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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
 
 
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