AMY1_DROAN
ID AMY1_DROAN Reviewed; 494 AA.
AC Q23835; B3LZH2; Q9GN69; Q9GN73;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-amylase 1;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amy35; Synonyms=Amy1; ORFNames=GF18844;
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=14629045; DOI=10.1007/s00239-003-2488-4;
RA Da Lage J.-L., Maisonhaute C., Maczkowiak F., Cariou M.L.;
RT "A nested alpha-amylase gene in Drosophila ananassae.";
RL J. Mol. Evol. 57:355-362(2003).
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, AND VARIANT LEU-2.
RC STRAIN=371-1, Bangalore, Beruwala, Bouake, Brazzaville, Colombo, Cuba,
RC Djeffa, Guadeloupe, Korat, Korat3422, Lambir, Mauritius, Mexico,
RC Porto Rico, Reunion, Sao Paulo, Tai 13-1610, Taka5, and Yaounde;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-206.
RC STRAIN=Tai 13-1610;
RX PubMed=8798339; DOI=10.1007/bf02339008;
RA Da Lage J.-L., Wegnez M., Cariou M.-L.;
RT "Distribution and evolution of introns in Drosophila amylase genes.";
RL J. Mol. Evol. 43:334-347(1996).
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; AAC79123.1; -; Genomic_DNA.
DR EMBL; CH902617; EDV44151.1; -; Genomic_DNA.
DR EMBL; AF238900; AAG45254.1; -; Genomic_DNA.
DR EMBL; AF238901; AAG45255.1; -; Genomic_DNA.
DR EMBL; AF238902; AAG45256.1; -; Genomic_DNA.
DR EMBL; AF238903; AAG45257.1; -; Genomic_DNA.
DR EMBL; AF238904; AAG45258.1; -; Genomic_DNA.
DR EMBL; AF238905; AAG45259.1; -; Genomic_DNA.
DR EMBL; AF238906; AAG45260.1; -; Genomic_DNA.
DR EMBL; AF238907; AAG45261.1; -; Genomic_DNA.
DR EMBL; AF238908; AAG45262.1; -; Genomic_DNA.
DR EMBL; AF238909; AAG45263.1; -; Genomic_DNA.
DR EMBL; AF238910; AAG45264.1; -; Genomic_DNA.
DR EMBL; AF238911; AAG45265.1; -; Genomic_DNA.
DR EMBL; AF238912; AAG45266.1; -; Genomic_DNA.
DR EMBL; AF238913; AAG45267.1; -; Genomic_DNA.
DR EMBL; AF238914; AAG45268.1; -; Genomic_DNA.
DR EMBL; AF238915; AAG45269.1; -; Genomic_DNA.
DR EMBL; AF238916; AAG45270.1; -; Genomic_DNA.
DR EMBL; AF238917; AAG45271.1; -; Genomic_DNA.
DR EMBL; AF238918; AAG45272.1; -; Genomic_DNA.
DR EMBL; AF238919; AAG45273.1; -; Genomic_DNA.
DR EMBL; AF238920; AAG45274.1; -; Genomic_DNA.
DR EMBL; AF238921; AAG45275.1; -; Genomic_DNA.
DR EMBL; AF238922; AAG45276.1; -; Genomic_DNA.
DR EMBL; AF238923; AAG45277.1; -; Genomic_DNA.
DR EMBL; AF238924; AAG45278.1; -; Genomic_DNA.
DR EMBL; AF238925; AAG45279.1; -; Genomic_DNA.
DR EMBL; AF238926; AAG45280.1; -; Genomic_DNA.
DR EMBL; AF238927; AAG45281.1; -; Genomic_DNA.
DR EMBL; AF238928; AAG45282.1; -; Genomic_DNA.
DR EMBL; AF238929; AAG45283.1; -; Genomic_DNA.
DR EMBL; AF238930; AAG45284.1; -; Genomic_DNA.
DR EMBL; AF238931; AAG45285.1; -; Genomic_DNA.
DR EMBL; AF238932; AAG45286.1; -; Genomic_DNA.
DR EMBL; AF238933; AAG45287.1; -; Genomic_DNA.
DR EMBL; AF238934; AAG45288.1; -; Genomic_DNA.
DR EMBL; AF238935; AAG45289.1; -; Genomic_DNA.
DR EMBL; AF238936; AAG45290.1; -; Genomic_DNA.
DR EMBL; AF238937; AAG45291.1; -; Genomic_DNA.
DR EMBL; AF238938; AAG45292.1; -; Genomic_DNA.
DR EMBL; AF238939; AAG45293.1; -; Genomic_DNA.
DR EMBL; AF238940; AAG45294.1; -; Genomic_DNA.
DR EMBL; AF238941; AAG45295.1; -; Genomic_DNA.
DR EMBL; AF238942; AAG45296.1; -; Genomic_DNA.
DR EMBL; AF238943; AAG45297.1; -; Genomic_DNA.
DR EMBL; AF238944; AAG45298.1; -; Genomic_DNA.
DR EMBL; AF238945; AAG45299.1; -; Genomic_DNA.
DR EMBL; AF238946; AAG45300.1; -; Genomic_DNA.
DR EMBL; AF238947; AAG45301.1; -; Genomic_DNA.
DR EMBL; AF238948; AAG45302.1; -; Genomic_DNA.
DR EMBL; AF238949; AAG45303.1; -; Genomic_DNA.
DR EMBL; AF238950; AAG45304.1; -; Genomic_DNA.
DR EMBL; AF238951; AAG45305.1; -; Genomic_DNA.
DR EMBL; AF238952; AAG45306.1; -; Genomic_DNA.
DR EMBL; AF238953; AAG45307.1; -; Genomic_DNA.
DR EMBL; AF238954; AAG45308.1; -; Genomic_DNA.
DR EMBL; AF238955; AAG45309.1; -; Genomic_DNA.
DR EMBL; AF238956; AAG45310.1; -; Genomic_DNA.
DR EMBL; AF238957; AAG45311.1; -; Genomic_DNA.
DR EMBL; U31122; AAC47353.1; -; Genomic_DNA.
DR RefSeq; XP_001955590.1; XM_001955554.2.
DR AlphaFoldDB; Q23835; -.
DR SMR; Q23835; -.
DR STRING; 7217.FBpp0122036; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblMetazoa; FBtr0123544; FBpp0122036; FBgn0261677.
DR GeneID; 6492910; -.
DR KEGG; dan:6492910; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; Q23835; -.
DR OMA; QNLNTTW; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; Q23835; -.
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 1"
FT /id="PRO_0000001360"
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 VARIANT 2
FT /note="F -> L (in strain: Taka5)"
FT /evidence="ECO:0000269|PubMed:11040291"
FT CONFLICT 121
FT /note="N -> D (in Ref. 1; AAC79123 and 4; AAC47353)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> A (in Ref. 1; AAC79123 and 4; AAC47353)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="K -> R (in Ref. 1; AAC79123)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="G -> D (in Ref. 1; AAC79123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 53575 MW; 9884FB907BE8E6B0 CRC64;
MFLAKSIVCL ALLAVANAQF NTNYASGRSG MVHLFEWKWD DIAAECENFL GPYGYAGVQV
SPVNENAVKD SRPWWERYQP ISYKLVTRSG NEEQFASMVR RCNNVGVRIY VDVVFNHMAA
NGGTYGTGGS 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
