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Database: UniProt
Entry: A1CJM8_ASPCL
LinkDB: A1CJM8_ASPCL
Original site: A1CJM8_ASPCL 
ID   A1CJM8_ASPCL            Unreviewed;       587 AA.
AC   A1CJM8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Oligo-1,6-glucosidase {ECO:0000313|EMBL:EAW09352.1};
GN   ORFNames=ACLA_035550 {ECO:0000313|EMBL:EAW09352.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09352.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW09352.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027056; EAW09352.1; -; Genomic_DNA.
DR   RefSeq; XP_001270778.1; XM_001270777.1.
DR   AlphaFoldDB; A1CJM8; -.
DR   STRING; 344612.A1CJM8; -.
DR   EnsemblFungi; EAW09352; EAW09352; ACLA_035550.
DR   GeneID; 4702857; -.
DR   KEGG; act:ACLA_035550; -.
DR   VEuPathDB; FungiDB:ACLA_035550; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_1_2_1; -.
DR   OMA; NSTYHYW; -.
DR   OrthoDB; 3680211at2759; -.
DR   Proteomes; UP000006701; 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   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; 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:UP000006701}.
FT   DOMAIN          21..440
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   587 AA;  68952 MW;  E8852090AFCEB1DB CRC64;
     MTRSDTTQIH RAWWKECSVY QIWPASYKDS NDDGIGDIPG IVSKLDYIKN LGVDIVWLCP
     SYKSPQVDMG YDISDYYSIA DEYGTVADVE NLIQGCHQRG MKLLMDLVVN HTSDQHEWFK
     QSRSSKDNEY RNWYIWKPAK YDEQGNRHPP NNWVSHFQGS AWQYDELTDE YYLHLYATEQ
     PDLNWEHPPV RKAVHDIMRF WLDKGADGFR MDVINFISKD QAFPDAPVQD PRSIWQWADK
     YYANGPRLHE YLQGLGEILK EYDAFSVGEM PFVKDTQEVL KAVRYGRNEL NMIFNFEHVD
     IDHGKYDKFE PGEWKLTDLK DFFERWEKFM YENDGWNALY WENHDQPRSI DRYTNAKEEH
     RLVASKLLAT LLTLQAGTPF IYQGQELGMS NVPIEWGIEE YKDIDCLNHW HGLIKHKHFD
     TKAQEIAKRE YQKKSRDNAR TPVQWSSAPN AGFTGPNVKP WMSVNPNYVR INAEAEVEDP
     NSTYHYWAAV LGLRKKYLDL FVYGNYDMVD RDSQEIFAYT RQYENQKALV VGNFTDKTLD
     WSFAARGIKG VKEVLLNTYE GVEKASQRFS GESWSLRPYE AVVVLVQ
//
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