ID   XG74_HYPJQ              Reviewed;         838 AA.
AC   Q7Z9M8; G0RLY9;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Xyloglucanase {ECO:0000303|PubMed:15541296};
DE            Short=XG {ECO:0000303|PubMed:15541296};
DE            EC=3.2.1.155;
DE   AltName: Full=Cel74a {ECO:0000312|EMBL:AAP57752.1};
DE   Flags: Precursor;
GN   Name=cel74a {ECO:0000312|EMBL:AAP57752.1}; ORFNames=TRIREDRAFT_49081;
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241;
RN   [1] {ECO:0000312|EMBL:AAP57752.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=QM6a {ECO:0000312|EMBL:AAP57752.1};
RX   PubMed=12788920; DOI=10.1074/jbc.m304750200;
RA   Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S.,
RA   Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S.,
RA   Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M.,
RA   Yao J., Ward M.;
RT   "Transcriptional regulation of biomass-degrading enzymes in the filamentous
RT   fungus Trichoderma reesei.";
RL   J. Biol. Chem. 278:31988-31997(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a;
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
RN   [3] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15541296; DOI=10.1016/j.bbagen.2004.07.001;
RA   Grishutin S.G., Gusakov A.V., Markov A.V., Ustinov B.B., Semenova M.V.,
RA   Sinitsyn A.P.;
RT   "Specific xyloglucanases as a new class of polysaccharide-degrading
RT   enzymes.";
RL   Biochim. Biophys. Acta 1674:268-281(2004).
CC   -!- FUNCTION: Hydrolyzes the glucosidic bonds of unbranched Glc residues in
CC       tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has a
CC       low activity against beta-glucan and carboxymethylcellulose. Not active
CC       against Avicel, laminarin, xylan, galactomannan, linear and branched
CC       arabinans, galactan, polygalacturonic acid, starch, beta-D-Glcp, beta-
CC       D-cellobiose, beta-D-Galp, beta-D-Xylp, alpha-D-Xylp, alpha-L-Araf and
CC       alpha-L-Arap. {ECO:0000269|PubMed:15541296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so
CC         as to successively remove oligosaccharides from the newly-formed
CC         chain end after endo-initiation on a polymer molecule.; EC=3.2.1.155;
CC         Evidence={ECO:0000269|PubMed:15541296};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.3. {ECO:0000269|PubMed:15541296};
CC       Temperature dependence:
CC         Has a half life of 15 minutes at 60 degrees Celsius.
CC         {ECO:0000269|PubMed:15541296};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000269|PubMed:15541296}.
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DR   EMBL; AY281371; AAP57752.1; -; mRNA.
DR   EMBL; GL985067; EGR47596.1; -; Genomic_DNA.
DR   RefSeq; XP_006966240.1; XM_006966178.1.
DR   AlphaFoldDB; Q7Z9M8; -.
DR   SMR; Q7Z9M8; -.
DR   STRING; 51453.EGR47596; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH74; Glycoside Hydrolase Family 74.
DR   CLAE; XEG74A_TRIRE; -.
DR   EnsemblFungi; EGR47596; EGR47596; TRIREDRAFT_49081.
DR   GeneID; 18485235; -.
DR   KEGG; tre:TRIREDRAFT_49081; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_49081; -.
DR   eggNOG; ENOG502QR03; Eukaryota.
DR   HOGENOM; CLU_004180_1_0_1; -.
DR   BioCyc; MetaCyc:MON-16608; -.
DR   BRENDA; 3.2.1.155; 6451.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0033950; F:xyloglucan-specific exo-beta-1,4-glucanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..838
FT                   /note="Xyloglucanase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395871"
FT   DOMAIN          802..838
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          750..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q70DK5"
FT   ACT_SITE        469
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q70DK5"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   838 AA;  87133 MW;  FBE3D08F2A74FA84 CRC64;
     MKVSRVLALV LGAVIPAHAA FSWKNVKLGG GGGFVPGIIF HPKTKGVAYA RTDIGGLYRL
     NADDSWTAVT DGIADNAGWH NWGIDAVALD PQDDQKVYAA VGMYTNSWDP SNGAIIRSSD
     RGATWSFTNL PFKVGGNMPG RGAGERLAVD PANSNIIYFG ARSGNGLWKS TDGGVTFSKV
     SSFTATGTYI PDPSDSNGYN SDKQGLMWVT FDSTSSTTGG ATSRIFVGTA DNITASVYVS
     TNAGSTWSAV PGQPGKYFPH KAKLQPAEKA LYLTYSDGTG PYDGTLGSVW RYDIAGGTWK
     DITPVSGSDL YFGFGGLGLD LQKPGTLVVA SLNSWWPDAQ LFRSTDSGTT WSPIWAWASY
     PTETYYYSIS TPKAPWIKNN FIDVTSESPS DGLIKRLGWM IESLEIDPTD SNHWLYGTGM
     TIFGGHDLTN WDTRHNVSIQ SLADGIEEFS VQDLASAPGG SELLAAVGDD NGFTFASRND
     LGTSPQTVWA TPTWATSTSV DYAGNSVKSV VRVGNTAGTQ QVAISSDGGA TWSIDYAADT
     SMNGGTVAYS ADGDTILWST ASSGVQRSQF QGSFASVSSL PAGAVIASDK KTNSVFYAGS
     GSTFYVSKDT GSSFTRGPKL GSAGTIRDIA AHPTTAGTLY VSTDVGIFRS TDSGTTFGQV
     STALTNTYQI ALGVGSGSNW NLYAFGTGPS GARLYASGDS GASWTDIQGS QGFGSIDSTK
     VAGSGSTAGQ VYVGTNGRGV FYAQGTVGGG TGGTSSSTKQ SSSSTSSASS STTLRSSVVS
     TTRASTVTSS RTSSAAGPTG SGVAGHYAQC GGIGWTGPTQ CVAPYVCQKQ NDYYYQCV