ID A0A0L1J8S6_ASPNO Unreviewed; 877 AA.
AC A0A0L1J8S6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Probable alpha/beta-glucosidase agdC {ECO:0000256|ARBA:ARBA00014002};
DE EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=ANOM_004427 {ECO:0000313|EMBL:KNG87818.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG87818.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG87818.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG87818.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG87818.1}.
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DR EMBL; JNOM01000069; KNG87818.1; -; Genomic_DNA.
DR RefSeq; XP_015408741.1; XM_015549684.1.
DR AlphaFoldDB; A0A0L1J8S6; -.
DR STRING; 1509407.A0A0L1J8S6; -.
DR GeneID; 26806231; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000037505; 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; 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; IPR030458; Glyco_hydro_31_AS.
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.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..877
FT /note="Probable alpha/beta-glucosidase agdC"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005553300"
FT DOMAIN 103..215
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 264..668
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 677..765
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 441..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 98758 MW; 32A9CFC65B497C8E CRC64;
MLGSLFLLVP LAGAAVIGSR ASTQQCPGYK ASNVQQNDQT LTADLTLAGK PCNTYGTDLP
NLKLLVEYQT DERLHVKIYD ADECVYQVPE KVVPRVDSGD GSSQDSALRF EYEKEPFSFT
VKRDKEVLFD SSAENLIFQS QYLKLRTWLP ENPHLYGLGE HSDSLRLSTT NYTRTFWNRD
AYGTPENSNL YGTHPVYYDH RGESGTHGVF LLNSNGMDVF IDKTADGKQY LEYNALGGVF
DFYFFTGSNP KEASIEYSKI VGLPAMQSYW TFGLHQCRYG YRDVYQVAEV VYNYSKAGIP
LETMWTDIDY MDRRRVFSLD PDRFPLEKMR ELVEYLHDHD QHYIVMVDPA VSVSDNGAFN
RGLEQGVFLK TQNGSLYKGA VWPGVTAYPD WFHSDTQDYW NSEFSTFFNA ETGVDIDGLW
IDMNEASNFC PDPCTDPEKY SIENNLPPAP PPVRPSSPRP LPGFPADFQP SSAGRSQKRV
FKAKNGLEGR NLINPPYKIR NAAGSLSNKT INTGIIHAGE GYAEYDTHNL YGTMMSSSSR
EAMQHRRPEV RPLVITRSTY AGAGRDVGHW LGDNFSKWEH YRISIAQGLA FASMFQIPMV
GADVCGFAGN TTEELCARWA SLGAFFTFYR NHNEIGNIGQ EFYNWPTVAE SARKAIDIRY
RLLDYIYTSF YKQSQTGEPF LQPMFYLYPE DEKTFAIDLQ FFYGDALLVS PVPDKGLTSV
DAYFPDDIFY DWYTGAPVRG HGANITLSNI DITHIPLHIR GGSIIPIRSS SAMTTTELRE
KSFQLIIAPG LDGTASGSLY LDDGDSLEQK ATLEVEFEYR RGVLHIDGKF ELHTSLLESV
TLLGHGKGGS RARREDGAKK TIQTNLELSK PTEIKLE
//
