ID A0A094KSJ3_9PEZI Unreviewed; 928 AA.
AC A0A094KSJ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=V502_00557 {ECO:0000313|EMBL:KFZ24973.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ24973.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ24973.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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:KFZ24973.1}.
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DR EMBL; JPKE01000208; KFZ24973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094KSJ3; -.
DR STRING; 1420915.A0A094KSJ3; -.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000029308; 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; 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:UP000029308};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..928
FT /note="Probable alpha/beta-glucosidase agdC"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001901442"
FT DOMAIN 104..225
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 274..705
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 713..801
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
SQ SEQUENCE 928 AA; 101821 MW; C8F597E6CD4723D4 CRC64;
MKVALSWLLA AAAAVSATSI EYRTTSNGDP LAKCPGYKAS NIKTGKSTLT ADLTLAGKAC
NVYGDDLKSL TLEVEYETDD RIHVKIQDAA NSVYQVPESV FPRPKATAGI KSAKSNIQFK
YKSNPFSFSI TRTKTGEVLF DSSAASIVFE SQYLRLRTSL PQNPNLYGLG EHSDSFRLNT
TDYIRTLWSQ DSYAIPAGAN LYGNHPVYYE HRTSGSHGVF FLNSNGMDIK IDNTNGKNQY
LEYNTLGGVL DFYFVAGPTP VAVAQQYAEV AGLPAMMPYW GLGFHNCRYG YEDAFEVAEV
IHNYSIAGIP LETMWTDIDY MDRRRVFSLD PERFPLGKMQ AINDYLHARD QKQIVMVDPA
VAYQDYPPYH SGIADDIFLK RDNGSTWLGV VWPGVSVFPD WFHTGVQDWW NNEFASFFAV
DGVNIDGLWI DMNEPSNFPC NFPCDDPFAA AVGFPPEAPA VRLPPRALPG FPCDFQPAGT
PCTASKERRV IEAPVVASAK VVERQAAGQQ LGLPGRDLLF PKYAIHNAAA FTVEDNAAGG
GISNHTVNTD VIHQNGIAMY DTHNLYGSMM SVASREAMQF RRPTERPLII TRSTFAGAGT
KVGKWLGDNV SSWNGYRITI RGMLAFASVF QVPMVGSDVC GFADNTTETL CARWAVLGAF
APFYRNHNGY IPQIAQEFYR WDSVAAAARK AIDIRYRLLD YIYTALHRQT LDGTPLVSPL
FYLYPNDKNT FDIETQYFFG PGILVSPVID EDSTSVSAYL PKDIFYDFFT HARVQGQGKA
VVINNLGTSD IALHYRGGAI VAQRVEGALT TTALRKHDFE LIVAIGADGK AAGELYLDDG
ISLVQKGTTS LQFVYDGKTL KVKGHYGYDA GVQIRQVTFL GLGLGVGGGK SCKVNGVKSK
STVKADTGAV VVQVGKGLAA DFTVEVDQ
//
