ID A0A139GYQ1_9PEZI Unreviewed; 967 AA.
AC A0A139GYQ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha/beta-glucosidase agdC {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC578_5265 {ECO:0000313|EMBL:KXS95326.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95326.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS95326.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95326.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001657};
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}.
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:KXS95326.1}.
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DR EMBL; LFZN01000221; KXS95326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139GYQ1; -.
DR STRING; 321146.A0A139GYQ1; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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:UP000070133}.
FT DOMAIN 129..236
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 283..735
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 743..831
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 486..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 108073 MW; 14DD79A9980E70A6 CRC64;
MAVSNISIPL LNDMLQHFFA GAVFAASTSA AALIPRQANT ICPGYAASNV QTHDTGLTAS
LSLAGPACDS YGKDIENLKL VVDYDSTNRL HVKIEDDPSI AYQVPTSVFP PPHGSSPVAA
DESALQFDWI ETPFSFSVKR RSNGEVLFDS SAASLIFQDQ YLRLRTSLPA NPNLYGLGEH
SDNFRLNTTN NTRTLWSRDA YGIPAGTNLY GNHPVYFDHR GADGTHGVFL LSSSGMDVKI
DVTESGEQYL EYNLMSGILD LYFVAGPSPI EVSRQYAEIS HLPAMMPYWG FGFHQCRYGY
RDFYAIAEVI ANYSRANIPL ETMWTDIDYM YERYIMTTDP DRFSLPRVRD IVNYLHEHDQ
HYIVMVDPAV AYREKKYDDL PYETFLTAQD KGYFLQKNGT TYKGVVWPGV TAFPDWFHPD
VQEYWDNEFV NFFNAETGVD IDALWIDMNE AANFNYFGEN PEETQEERGF PPTRPALRSQ
PRPIPGFGPE FQPGAQPYPA DDYAYAPPWL APDSNPGDNK KVKRSAKTSA ATSKRQATMA
PSGASVIGYP NRNYLSPPYQ IDNENTYEDY GGLSNFTLDT DIVHYDGHVE LDVHNLYGTM
MSEASRHAML ARRPERRPMV ITRSTFAGAG RSVGKWLGDN LSTWELYRNS IQGMLNFASI
FQVPMVGSDI CGFGANTTET LCARWATLGA FYPFMRNHNG DTSIPQEFYL WETVADAARG
ALDIRYRLLD YIYTAMHKQS KDGSPLLNPL FYLYPEDKNT FGIELQFFYG DSLLVSPVTE
ENSTSVTIYL PEDRFYSWGS WDIVEGTGAD VTLKNISFTE IPLHVKGGSI LPVRKSSGYT
TTETRKQPFD IIVAPGKDGK ASGSLYLDDG DSLKQTATSE ITFAYENGVL DVGGTFAYTA
ENNRIASVTV LGVQAQGGRP SWRKGHEGGR GQGWKQCREN EWSHDSERSV TTVHVNQPLD
GELSVSL
//
