AMYR_DROYA
ID AMYR_DROYA Reviewed; 493 AA.
AC O76264; Q9BH40; Q9BN03; Q9BN04; Q9BN05;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alpha-amylase-related protein;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amyrel;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Da Lage J.-L.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LBV2, LO4, SA3, and SA4;
RX PubMed=11298976; DOI=10.1046/j.1365-294x.2001.01225.x;
RA Cariou M.-L., Silvain J.-F., Daubin V., Da Lage J.-L., Lachaise D.;
RT "Divergence between Drosophila santomea and allopatric or sympatric
RT populations of D. yakuba using paralogous amylase genes and migration
RT scenarios along the Cameroon volcanic line.";
RL Mol. Ecol. 10:649-660(2001).
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; AF039561; AAC39096.2; -; Genomic_DNA.
DR EMBL; AF280874; AAG60601.1; -; Genomic_DNA.
DR EMBL; AF280875; AAG60602.1; -; Genomic_DNA.
DR EMBL; AF280876; AAG60603.1; -; Genomic_DNA.
DR EMBL; AF280877; AAG60604.1; -; Genomic_DNA.
DR EMBL; AF280878; AAG60605.1; -; Genomic_DNA.
DR AlphaFoldDB; O76264; -.
DR SMR; O76264; -.
DR STRING; 7245.FBpp0259058; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR eggNOG; KOG2212; Eukaryota.
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 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; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..493
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001394"
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 57
FT /note="A -> G (in strain: LBV2)"
FT VARIANT 70
FT /note="S -> A (in strain: LBV2, SA3 and SA4)"
FT VARIANT 148
FT /note="S -> T (in strain: LO4, LBV2, SA3 and SA4)"
FT VARIANT 189
FT /note="P -> L (in strain: LO4, LBV2, SA3 and SA4)"
FT VARIANT 198
FT /note="E -> D (in strain: LBV2, SA3 and SA4)"
FT VARIANT 360
FT /note="A -> E (in strain: LO4, LBV2, SA3 and SA4)"
FT VARIANT 365
FT /note="I -> V (in strain: LBV2, SA3 and SA4)"
FT VARIANT 401
FT /note="T -> A (in strain: SA3)"
FT VARIANT 401
FT /note="T -> M (in strain: LO4)"
SQ SEQUENCE 493 AA; 55420 MW; D95D63C49C3E1028 CRC64;
MFKLALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECENF LGPRGFAGVQ
VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS
GDFDGVAVGT AGTEAEPGKK SFPGVPYSAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ
SSDWVRSKPI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNARPF
IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ
ALTFVDNHDN QRDAGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA
QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN
KGFLAINNNL YDLSQDLNTC LPQGTYCDVI SGSLIDGSCT GKSVTVNEHG YGYIHIGSDD
FDGVLALHVD AKV
