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Database: UniProt
Entry: A0A2G7G438_9EURO
LinkDB: A0A2G7G438_9EURO
Original site: A0A2G7G438_9EURO 
ID   A0A2G7G438_9EURO        Unreviewed;       968 AA.
AC   A0A2G7G438;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:PIG87626.1};
GN   ORFNames=AARAC_007240 {ECO:0000313|EMBL:PIG87626.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG87626.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG87626.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG87626.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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:PIG87626.1}.
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DR   EMBL; NEXV01000143; PIG87626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G7G438; -.
DR   STRING; 656916.A0A2G7G438; -.
DR   OrthoDB; 3680211at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   CDD; cd06532; Glyco_transf_25; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR002654; Glyco_trans_25.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF232; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT   DOMAIN          20..435
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   968 AA;  112324 MW;  8C8749551723297A CRC64;
     MATPANQNHR AWWKESSVYQ IWPCSFKDSN DDGIGDIPGI ISKLDHIKNL GIDIVWLCPS
     YKSPQVDMGY DIADYYDIAP EYGTVADVEK LIKGCHERGM KLLMDLVVNH TSDQHEWFKQ
     SRSSKDNEYR NWYIWKPARY DEQGNRQPPN NWVSHFQGSA WEWDEHTQEY YLHLYATEQP
     DLNWEHPPVR KAVHDIMRFW LDKGANGFRM DVINFISKDQ RFPDAPIKDP RTPWQWGDKY
     YANGPRLHEY FQELGKILKE YDTFSVGEMP FVTDTEEVLR AVKYDRNELN MIFNFEHVDI
     DHGKYDKFEP GSWKLTDLKS FFERWQKFMY DNDGWNALYW ENHDQPRSVD RYTNAKEEDR
     VIASKMLATI LALKAGSPFV YQGQEIGMGN VPLEWDIEEY KDIDCLNHWK RLPNDPEIQK
     IARQEYQKKS RDNGRTPPWM SVNPNYARGI NAEAQVNDPN STYSYWASVL GLRKKYVDIF
     VYGNYELVDR DSQEIFAYTR QYEGQKALVL ANWTDGTLEW DSSSNGVKAV KDVLLNTYDS
     ASDVKERFSG SKWSLHTHSR AAGPYQVIIV EEMTFVMSRS NTKTIIKLVA AACCSYFIFT
     ILLADREAYY STTRDVFRAG QHHLTEETTF DHINNETLGF QHIYAIGMKE RTDKRDYLTL
     AASFLGIKVD WRDGVYPDNV SEKSYPLKLG ESGVKPAAIG CWRAHMNTLI DIVENGYTTA
     LILEDDADWD VSLRQQLAEF ARGVRTLTNN QHESKKAPYG TNWDILWVGG CASGAHQNET
     DFYVIPNDPT VPNTTIRGPW ESPAGPSIKW RQEHPEWPVD STRYIYRANM GCCTFGYAVT
     LEGARRILAE LSINYLNLPV DNAMSDLCAG SNRPQLRCYA PFPNLIGTFR SEGYVSRDSD
     IDQWEDRKFE WHPALAYNMV YSTRLNIHRL VAGEETVYSQ WRESPDPWSK AEVKLGELEY
     PRGVFVSQ
//
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