ID Q5IFF0_DROME Unreviewed; 232 AA.
AC Q5IFF0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Alpha amylase {ECO:0000313|EMBL:AAW31967.1};
DE Flags: Fragment;
GN Name=amy-p {ECO:0000313|EMBL:AAW31967.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAW31967.1};
RN [1] {ECO:0000313|EMBL:AAW31967.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZH23 {ECO:0000313|EMBL:AAW31966.1}, and ZH31
RC {ECO:0000313|EMBL:AAW31967.1};
RX PubMed=15483321; DOI=10.1093/molbev/msi015;
RA Thornton K., Long M.;
RT "Excess of amino acid substitutions relative to polymorphism between X-
RT linked duplications in Drosophila melanogaster.";
RL Mol. Biol. Evol. 22:273-284(2005).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AY752510; AAW31966.1; -; Genomic_DNA.
DR EMBL; AY752511; AAW31967.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5IFF0; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PeptideAtlas; Q5IFF0; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 182..232
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:AAW31967.1"
SQ SEQUENCE 232 AA; 25398 MW; 8F7B719CBFB9D3BB CRC64;
MNTDHGFASG SKAYIVQEVI DMGGEAISKS EYTGLGAITE FRHSDSIGKV FRGKDQLQYL
TNWGTAWGFA ASDRSLVFVD NHDNQRGHGA GGADVLTYKV PKQYKMASAF MLAHPFGTPR
VMSSFSFTDT DQGPPTTDGH NIASPIFNSD NSCSGGWVCE HRWRQIYNMV AFRNAVGSDE
IQNWWDNGSN QISFSRGSRG FVAFNNDNYD LNSSLQTGLP AGTYCDVISG SK
//
