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AMYR_DROBP
ID   AMYR_DROBP              Reviewed;         494 AA.
AC   Q9NJN8;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alpha-amylase-related protein;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   Flags: Precursor;
GN   Name=Amyrel;
OS   Drosophila bipectinata (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=42026;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Da Lage J.-L., Renard E., Chartois F., Cariou M.-L.;
RT   "Origin and evolution of the Amyrel gene in Drosophila.";
RL   Submitted (MAR-1999) 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; AF136936; AAF25718.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9NJN8; -.
DR   SMR; Q9NJN8; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   FlyBase; FBgn0029467; Dbip\Amyrel.
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; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..494
FT                   /note="Alpha-amylase-related protein"
FT                   /id="PRO_0000001373"
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|UniProtKB:P56634"
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;  55339 MW;  60EEEF2C9F685491 CRC64;
     MFKFATAVIL CLVAASSTLA QHNPHWWGNR NTIVHLFEWK WSDIAAECEN FLGPRGFAGV
     QVSPVNENIV SAGRPWWERY QPISYKLTTR SGNEKEFADM VRRCNEVGVR IYVDVLLNHM
     SGDFDGIAVG TAGSEAEPSK KSYPGVPYSA LDFHPSCEIT DWNDRFQVQQ CELVGLKDLD
     QSSEWVRSKL IEFLDHLIEL GVAGFRVDAA KHMAADDLSF IYSSLSDLNI EHGFPHNARP
     FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEGIGNAFRG NNALKWLQSW GTGWGFLPSG
     QALTFVDNHD NQRDMGAVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTAPPQD
     EQEKIISPEF DEEGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSNWWDN GDSQISFCRG
     NKGFLAVNNN LYDLSQELQT CLPAGVYCDV ISGSLVDGSC TGKSVTVDDN GYGYAHIGSD
     DFDGVLALHV DAKV
 
 
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