ID W6ZKW3_COCMI Unreviewed; 1244 AA.
AC W6ZKW3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=COCMIDRAFT_88120 {ECO:0000313|EMBL:EUC48154.1};
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:EUC48154.1};
RN [1] {ECO:0000313|EMBL:EUC48154.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC48154.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; KI963944; EUC48154.1; -; Genomic_DNA.
DR RefSeq; XP_007685354.1; XM_007687164.1.
DR AlphaFoldDB; W6ZKW3; -.
DR STRING; 930090.W6ZKW3; -.
DR GeneID; 19127206; -.
DR KEGG; bor:COCMIDRAFT_88120; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_006962_0_0_1; -.
DR OrthoDB; 2783936at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF29; BETA-GLUCOSIDASE L-RELATED; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EUC48154.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1244
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004887177"
FT DOMAIN 656..725
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT DOMAIN 810..949
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1208..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1066
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1244 AA; 133726 MW; 200E58B32888FA30 CRC64;
MRSAIFPLLA TAALSTAIPF DQPTSKRAVG SWDDAYTKAT AALAKLSQDE KIGIVTGTGW
SKSNCVGNTK PASSIGYPEL CLQDGPLGIR YVRGITAFAA GIHAASTWDI DLVRERGAFL
GNEAKQLGIH VQLGPSAGPL GKFAKGGRNW EGFGSDPYLQ GIMMAETIEG MQESGVQATA
KHWIVNEQEL NRDTMSSDVS DRVLRELYVW PFADAAHSKV AAFMCSYNKL NSTWACESEG
VMQKLLKDEL GHRGYIMSDW NAQHTTTGSA NGGLDMTMPG TDFSGGNVLW GPQLKTAISN
GQVQQSRLDD MVKRVLAAWY LLGQDKGYPA TSFNSWTIGS KQISGNHKTN VRATARDGTI
LLKNANGALP LKKPKSIAVI GTDSIVAPRG ANACVDRGCT EGVLTMGWGS GSVELPLDMV
APLDAIKTQA QKDGTTVTSS PTDNAQQGAS AAQNAEIAVV CINSNAGEGY ITVEGNAGDR
NNLDPWHNGN ELVKAVAAVN KKTVVVVHSV GPVIMEQWIE NPNVVAVVWA GLPGQEPGNG
VVDIIYGAAS PSGKLPYTIA KKESDYGTTI ARGDDKSWDL YIDYRYFDKQ NITPRFEFGF
GLSYTNFTYS DLTVTGKPSA GPATGAVGPG GPVDLFETVA TVTAKIANSG GVAGAEVPQL
YLGYPASTNS PPKQLRGFTK LKLEAGASGT ATFKLRRRDL SFWDEKTRKW TVATGEYTVF
VGASSRDVRL TGKIVVHLPN KSPNQLPLYN TSSVIMISQL FKPSTVRSAG LLGRATKSRV
QARYLATVQS NTERVMPAPS ARRATAVSNE PATFTIKNGP IFEGKSFGAK TNISGEAVFT
TSLVGYPESM TDPSYRGQIL VFTQPLIGNY GVPSSARDEH GLLRYFESPY IQASGIVVQD
YALKHSHWTA VESLGAWCAR EGVPAISGVD TREVVTYLRE QGSSLARISV GEEYDADEDE
AYIDPEAIHL VRRVSTKAPF HVSSSLGDMH VALIDCGVKE NILRSLVSRG ASVTCFPYDY
PIHKVAHHFD GVFISNGPGD PTHCTTTVHN LRKLFETSQL PVMGICMGHQ LIALAAGAKT
IKLKYGNRAH NIPALDLTTG KCHITSQNHG YAVDPTTLTS EWREYFTNLN DQSNEGLIHS
SRPIFSAQFH PEAKGGPLDS AYLFDKYIEN VQQYKEQQAS FSQRSNKPSP LLVDLLAKER
VGVHPDAPDF EGHAAGMDSQ QVNVGGPVAP PYQPITQKPV ASAA
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