ID AMYR_DROSE Reviewed; 493 AA.
AC O76261; B4HT73; B6C8H3; B6C8H4; B6C8H9; B6C8I0; B6C8I2; B6C8I4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Alpha-amylase-related protein;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amyrel; ORFNames=GM20043;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Da Lage J.-L.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-143; SER-152; LEU-293
RP AND SER-423.
RC STRAIN=Seychelles-1, Seychelles-10, Seychelles-11, Seychelles-12,
RC Seychelles-13, Seychelles-14, Seychelles-15, Seychelles-2, Seychelles-3,
RC Seychelles-4, Seychelles-5, Seychelles-6, Seychelles-7, Seychelles-8, and
RC Seychelles-9;
RA Legrand D., Tenaillon M., Lachaise D., Cariou M.-L.;
RT "Multilocus patterns of nucleotide diversity in Drosophila sechellia: the
RT evolutionary history of the least variable Drosophila species.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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).
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:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF039558; AAC39093.1; -; Genomic_DNA.
DR EMBL; EU018418; ABW69388.1; -; Genomic_DNA.
DR EMBL; EU018419; ABW69389.1; -; Genomic_DNA.
DR EMBL; EU018420; ABW69390.1; -; Genomic_DNA.
DR EMBL; EU018421; ABW69391.1; -; Genomic_DNA.
DR EMBL; EU018422; ABW69392.1; -; Genomic_DNA.
DR EMBL; EU018423; ABW69393.1; -; Genomic_DNA.
DR EMBL; EU018424; ABW69394.1; -; Genomic_DNA.
DR EMBL; EU018425; ABW69395.1; -; Genomic_DNA.
DR EMBL; EU018426; ABW69396.1; -; Genomic_DNA.
DR EMBL; EU018427; ABW69397.1; -; Genomic_DNA.
DR EMBL; EU018428; ABW69398.1; -; Genomic_DNA.
DR EMBL; EU018429; ABW69399.1; -; Genomic_DNA.
DR EMBL; EU018430; ABW69400.1; -; Genomic_DNA.
DR EMBL; EU018431; ABW69401.1; -; Genomic_DNA.
DR EMBL; EU018432; ABW69402.1; -; Genomic_DNA.
DR EMBL; CH480816; EDW48174.1; -; Genomic_DNA.
DR RefSeq; XP_002034161.1; XM_002034125.1.
DR AlphaFoldDB; O76261; -.
DR SMR; O76261; -.
DR STRING; 7238.O76261; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblMetazoa; FBtr0203028; FBpp0201520; FBgn0025060.
DR GeneID; 6609476; -.
DR KEGG; dse:6609476; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR OMA; SCEIYDW; -.
DR OrthoDB; 3249969at2759; -.
DR PhylomeDB; O76261; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EnsemblMetazoa.
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 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; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..493
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001386"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 205
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 307
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 342
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 47..103
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 156..170
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 375..381
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 417..440
FT /evidence="ECO:0000255"
FT DISULFID 447..459
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT VARIANT 143
FT /note="P -> T (in strain: Seychelles-1 and Seychelles-15)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 152
FT /note="F -> S (in strain: Seychelles-12)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 293
FT /note="W -> L (in strain: Seychelles-7 and Seychelles-8)"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 423
FT /note="F -> S (in strain: Seychelles-8 and Seychelles-10)"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 493 AA; 55461 MW; 5E02E633FFB270EB CRC64;
MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ
VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF
IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ
ALTFVDNHDN QRDAGAVLSY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA
QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQIAFCRGN
KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG FGYIHIGSDD
FDGVLALHVD AKV
//
