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AMYR_DROAN
ID   AMYR_DROAN              Reviewed;         493 AA.
AC   O18344;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Alpha-amylase-related protein;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   AltName: Full=Amy c6;
DE   Flags: Precursor;
GN   Name=Amyrel; Synonyms=Amyc6;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tai 13-1610;
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 TO 134 AND 451.
RA   Da Lage J.-L., Alland C.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AF024691; AAC39090.3; -; Genomic_DNA.
DR   AlphaFoldDB; O18344; -.
DR   SMR; O18344; -.
DR   STRING; 7217.FBpp0116650; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   eggNOG; KOG2212; Eukaryota.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:EnsemblMetazoa.
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; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..493
FT                   /note="Alpha-amylase-related protein"
FT                   /id="PRO_0000001368"
FT   ACT_SITE        207
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        244
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         117
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         205
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         307
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   BINDING         342
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   SITE            309
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   MOD_RES         20
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..103
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        156..170
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        375..381
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
FT   DISULFID        417..440
FT                   /evidence="ECO:0000255"
FT   DISULFID        447..459
FT                   /evidence="ECO:0000250|UniProtKB:P56634"
SQ   SEQUENCE   493 AA;  55400 MW;  AADC543547BC3C79 CRC64;
     MFKFATAVIL CLAASSTLAQ HNPHWWGNRN TIVHLFEWKW SDIAAECENF LGPKGFAGVQ
     VSPVNENIIS AGRPWWERYQ PISYKLITRS GNEQEFADMV RRCNDVGVRI YVDVLLNHMS
     GDFDGIAVGT AGSEAEPSKK SYPGVPYSAQ DFHPSCEITD WNDRFQVQQC ELVGLKDLDQ
     SSEWVRSKLI EFLDHLIELG VAGFRVDAAK HMAADDLSYI YSTISDLNTE HGFPHNARPF
     IFQEVIDHGH ETVSREEYNQ LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLASGQ
     ALTFVDNHDN QRDMGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTAPPQDE
     QERIISPEFD EEGACVNGWI CEHRWRQIYA MVGFKNAVRD TELSNWWDNG DSQISFCRGN
     KGFLAVNNNL YDLSQELQTC LPAGVYCDVI CGSLVDGSCT GKSVIVDDSG FGYIHIGSED
     FDGVLALHVD ARV
 
 
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