ID   GUN16_TRIHA             Reviewed;         490 AA.
AC   Q8J0I9; P84511;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Endo-1,6-beta-D-glucanase BGN16.3;
DE            EC=3.2.1.75;
DE   AltName: Full=Beta-1,6-glucanase BGN16.3;
DE   AltName: Full=Glucan endo-1,6-beta-glucosidase BGN16.3;
DE   Flags: Precursor;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1] {ECO:0000312|EMBL:CAC80492.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150;
RA   Montero M.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 29-42 AND 168-180, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 48131 / CBS 354.33 / CECT 2413 / VTT D-80150;
RX   PubMed=15982190; DOI=10.1111/j.1742-4658.2005.04762.x;
RA   Montero M., Sanz L., Rey M., Monte E., Llobell A.;
RT   "BGN16.3, a novel acidic beta-1,6-glucanase from mycoparasitic fungus
RT   Trichoderma harzianum CECT 2413.";
RL   FEBS J. 272:3441-3448(2005).
CC   -!- FUNCTION: Has highest activity on the linear beta-1,6-glucan pustulan.
CC       Lower activity against yeast glucan and laminarin (beta-1,3-glucans
CC       with beta-1,6-branches). No activity on colloidal chitin, pachyman,
CC       starch, cellulose, nigeran, dextran or gentobiose.
CC       {ECO:0000269|PubMed:15982190}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC         glucans.; EC=3.2.1.75; Evidence={ECO:0000269|PubMed:15982190};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=390 umol/min/mg enzyme {ECO:0000269|PubMed:15982190};
CC       pH dependence:
CC         Optimum pH is 5.0. At least 20% of maximum activity is retained
CC         between pH 4.0 and 7.0. {ECO:0000269|PubMed:15982190};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. After 30 min incubation at
CC         50 degrees Celsius in the absence of substrate 50% of activity is
CC         lost. {ECO:0000269|PubMed:15982190};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:15982190}.
CC   -!- INDUCTION: By fungal cell walls. {ECO:0000269|PubMed:15982190}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000255}.
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DR   EMBL; AJ243823; CAC80492.1; -; mRNA.
DR   AlphaFoldDB; Q8J0I9; -.
DR   SMR; Q8J0I9; -.
DR   CAZy; GH30; Glycoside Hydrolase Family 30.
DR   CLAE; BGN30P_TRIHA; -.
DR   SABIO-RK; Q8J0I9; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:UniProtKB.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IDA:UniProtKB.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR033452; GH30_C.
DR   InterPro; IPR001139; Glyco_hydro_30.
DR   InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11069; PTHR11069; 1.
DR   Pfam; PF02055; Glyco_hydro_30; 1.
DR   Pfam; PF17189; Glyco_hydro_30C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:15982190"
FT   CHAIN           29..490
FT                   /note="Endo-1,6-beta-D-glucanase BGN16.3"
FT                   /evidence="ECO:0000269|PubMed:15982190"
FT                   /id="PRO_0000042853"
FT   ACT_SITE        243
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04062"
FT   ACT_SITE        339
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04062"
SQ   SEQUENCE   490 AA;  51890 MW;  5900F8B8D4B6E9F7 CRC64;
     MRYALIASML GQAAISVAMP SEPAHSPRAA GAQAYASNQA GNYKLTSIAA PVQGNGSPGP
     STWNLSIDDT SSGYKQKIVG FGAAVTDATV SAFNELSAST LSQLLDELMT GAGASFSLMR
     HTIGASDLSG DPAYTYDDNG GNADPGMTGF NLGDRGTAMA TMLAQMKGLN SNLQIFGSPW
     SAPGWMKLNN AIDGNTNNNN LNDGYLTNNG AQYSAAFAQY FVKYIQAFES HGATINAITL
     QNEPLNSQAG YPTMYMFSYE QGDLIQNYVA PALKAAGLST KIWAYDHNTD QPDFPEQVMG
     IAADDVSAVA WHCYATNLDW TVLTNFHNSY PNTDQYMTEC WTPSTGAWNQ AASFTMGPLQ
     NWARGVAAWT LGTTAQDGPH LSSGGCGTCT GLVTINNGQY TFQTAYYMMA QFSKFMPVGA
     TVLSGTGSYT YSGSGGVQSV ASLNPDGTRT VVIENTFGND IYIHLSTSSG QEWSGNVPTN
     SVTTWVLPAV