AMYB_DROYA
ID AMYB_DROYA Reviewed; 494 AA.
AC Q9BN01; B4P8G7; P51548;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-amylase B;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=Amy-d; ORFNames=GE11648;
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].
RX PubMed=8536970; DOI=10.1093/genetics/141.1.223;
RA Shibata H., Yamazaki T.;
RT "Molecular evolution of the duplicated Amy locus in the Drosophila
RT melanogaster species subgroup: concerted evolution only in the coding
RT region and an excess of nonsynonymous substitutions in speciation.";
RL Genetics 141:223-236(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LBV1, LO4, SA2, and SA3;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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: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; D17737; BAA04590.1; -; Genomic_DNA.
DR EMBL; AF280886; AAG60011.1; -; Genomic_DNA.
DR EMBL; AF280887; AAG60012.1; -; Genomic_DNA.
DR EMBL; AF280888; AAG60013.1; -; Genomic_DNA.
DR EMBL; AF280889; AAG60014.1; -; Genomic_DNA.
DR EMBL; CM000158; EDW92184.1; -; Genomic_DNA.
DR PIR; S58946; S58946.
DR RefSeq; XP_002092472.1; XM_002092436.2.
DR AlphaFoldDB; Q9BN01; -.
DR SMR; Q9BN01; -.
DR STRING; 7245.FBpp0256658; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblMetazoa; FBtr0258166; FBpp0256658; FBgn0013165.
DR GeneID; 6531681; -.
DR KEGG; dya:Dyak_GE11648; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR OMA; HEPCSIN; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; Q9BN01; -.
DR Proteomes; UP000002282; Chromosome 2R.
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; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..494
FT /note="Alpha-amylase B"
FT /id="PRO_0000001367"
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 MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
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 179..180
FT /note="NS -> DP (in strain: LO4)"
FT VARIANT 195
FT /note="D -> N (in strain: LO4)"
FT VARIANT 330
FT /note="A -> V (in strain: LO4)"
FT VARIANT 381
FT /note="V -> A (in strain: LO4)"
FT VARIANT 405
FT /note="Q -> P (in strain: LO4)"
FT VARIANT 427
FT /note="F -> Y (in strain: LO4)"
SQ SEQUENCE 494 AA; 53688 MW; EBDC615F3C0044B8 CRC64;
MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGFAGVQV
SPVNENAVKD SRPWWERYQP ISYKLETRSG NEQQFASMVK RCNAVGVRTY VDVVFNHMAA
DGGTYGTGGS TASPSTKSFP GVPYSSLDFN PTCSINNYND ANQVRNCELV GLRDLNQGNS
YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKTLNTDHGF NSGSKAYIVQ
EVIDMGGEAI SKSEYTGLGA VTEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF SDTDQGPPTT
DGHNIASPVF NSDNSCSGGW VCEHRWRQIY NMVAFRNAVG SDAIQNWWDN GSNQIAFSRG
SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVSVGSD GRASIYLGSS
EDDGVLAIHV NAKL
