ID G3JS04_CORMM Unreviewed; 600 AA.
AC G3JS04;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Maltase {ECO:0000313|EMBL:EGX88650.1};
GN ORFNames=CCM_08695 {ECO:0000313|EMBL:EGX88650.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX88650.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX88650.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX88650.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126405; EGX88650.1; -; Genomic_DNA.
DR RefSeq; XP_006673895.1; XM_006673832.1.
DR AlphaFoldDB; G3JS04; -.
DR STRING; 983644.G3JS04; -.
DR GeneID; 18170701; -.
DR KEGG; cmt:CCM_08695; -.
DR VEuPathDB; FungiDB:CCM_08695; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_1_2_1; -.
DR InParanoid; G3JS04; -.
DR OrthoDB; 3680211at2759; -.
DR Proteomes; UP000001610; 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:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 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:UP000001610}.
FT DOMAIN 18..443
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 600 AA; 68116 MW; 946C53C0896CA5BD CRC64;
MTVIGREKKW WKQASIYQIY PASFCDSNGD GIGDIPGITS KLDYIASLGV DAIWVCPMYD
SPQIDMGYDI SNYEDVYRPY GTVQDMETLI RETHARGMRI MLDLVINHTS DQHAWFKESR
ASKDSPKRDW YIWKPAKYSA TGERLPPNNW RGNFGGGSTW EWDEATQEYY LHLFATEQPD
LNWENPVTRK AIYASAMEFW LDRGVDGFRV DTVNMYSKHQ DFADAPVTDP KAPFQPAGFV
YCNGPRMHEF LSEMNAVLSR YGAITVGELP CTPDMAKVVK YVSAKEKQLD MVFQFDLVDV
GFGKTHKFET APRNWTLPDV KAAVERTQSI IRGTDAWTTA FIENHDQARS VSRFTDDSPE
FRVAGAKMLA LMQSCLSGTQ YIYQGQEIGC INTPKIGYPP ENYLDIDSSL YYKMVQECFG
ADNKAELDRA FSAMQYLARD HARVPIAWDG REKYGGFSEP AIKAGQDVAE PWMKVHPLAG
EINVAAQLDD PSSVLAFWRK MLAFRKEHAD VLVYGDYKGL QEDNKETFMF LKEAQGGAHR
VLVVLNFTKE PQTWTVPSAA ELGLPEQDLV NMTRILSTHE GKRAEQTLQP FEGHVYTISN
//
