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AMYR_DROSU
ID   AMYR_DROSU              Reviewed;         494 AA.
AC   O18420;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
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 subobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7241;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Montgenevre;
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).
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; U79724; AAC48344.1; -; Genomic_DNA.
DR   AlphaFoldDB; O18420; -.
DR   SMR; O18420; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; O18420; -.
DR   FlyBase; FBgn0020466; Dsub\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_0000001389"
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;  55602 MW;  AFB4145BF8DE6DE9 CRC64;
     MFKFTFALAL CVLAAGSALA QHNPHWWGNR NTIVHLFEWQ WEDIAEECEN FLGPRGFAGV
     QVSPANENIV SPGRPWWERY QPISYKLITR SGDEEQFADM VRRCNDVGVR IYVDVLLNHM
     SADFYGQAVG TAGTEADPAT KSFPGVPYTA EDFHPSCQIY DWNDRFQIQQ CELVGLKDLD
     QSRDHVRTKL IEFLDHLIEL GVAGFRVDAA KHMASEDLEF IYGSLSDLKT EHGFPHNARP
     FIFQEVIDHG GQEVTREEYN SLGAVTEFRF WQEIGNAFRG NNAFKWLQSW GTDWGFFSSG
     QAFTFVDNHD NQRDGGAVLT YKIPRQYKMA TAFHLAYPYG ISRVMSSFAF DDHDSAPPQN
     AQEQLISPEF DSDGACVNGW ICEHRWRQIY NMVGFKNAVR DTPVTNWWDN GDSQIAFCRG
     SKGFIAINNN LYDLAETLQT CLPAGVYCDV ISGDLIHGSC SGKSVTVGND GRAFVSIGSN
     DFDGVLAIHV DAKL
 
 
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