ID A0A179F3Z0_METCM Unreviewed; 430 AA.
AC A0A179F3Z0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=glucan endo-1,6-beta-glucosidase {ECO:0000256|ARBA:ARBA00038935};
DE EC=3.2.1.75 {ECO:0000256|ARBA:ARBA00038935};
DE AltName: Full=Beta-1,6-glucanase B {ECO:0000256|ARBA:ARBA00042025};
DE AltName: Full=Endo-1,6-beta-D-glucanase B {ECO:0000256|ARBA:ARBA00041472};
DE AltName: Full=Endo-1,6-beta-glucanase B {ECO:0000256|ARBA:ARBA00043257};
GN ORFNames=VFPPC_09937 {ECO:0000313|EMBL:OAQ59829.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ59829.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ59829.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ59829.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. Acts on lutean,
CC pustulan and 1,6-oligo-beta-D-glucosides.
CC {ECO:0000256|ARBA:ARBA00037628}.
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:0000256|ARBA:ARBA00036633};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAQ59829.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSBJ02000004; OAQ59829.1; -; Genomic_DNA.
DR RefSeq; XP_018137790.1; XM_018288393.1.
DR AlphaFoldDB; A0A179F3Z0; -.
DR STRING; 1380566.A0A179F3Z0; -.
DR GeneID; 28852387; -.
DR KEGG; pchm:VFPPC_09937; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000078397; Chromosome 4.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR PANTHER; PTHR31297:SF39; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:OAQ59829.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..430
FT /note="glucan endo-1,6-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008101204"
FT DOMAIN 102..355
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 430 AA; 48178 MW; C3C3721668F3867C CRC64;
MHLSALVLLF LTNAVSAWLP HERDLEAFNQ TARFEKLGKR FKPSLPNGVT KIRGVNFGGW
LICEPWMMPN EWGNVMGCGD SASEFDCMRD HYAGGNREAG NQKFENHWRD WINPDTVQSV
HDVGLNTIRI PIGYWSYTDI VDTASEPFAD GSRMLPYLDA VVQKAADLGI YVIIDLHGAP
GGQQEDAFTG QINKPAGFFN DYNFGRAEKW LSWMTNRIHT NSAYSTVGMI EVLNEPVSKH
DAGGRYPAPG EDPGLVQTYY PAALKAVRDA EESLNVPDGK KLHVQFMSSK WDSGDARTVA
VVANDPMTAF DDHNYIGFAL GSNNGDQYQL MHSACTDSRV VSGQAFEFTG EWSMTSNVDW
SDGAFFKKFF TAQQQLYEKP GMDGWVYWTW KTELNDPRWT YSYATSLKYV PTDAAGLESN
VYQDVCNGFT
//