ID G3JLD7_CORMM Unreviewed; 807 AA.
AC G3JLD7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Alpha-amylase, putative {ECO:0000313|EMBL:EGX90511.1};
GN ORFNames=CCM_06931 {ECO:0000313|EMBL:EGX90511.1};
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:EGX90511.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX90511.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX90511.1,
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; JH126403; EGX90511.1; -; Genomic_DNA.
DR RefSeq; XP_006672132.1; XM_006672069.1.
DR AlphaFoldDB; G3JLD7; -.
DR STRING; 983644.G3JLD7; -.
DR GeneID; 18168942; -.
DR KEGG; cmt:CCM_06931; -.
DR VEuPathDB; FungiDB:CCM_06931; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_1_1_1; -.
DR InParanoid; G3JLD7; -.
DR OMA; WNQPEVH; -.
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; IPR032091; Malt_amylase_C.
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 Pfam; PF16657; Malt_amylase_C; 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 255..667
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 807 AA; 91194 MW; DB01D2BADEBBCFA2 CRC64;
MEICNGSAAA SARVGSSGWS ENIPQTSYRG SKLFTTSYRE MLQDQLGDAR HAAAPPKAYP
RPARCRSLVQ GCGHSAVALQ PGTRHKAQGM VISPMGFLKQ VADIDASCDD QGLPSYASSV
GRAIAVTDDL RFYISNLAVF SKIHILETRC VWRWSKAAIA EDHFSILPNE KKNQETIDRH
TGIRRRIRVA RWSLGSYAIP SLRRGSDNGP ELDGLRYRFL GFSLLSKDET TGEILTMPGQ
KDQLRTWWKE SAVYQIYPAS FQDSNGDGVG DLKGIISRVD YLKELGVDIV WLSPIFKSPQ
VDMGYDVSDY RAIHPPYGDI ADVDTLKDKL HERGMKLVLD LVMNHTSDQH EWFQASRKSK
DNPYRDWYIW RPPRYDAHGQ RQPPNNWDSH FQGSAWEYDE ATDEYYLRLF AREQPDLNWE
NPAVRAACYD TTRFWLDRGA DGFRLDVINF ISKDQRFPDS DRAFAKGTEY YACGPRLHEY
LKELGAILQE YDAFSVGEMP CVGDEQELLN AVGADRGELS MIFHFEFMDL DHGAEGKFSP
KQMTLGEIRQ TLNKWQRFMY DNNGWNALYL ENHDQPRAVS RFASDAPEHR AASAKMLAVF
MAFQAGTPFI YQGQEIGMTN LPKEWPMDEY QDIDCLNHWN LRKDAADEAT KAALKVEYQK
KSRDNARTPM QWDGTAHAGF TTGDAKPWMR VHDNYPQVNA AAQVRDASSV YAAYRAVLGE
RRARKDIFVY GDFAAVDETH DKVLAYRRTA ANGDTALVAC NFSADAVTWA FEGGTPREVV
FSPTGKTTAD VDGKVELGPY EAIALLL
//
