WLTFGTTPAP PEVSPKLGWM IGDLEIDPFD
     SDRMMYGTGA TIYGTNNLTN WDNNEKIDIS VMAKGVEEMA VLDLVSPPSG AHLVSGLGDV
     NGFRHDDLDQ PPAKMFSSPN YASTESLDFA ELNPSTMVRV GKADYAADPN AKSIGLSSDG
     GTNWYKANAE PAGTAGGGTV AISSDGSKLV WSTSDKGVHY SSTGGNSWTA STGIPAQAKV
     ISDRVNPNKF YGFAAGKIYV SVNGGVSFSQ TAAAGLPVDG NADLDAVPGV EGELWFAGGN
     EDGGPYGLWH STDSGASFAK LSNVEEADSI GFGKAAPGRN SAALYAVAQI DGTRGFFRSD
     DGGASWVRIN DDAHQYARVT TITGDPRIYG RVYLGTNGRG ILYADPVGGN NGGETPPVSH
     SGISPQSTEF DLNADRQADI PVALTLNGNT LASIRNGNHV LVQGSDYTMS GSQVFLSKTY
     LATLSKGVQS LVFRFSAGND ATLSITVKDT TQVPLPEGSI RIEMYNGTTS ATANSINPKF
     KLTNTGTAPL QLADVNIRYY YTIDGEKPLN FFCDWATAGS ANVTGTFSAL PAAVNGADHV
     LEIGFTASAG TLAAGQSTEV QVRFSKTDWT NFTQTDDYSF AASSTAYENW SKVTGYVSGT
     LQWGIEP