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 24-JAN-2024, entry version 114. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; HPWWEVY; -. DR OrthoDB; 3249969at2759; -. 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 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; 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 //