AMY_PHACE
ID AMY_PHACE Reviewed; 485 AA.
AC O97396; P81519;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
OS Phaedon cochleariae (Mustard beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX NCBI_TaxID=80249;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA76926.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA Girard C., Jouanin L.;
RT "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT phytophagous beetle, Phaedon cochleariae.";
RL Insect Biochem. Mol. Biol. 29:1129-1142(1999).
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|UniProtKB:P56634}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in larval and adult gut.
CC {ECO:0000269|PubMed:10612046}.
CC -!- DEVELOPMENTAL STAGE: Larvae and adult, but not eggs.
CC {ECO:0000269|PubMed:10612046}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000255}.
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DR EMBL; Y17902; CAA76926.1; -; mRNA.
DR AlphaFoldDB; O97396; -.
DR SMR; O97396; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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 GO; GO:0007586; P:digestion; 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 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Chloride; Digestion; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..485
FT /note="Alpha-amylase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000147323"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 201
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 303
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 339
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 305
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 152..166
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 439..451
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 485 AA; 52832 MW; 0038E265BCB9A825 CRC64;
MFLTSVLILC SLAALSLGQK NNNFAPGRNT IVHLFEWHWD DIANECENFL GPKGFAGVQI
SPPAENTVIG DRPWWERYQP ISYALNTRSG DESALASMIR RCNNAGVRIY VDAVFNHMSA
TSGIGTGGSS CDVEPSASPA VPYGSGDFHG RCTSNNYQDP NNIRNCWLSG LPDLDQSKDY
VRDKILEYLN HLVDLGVAGF RVDAAKHMWP ADLQVIYGRV KDLNTDHGFS QGSRPFFYQE
VIDLGGEGVS KNEYTGFGTV LEFKYGTELG NAFQGNNALH NLENWGPAWG LLEGTDAVVF
IDNHDNQRTG SGAILTYKNP RPYKMAIGFM LAHPYGTTRI MSSFSFDYND QGPPTQGPGF
NSVRNLHQWV GGANTGWRQI LRVMVGFRNA VDGTSISNWW SDGNQQIAFG RGDKGFVAFT
LAGDINGNLQ TSLPAGSYCD IVSGKLENGS CTGKTVNVDG NGQAYITLSS GEDDGFLAIH
VGAKV
