ID W6ZBA0_COCMI Unreviewed; 453 AA.
AC W6ZBA0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=COCMIDRAFT_2142 {ECO:0000313|EMBL:EUC49077.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC49077.1};
RN [1] {ECO:0000313|EMBL:EUC49077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC49077.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR EMBL; KI963935; EUC49077.1; -; Genomic_DNA.
DR RefSeq; XP_007684385.1; XM_007686195.1.
DR AlphaFoldDB; W6ZBA0; -.
DR GeneID; 19120059; -.
DR KEGG; bor:COCMIDRAFT_2142; -.
DR eggNOG; ENOG502RBRB; Eukaryota.
DR HOGENOM; CLU_004624_7_0_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
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:EUC49077.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..453
FT /note="glucan endo-1,6-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004889878"
FT DOMAIN 102..391
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 453 AA; 51669 MW; 696D3FC8BA321148 CRC64;
MVRGFSLLTA LLAASAHAWM PEHRELGAFN RTSNYLSKRA HSLPNWKVRG VNLGGWLLSE
PWMMNEEWKT MGCGNTCSEF DCVSALGQSK ADKAFNDHYA RWITPSMIQD MYNAGLNTIR
IPIGYWSLRS IVDSSEKFPT MDLQYLDAIV QKAADLGMFV VMDLHGAPGA QKTLDAFTGQ
CLPVSHLPGF FTQYNYDRAT KWLDWMTRRI HTKPAYKSAI GIIGVVNEPQ TSRDQGGMPK
EELDTLTQVY YPQALKAVRA AEQDLNIPET ERLHVQFMDS LWGAGNPQSH LPPSDTRVVY
DDHNYIGGAV VAKNPNAKQA DYMYYTCFED DRLSDGDTPK MVQEWSLTVR NEYSAEFDWK
LAQNEAFYKQ WFVAQQRLYE RTGGWIFWSW RTQLNDPRWD YSYLVWKKWV PTTAAGLDAS
VKQDVCTKYF GNQGMIAKTK GMTLRRGGST IPL
//
