AMY2_DROAN
ID AMY2_DROAN Reviewed; 494 AA.
AC O18345; B3LZH0; Q9GN73;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Alpha-amylase 2;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amy58; Synonyms=Amy2; ORFNames=GF18843;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tai 13-1610;
RX PubMed=9618501; DOI=10.1073/pnas.95.12.6848;
RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.;
RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila
RT melanogaster and the Sophophora subgenus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RC STRAIN=371-1, Beruwala, Bouake, Brazzaville, Colombo, Guadeloupe,
RC Korat3422, Lambir, Mauritius, Mexico, Porto Rico, Reunion, Sao Paulo, and
RC Tai 13-1610;
RX PubMed=11040291; DOI=10.1007/s002390010102;
RA Da Lage J.-L., Maczkowiak F., Cariou M.-L.;
RT "Molecular characterization and evolution of the amylase multigene family
RT of Drosophila ananassae.";
RL J. Mol. Evol. 51:391-403(2000).
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:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; U53698; AAC79122.1; -; Genomic_DNA.
DR EMBL; CH902617; EDV44149.1; -; Genomic_DNA.
DR EMBL; AF238958; AAG45312.1; -; Genomic_DNA.
DR EMBL; AF238959; AAG45313.1; -; Genomic_DNA.
DR EMBL; AF238960; AAG45314.1; -; Genomic_DNA.
DR EMBL; AF238961; AAG45315.1; -; Genomic_DNA.
DR EMBL; AF238962; AAG45316.1; -; Genomic_DNA.
DR EMBL; AF238963; AAG45317.1; -; Genomic_DNA.
DR EMBL; AF238964; AAG45318.1; -; Genomic_DNA.
DR EMBL; AF238965; AAG45319.1; -; Genomic_DNA.
DR EMBL; AF238966; AAG45320.1; -; Genomic_DNA.
DR EMBL; AF238967; AAG45321.1; -; Genomic_DNA.
DR EMBL; AF238968; AAG45322.1; -; Genomic_DNA.
DR EMBL; AF238969; AAG45323.1; -; Genomic_DNA.
DR EMBL; AF238970; AAG45324.1; -; Genomic_DNA.
DR EMBL; AF238971; AAG45325.1; -; Genomic_DNA.
DR EMBL; AF238972; AAG45326.1; -; Genomic_DNA.
DR EMBL; AF238973; AAG45327.1; -; Genomic_DNA.
DR EMBL; AF238974; AAG45328.1; -; Genomic_DNA.
DR EMBL; AF238975; AAG45329.1; -; Genomic_DNA.
DR EMBL; AF238976; AAG45330.1; -; Genomic_DNA.
DR EMBL; AF238977; AAG45331.1; -; Genomic_DNA.
DR RefSeq; XP_001955588.1; XM_001955552.2.
DR AlphaFoldDB; O18345; -.
DR SMR; O18345; -.
DR STRING; 7217.FBpp0122035; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblMetazoa; FBtr0123543; FBpp0122035; FBgn0261676.
DR GeneID; 6501610; -.
DR KEGG; dan:6501610; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; O18345; -.
DR OMA; ACTGNTI; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; O18345; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 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 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; SSF51445; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW Hydrolase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..494
FT /note="Alpha-amylase 2"
FT /id="PRO_0000001361"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 202
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 304
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 343
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 306
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 153..167
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 376..382
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT CONFLICT 25
FT /note="A -> P (in Ref. 1; AAC79122)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="V -> A (in Ref. 1; AAC79122)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> A (in Ref. 1; AAC79122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 53576 MW; 3886599639E9126C CRC64;
MFLAKSIVCL ALLAVANAQF NTNYASGRSG MVHLFEWKWD DIAAECENFL GPYGYAGVQV
SPVNENAVKD SRPWWERYQP ISYKLVTRSG NEEQFASMVR RCNNVGVRIY VDVVFNHMAA
DGGTYGTGGS TASPSSKSYP GVPFSSLDFN PTCAISNYND ANQVRNCELV GLRDLNQGNS
YVQEKIVEFL NHLIDLGVAG FRVDAAKHMW PADLGVIYGS LKNLNTDHGF ESGAKAYIVQ
EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKAFRGKNQL QYLVNWGVSW GFAASDRSLV
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT
DGQNIASPSF NSDNSCSGGW VCEHRWKQIY NMVGFRNAVG SDAIQNWWDN GSNQIAFSRG
SKGFVAFNND NYDLNSSVQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRANISIGSS
EDDGVLAIHV NAKL
