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Database: UniProt
Entry: Q25593_OSTNU
LinkDB: Q25593_OSTNU
Original site: Q25593_OSTNU 
ID   Q25593_OSTNU            Unreviewed;       397 AA.
AC   Q25593;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   03-MAY-2023, entry version 97.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE   Flags: Fragment;
OS   Ostrinia nubilalis (European corn borer) (Pyralis nubilalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Crambidae; Pyraustinae; Ostrinia.
OX   NCBI_TaxID=29057 {ECO:0000313|EMBL:AAA03641.1};
RN   [1] {ECO:0000313|EMBL:AAA03641.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Foster P.G., Hickey D.A.;
RT   "Ostrinia nubilalis alpha-amylase cDNA.";
RL   Submitted (DEC-1993) 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         ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; U04226; AAA03641.1; -; Unassigned_DNA.
DR   AlphaFoldDB; Q25593; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          1..297
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          306..394
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAA03641.1"
SQ   SEQUENCE   397 AA;  44153 MW;  8057279B51F1C6DD CRC64;
     NVGVRIYVDA IINHMTGTWS ENVGTAGSTA TFGQWSYPAV PYGWNDFNWP NCVIQGSDYA
     NNAERVRNCE LSGLKDLNQG TEHVRTMIVN YMNHLIDLGV AGFRIDAAKH MWPGDLRVIY
     ERLRNLNTNH GFPAGARPYI YQEVIDLGGE AVTKHEYTPL AAVTEFKFGM ELSRAFQRGN
     QLRWLVNWGP QWGLMDSEDS LTFIDNHDNQ RGHGAGGNIL THRQPKEYKA AIAFMLAHPY
     GEPQLMSSYS FTDTEAGPPM NSNQDIISPS INSDGTCGNG WVCEHRWRQI FQMVQFRNVA
     GNTGLNDWWD NGSNQIAFCR GGQAFIAFNN DLWDLSQTLQ TCLPAGQYCD IISGSRSGNG
     CTGKVVTVGN DGRAHISVGA NEYDMMLAIH VGTQSRI
//
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