ID K5XIW3_AGABU Unreviewed; 882 AA.
AC K5XIW3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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=AGABI1DRAFT_54075 {ECO:0000313|EMBL:EKM83267.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM83267.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Has both alpha- and beta-glucosidase activity.
CC {ECO:0000256|ARBA:ARBA00025512}.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; JH971386; EKM83267.1; -; Genomic_DNA.
DR RefSeq; XP_007326191.1; XM_007326129.1.
DR AlphaFoldDB; K5XIW3; -.
DR STRING; 597362.K5XIW3; -.
DR GeneID; 18830067; -.
DR KEGG; abp:AGABI1DRAFT54075; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR InParanoid; K5XIW3; -.
DR OMA; MHNVYGH; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000008493; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF67; ALPHA_BETA-GLUCOSIDASE AGDC-RELATED; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..882
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003886443"
FT DOMAIN 108..219
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 269..660
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 668..756
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 98492 MW; 31C16A7430A553E6 CRC64;
MHWTLLTLWL RLVSYICAAN VDPAALDACP GYNAQNVKTE GGTLTADLTL AGEACNVFGE
DLVALSLRVD YETKDRIHLK IVDANSSRYE IPDSVFPRPS SQAVSPDSAS IQFNFTTSPF
TFSIYRSSSQ EVLFSTASHP IIFEPQYLRV KTNLPDNANI YGFGEHTNPF HLPTDNMTLT
LWSRDSFGIP TGTNLYGNHP VYFEHRTTGT HGVFLLNSNG MDVKLSNTAG TSLEYNVIGG
IMDFYFLAGS ESDPAEVARQ YAEVVGLPAE VAYWTFGLHQ CRFGYKDFVD VAGVVSKYAA
AGIPLETMWT DIDYMDRRRI FTVDPQYFPM NRMREIVDFL HSHDQRFILM TDPAVAFIPD
DPDYTPYHRG KDLNIYLKAV NGSDFVALVW PGVTVYPDWF HPNVTEYWTN EFLDFYDPET
GLDIDGAWID MNEPANFCNL PCDDPFQQAK EQNLPPPRTN PAPDPNAPIF QNDSLSQLRK
RDDILNPPYA INNAAGALSS KTSMTNTVHA NGLQEYDAHN LYGSMMSIAT RAAMLARRPG
KRTLVITRST FAGIGAHVGK WLGDNVSLWE HYRFSIAGML NFATIFQVPM VGSDICGFSG
ETTETLCARW ATLGAFYPFM RNHNQDTSPS QEYYIWPLVT QAAKNAIDIR YRLMDYFYTA
FHQAHTDGTP VLHPLWFKYP KDANTFPLDL QFFFGDSILV SPVTEEGSTS VDIYLPDDIF
YNFTSLAPIE GTGSTVSLTN VDFTTIPVHI KGGVVLPLRV ESAMTTTELR TKDFEFVVAT
GQDGTASGSL YIDDGESIEQ SQMTTVDMSF KEGKLDVKGT FDFPTGVNVA RVRFLNVEKA
PKKVKVNGKN LGHSRIEHDA TNKVLDVIVD VAFDKDLSVE LS
//
