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-MAY-2023, entry version 60.
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; Bacillota; 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 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 CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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 PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF03442; CBM_X2; 1.
DR SMART; SM01067; CBM_3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
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
//
