AMYR_DROPS
ID AMYR_DROPS Reviewed; 494 AA.
AC O18552; Q28WP1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alpha-amylase-related protein;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE Flags: Precursor;
GN Name=Amyrel; ORFNames=GA20907;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Phoenix;
RX PubMed=9618501; DOI=10.1073/pnas.95.12.6848;
RA Da Lage J.-L., Renard E., Chartois F., Lemeunier F., Cariou M.-L.;
RT "Amyrel, a paralogous gene of the amylase gene family in Drosophila
RT melanogaster and the Sophophora subgenus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6848-6853(1998).
RN [2]
RP SEQUENCE REVISION.
RA Da Lage J.-L.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL26626.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U82556; AAC48346.3; -; Genomic_DNA.
DR EMBL; CM000071; EAL26626.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001362046.2; XM_001362009.3.
DR AlphaFoldDB; O18552; -.
DR SMR; O18552; -.
DR STRING; 7237.FBpp0278794; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 4805687; -.
DR KEGG; dpo:Dpse_GA20907; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; O18552; -.
DR OMA; QSWGTDW; -.
DR PhylomeDB; O18552; -.
DR Proteomes; UP000001819; Chromosome 3.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..494
FT /note="Alpha-amylase-related protein"
FT /id="PRO_0000001385"
FT ACT_SITE 208
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 206
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 308
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 343
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 48..104
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 157..171
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 376..382
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 418..441
FT /evidence="ECO:0000255"
FT DISULFID 448..460
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 494 AA; 55590 MW; 95C0443078F4FC3B CRC64;
MFKFTFALAL CVLAAGLVLA QHNPHWWGNR NTIVHLFEWK WEDIAEECEN FLGPRGFAGV
QVSPANENIV SPGRPWWERY QPISYKLITR SGNEEQFADM VRRCNEVGVR IYVDVLLNHM
SADFVGQAVG TAGTEADPAV KSFPGVPYSA EDFHPSCEIY DWNDRYQIQH CELVGLKDLD
QSRDWVRTKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEF IYGSLSDLKI EHGFPHSSRP
FIFQEVIDHG GQEVTREEYN SLGAVTEFRF SQEIGNAFRG NNALKWLQSW GTDWGFLSSG
QALTFVDNHD NQRDGGAVLT YKSPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDSAPPQD
AQEELISPEF DADGGCANGW ICEHRWRQIY NMVGFKNAVR DTEISNWWDN GDSQIAFCRG
SKGFIAFNNN MYNLAEVLQT CLPKGVYCDV ISGDLINGSC SGKSVYVGDD GLGFVSIDSD
DFDGVLAIHV DARI
