AMYB_DROME
ID AMYB_DROME Reviewed; 494 AA.
AC P81641; Q27578; Q27581; Q27585; Q27882; Q27885; Q27897; Q8WP56; Q95NK4;
AC Q969D1; Q9BH39; Q9BH72; Q9BPS5; Q9BPS6; Q9BPS7; Q9BPS8; Q9BPT0; Q9BPT1;
AC Q9BPT2; Q9BPT3; Q9V7Z0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 164.
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; Synonyms=AmyB; ORFNames=CG17876;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TN329;
RA Okuyama E., Yamazaki T.;
RT "Nucleotide sequences of the duplicated Amylase structural genes in
RT Drosophila melanogaster.";
RL Proc. Jpn. Acad., B, Phys. Biol. Sci. 64:274-277(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND POLYMORPHISM.
RC STRAIN=1420#1, AO168, J87, KO123, KO140, L16, TN22, TN256, and TN329;
RX PubMed=8536971; DOI=10.1093/genetics/141.1.237;
RA Inomata N., Shibata H., Okuyama E., Yamazaki T.;
RT "Evolutionary relationships and sequence variation of alpha-amylase
RT variants encoded by duplicated genes in the Amy locus of Drosophila
RT melanogaster.";
RL Genetics 141:237-244(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JP-1, JP-15, JP-169, JP-186, JP-190, JP-35, JP-5, JP-55, JP-60,
RC JP-65, JP-70, JP-75, JP-84, KN-10, KN-12, KN-15, KN-17, KN-21, KN-22,
RC KN-23, KN-27, KN-3, and KN-9;
RX PubMed=11156987; DOI=10.1093/genetics/157.2.667;
RA Araki H., Inomata N., Yamazaki T.;
RT "Molecular evolution of duplicated amylase gene regions in Drosophila
RT melanogaster: evidence of positive selection in the coding regions and
RT selective constraints in the cis-regulatory regions.";
RL Genetics 157:667-677(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC STRAIN=Oregon-R;
RX PubMed=3024105; DOI=10.1093/nar/14.21.8399;
RA Boer P.H., Hickey D.A.;
RT "The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence,
RT gene structure and expression motifs.";
RL Nucleic Acids Res. 14:8399-8411(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC STRAIN=Canton-S;
RX PubMed=1616481; DOI=10.1007/bf02396216;
RA Hawley S.A., Doane W.W., Norman R.A.;
RT "Molecular analysis of cis-regulatory sequences at the alpha-amylase locus
RT in Drosophila melanogaster.";
RL Biochem. Genet. 30:257-277(1992).
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 -!- POLYMORPHISM: At least 6 electrophoretic isozymes are known: Amy1,
CC Amy2, Amy3, Amy4, Amy5 and Amy6. Strains KO123 expresses Amy1; J87
CC expresses Amy3; 1420#1, L16 and TN256 express Amy6.
CC {ECO:0000269|PubMed:8536971}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X84405; CAA59126.1; -; Genomic_DNA.
DR EMBL; L22717; AAA92227.1; -; Genomic_DNA.
DR EMBL; L22718; AAA92228.1; -; Genomic_DNA.
DR EMBL; L22720; AAA92230.1; -; Genomic_DNA.
DR EMBL; L22724; AAA92232.1; -; Genomic_DNA.
DR EMBL; L22727; AAA92233.1; -; Genomic_DNA.
DR EMBL; L22728; AAA92242.1; -; Genomic_DNA.
DR EMBL; L22730; AAA92237.1; -; Genomic_DNA.
DR EMBL; L22732; AAA92243.1; -; Genomic_DNA.
DR EMBL; L22734; AAA92238.1; -; Genomic_DNA.
DR EMBL; AB043027; BAB32525.1; -; Genomic_DNA.
DR EMBL; AB043028; BAB32526.1; -; Genomic_DNA.
DR EMBL; AB043029; BAB32527.1; -; Genomic_DNA.
DR EMBL; AB043030; BAB32528.1; -; Genomic_DNA.
DR EMBL; AB043031; BAB32529.1; -; Genomic_DNA.
DR EMBL; AB043032; BAB32530.1; -; Genomic_DNA.
DR EMBL; AB043033; BAB32531.1; -; Genomic_DNA.
DR EMBL; AB043034; BAB32532.1; -; Genomic_DNA.
DR EMBL; AB043035; BAB32533.1; -; Genomic_DNA.
DR EMBL; AB043036; BAB32534.1; -; Genomic_DNA.
DR EMBL; AB043037; BAB32535.1; -; Genomic_DNA.
DR EMBL; AB043039; BAB32537.1; -; Genomic_DNA.
DR EMBL; AB043040; BAB32538.1; -; Genomic_DNA.
DR EMBL; AB043041; BAB32539.1; -; Genomic_DNA.
DR EMBL; AB043042; BAB32540.1; -; Genomic_DNA.
DR EMBL; AB043043; BAB32541.1; -; Genomic_DNA.
DR EMBL; AB043044; BAB32542.1; -; Genomic_DNA.
DR EMBL; AB043045; BAB32543.1; -; Genomic_DNA.
DR EMBL; AB043046; BAB32544.1; -; Genomic_DNA.
DR EMBL; AB043047; BAB32545.1; -; Genomic_DNA.
DR EMBL; AB043049; BAB72141.1; -; Genomic_DNA.
DR EMBL; AB043050; BAB72142.1; -; Genomic_DNA.
DR EMBL; AB043051; BAB72143.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57894.1; -; Genomic_DNA.
DR EMBL; X04570; CAA28239.1; -; Genomic_DNA.
DR EMBL; X84410; CAA59130.1; -; Genomic_DNA.
DR PIR; S58951; S58951.
DR PIR; S58954; S58954.
DR PIR; S58959; S58959.
DR PIR; S58960; S58960.
DR PIR; S58962; S58962.
DR PIR; S58964; S58964.
DR RefSeq; NP_523768.1; NM_079044.2.
DR AlphaFoldDB; P81641; -.
DR SMR; P81641; -.
DR BioGRID; 62629; 2.
DR STRING; 7227.FBpp0086155; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P81641; -.
DR DNASU; 36932; -.
DR GeneID; 36932; -.
DR KEGG; dme:Dmel_CG17876; -.
DR CTD; 36932; -.
DR FlyBase; FBgn0000078; Amy-d.
DR VEuPathDB; VectorBase:FBgn0000079; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; P81641; -.
DR Reactome; R-DME-189085; Digestion of dietary carbohydrate.
DR BioGRID-ORCS; 36932; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36932; -.
DR PRO; PR:P81641; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR ExpressionAtlas; P81641; baseline and differential.
DR Genevisible; P81641; DM.
DR GO; GO:0004556; F:alpha-amylase activity; TAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:UniProtKB.
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; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT CHAIN 19..494
FT /note="Alpha-amylase B"
FT /id="PRO_0000001365"
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 6
FT /note="Missing (in strain: KN-22)"
FT VARIANT 11
FT /note="A -> S (in strain: Berkeley, JP-5, JP-35, JP-55, JP-
FT 75, KN-12 and Oregon-R)"
FT VARIANT 71
FT /note="S -> R (in strain: 1420#1, JP-169, JP-186, JP-190,
FT KO123, KN-3, KN-9, KN-10, TN22 and TN256)"
FT VARIANT 121
FT /note="D -> E (in strain: JP-55)"
FT VARIANT 121
FT /note="D -> G (in strain: 1420#1, JP-190, JP-169, JP-186,
FT KO123, TN22 and TN256)"
FT VARIANT 121
FT /note="D -> N (in strain: KN-10, KN-3 and KN-9)"
FT VARIANT 138
FT /note="S -> T (in strain: JP-75, KN-17, KN-21, KN-22 and
FT L16)"
FT VARIANT 156
FT /note="S -> R (in strain: 1420#1, JP-169, JP-186, JP-190,
FT KO123, KN-3, KN-9, KN-10, TN22 and TN256)"
FT VARIANT 278
FT /note="D -> N (in strain: 1420#1, AO168, J87, JP-60, JP-
FT 169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and
FT TN256)"
FT VARIANT 288
FT /note="T -> I (in strain: KN-15)"
FT VARIANT 398
FT /note="T -> A (in strain: Berkeley, JP-5, JP-35, JP-55, JP-
FT 60, JP-65, JP-70, JP-75, JP-169, JP-186, JP-190, KN-3, KN-
FT 9, KN-10, KN-12, KN-17, KN-21 and KN-23)"
FT VARIANT 401
FT /note="S -> L (in strain: Berkeley, JP-5, JP-35, JP-55, JP-
FT 65, JP-70, KN-12 and KN-21)"
FT VARIANT 403
FT /note="E -> A (in strain: 1420#1, AO168, J87, JP-60, JP-
FT 169, JP-186, JP-190, KO123, KN-3, KN-9, KN-10, TN22 and
FT TN256)"
FT VARIANT 410
FT /note="N -> S (in strain: Berkeley, JP-5, JP-35, JP-55, JP-
FT 65 and KN-12)"
FT VARIANT 465
FT /note="V -> I (in strain: JP-1, JP-15, JP-84, KO140 and KN-
FT 27)"
FT VARIANT 476
FT /note="Y -> N (in strain: 1420#1, AO168, J87, JP-1, JP-15,
FT JP-55, JP-60, JP-75, JP-84, JP-169, JP-186, JP-190, KO123,
FT KO140, KN-3, KN-9, KN-10, KN-15, KN-17, KN-21, KN-22, KN-
FT 23, KN-27, L16, TN22 and TN256)"
FT VARIANT 478
FT /note="G -> A (in strain: KN-21)"
SQ SEQUENCE 494 AA; 53795 MW; B477CB031754C298 CRC64;
MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGYAGVQV
SPVNENAVKD SRPWWERYQP ISYKLETRSG NEEQFASMVK RCNAVGVRTY VDVVFNHMAA
DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAISNYND ANEVRNCELV GLRDLNQGNS
YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ
EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT
DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDEIQNWWDN GSNQISFSRG
SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRASIYIGSS
EDDGVLAIHV NAKL
