ID   6GAL_HYPRU              Reviewed;         479 AA.
AC   Q76FP5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Endo-beta-1,6-galactanase {ECO:0000312|EMBL:BAC84995.1};
DE            EC=3.2.1.164;
DE   Flags: Precursor;
GN   Name=6GAL {ECO:0000312|EMBL:BAC84995.1};
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC84995.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-55, FUNCTION, CATALYTIC
RP   ACTIVITY, AND MASS SPECTROMETRY.
RC   STRAIN=NBRC 31137 {ECO:0000269|PubMed:14565843};
RC   TISSUE=Conidium {ECO:0000269|PubMed:14565843};
RX   PubMed=14565843; DOI=10.1042/bj20031145;
RA   Kotake T., Kaneko S., Kubomoto A., Haque M.A., Kobayashi H., Tsumuraya Y.;
RT   "Molecular cloning and expression in Escherichia coli of a Trichoderma
RT   viride endo-beta-(1-->6)-galactanase gene.";
RL   Biochem. J. 377:749-755(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-31, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12543554; DOI=10.1016/s0008-6215(02)00405-6;
RA   Okemoto K., Uekita T., Tsumuraya Y., Hashimoto Y., Kasama T.;
RT   "Purification and characterization of an endo-beta-(1-->6)-galactanase from
RT   Trichoderma viride.";
RL   Carbohydr. Res. 338:219-230(2003).
CC   -!- FUNCTION: Hydrolyzes galactooligomers with a degree of polymerization
CC       higher than 3. Hydrolyzes radish root arabinogalactan-protein. Does not
CC       hydrolyze dextran, arabinan, starch, laminarin, beta-1,4- and beta-1,3-
CC       galactans, larch wood arabinogalactan or acid-insoluble
CC       polygalacturonic acid. {ECO:0000269|PubMed:12543554,
CC       ECO:0000269|PubMed:14565843}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->6)-beta-D-galactosidic linkages in
CC         arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield
CC         galactose and beta-(1->6)-galactaobiose as the final products.;
CC         EC=3.2.1.164; Evidence={ECO:0000269|PubMed:12543554,
CC         ECO:0000269|PubMed:14565843};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.3. Stable between pH 3.0 and 11.0 in the presence of
CC         BSA, and pH 4.0 and 9.5 in the absence of BSA.
CC         {ECO:0000269|PubMed:12543554};
CC       Temperature dependence:
CC         Loses 30% of activity after 10 minutes incubation at 50 degrees
CC         Celsius, activity is abolished after 10 minutes incubation at 60
CC         degrees Celsius. {ECO:0000269|PubMed:12543554};
CC   -!- MASS SPECTROMETRY: Mass=50687.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14565843};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AB104898; BAC84995.1; -; mRNA.
DR   AlphaFoldDB; Q76FP5; -.
DR   SMR; Q76FP5; -.
DR   CAZy; GH30; Glycoside Hydrolase Family 30.
DR   CLAE; GAL5F_TRIVI; -.
DR   PRIDE; Q76FP5; -.
DR   KEGG; ag:BAC84995; -.
DR   BioCyc; MetaCyc:MON-20546; -.
DR   BRENDA; 3.2.1.164; 6447.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR039743; 6GAL.
DR   InterPro; IPR039514; 6GAL-like.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR42767; PTHR42767; 1.
DR   Pfam; PF14587; Glyco_hydr_30_2; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:12543554,
FT                   ECO:0000269|PubMed:14565843"
FT   CHAIN           21..479
FT                   /note="Endo-beta-1,6-galactanase"
FT                   /evidence="ECO:0000269|PubMed:12543554,
FT                   ECO:0000269|PubMed:14565843"
FT                   /id="PRO_0000398806"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q45070"
FT   ACT_SITE        311
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q45070"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        25
FT                   /note="T -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  52762 MW;  1E5524252CE247B7 CRC64;
     MRSIVLPSLA LALFSQRARA DTTLTIDPTS NWGTWEGWGV SLAWWAKAFG NRDDLASVFF
     SRNNQAVNGQ TLPGLGFNIV RYNAGACSNN SYDGSTMVVS PNIKPSRQMD GFWLDWASSD
     PSSSSWNWNV DANQRAMLQK AKANGANIFE LFSNSPMWWM CNNHNPSGSG SSDNLQSWNY
     QNHAVYLADI AQHAQQSWRI QFQSVEAFNE PSSSWWTAEG TQEGCHFDVS TMATVIGYLN
     TELSSRGLSS FVASSDENTY DLAISTWQGF NSSTRNIVKR INVHGYQDGG GRRDTLYSLA
     SQAGKRLWNS EYGDSDASGK SMYQNLLLDF TWLHPTAWVY WQAIDGAGWG LIVGDNDNLT
     LSSASTKYFV LAQLTRHIRQ GMQILTTPDV NTAVAYDAGS QKLVIVTANW GSAQTITFDL
     TRARTAGSNG ATVPRWSTQT GGGDQYRSYT DTKINNGKFS ASFSSGQVQT FEVSGVVLQ