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 24-JAN-2024, entry version 95.
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; 431241.Q7Z9M8; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH74; Glycoside Hydrolase Family 74.
DR CLAE; XEG74A_TRIRE; -.
DR GlyCosmos; Q7Z9M8; 2 sites, No reported glycans.
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 OrthoDB; 1328190at2759; -.
DR BioCyc; MetaCyc:MONOMER-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 CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
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
//
