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AMYB_DROYA
ID   AMYB_DROYA              Reviewed;         494 AA.
AC   Q9BN01; B4P8G7; P51548;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Alpha-amylase B;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=Amy-d; ORFNames=GE11648;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8536970; DOI=10.1093/genetics/141.1.223;
RA   Shibata H., Yamazaki T.;
RT   "Molecular evolution of the duplicated Amy locus in the Drosophila
RT   melanogaster species subgroup: concerted evolution only in the coding
RT   region and an excess of nonsynonymous substitutions in speciation.";
RL   Genetics 141:223-236(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LBV1, LO4, SA2, and SA3;
RX   PubMed=11298976; DOI=10.1046/j.1365-294x.2001.01225.x;
RA   Cariou M.-L., Silvain J.-F., Daubin V., Da Lage J.-L., Lachaise D.;
RT   "Divergence between Drosophila santomea and allopatric or sympatric
RT   populations of D. yakuba using paralogous amylase genes and migration
RT   scenarios along the Cameroon volcanic line.";
RL   Mol. Ecol. 10:649-660(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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:P04746};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P04746};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; D17737; BAA04590.1; -; Genomic_DNA.
DR   EMBL; AF280886; AAG60011.1; -; Genomic_DNA.
DR   EMBL; AF280887; AAG60012.1; -; Genomic_DNA.
DR   EMBL; AF280888; AAG60013.1; -; Genomic_DNA.
DR   EMBL; AF280889; AAG60014.1; -; Genomic_DNA.
DR   EMBL; CM000158; EDW92184.1; -; Genomic_DNA.
DR   PIR; S58946; S58946.
DR   RefSeq; XP_002092472.1; XM_002092436.2.
DR   AlphaFoldDB; Q9BN01; -.
DR   SMR; Q9BN01; -.
DR   STRING; 7245.FBpp0256658; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblMetazoa; FBtr0258166; FBpp0256658; FBgn0013165.
DR   GeneID; 6531681; -.
DR   KEGG; dya:Dyak_GE11648; -.
DR   eggNOG; KOG2212; Eukaryota.
DR   HOGENOM; CLU_013336_2_1_1; -.
DR   OMA; HEPCSIN; -.
DR   OrthoDB; 665362at2759; -.
DR   PhylomeDB; Q9BN01; -.
DR   Proteomes; UP000002282; Chromosome 2R.
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; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..494
FT                   /note="Alpha-amylase B"
FT                   /id="PRO_0000001367"
FT   ACT_SITE        204
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         165
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         174
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         202
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         304
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         343
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   SITE            306
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..102
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        153..167
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        376..382
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        448..460
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   VARIANT         179..180
FT                   /note="NS -> DP (in strain: LO4)"
FT   VARIANT         195
FT                   /note="D -> N (in strain: LO4)"
FT   VARIANT         330
FT                   /note="A -> V (in strain: LO4)"
FT   VARIANT         381
FT                   /note="V -> A (in strain: LO4)"
FT   VARIANT         405
FT                   /note="Q -> P (in strain: LO4)"
FT   VARIANT         427
FT                   /note="F -> Y (in strain: LO4)"
SQ   SEQUENCE   494 AA;  53688 MW;  EBDC615F3C0044B8 CRC64;
     MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGFAGVQV
     SPVNENAVKD SRPWWERYQP ISYKLETRSG NEQQFASMVK RCNAVGVRTY VDVVFNHMAA
     DGGTYGTGGS TASPSTKSFP GVPYSSLDFN PTCSINNYND ANQVRNCELV GLRDLNQGNS
     YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKTLNTDHGF NSGSKAYIVQ
     EVIDMGGEAI SKSEYTGLGA VTEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV
     FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF SDTDQGPPTT
     DGHNIASPVF NSDNSCSGGW VCEHRWRQIY NMVAFRNAVG SDAIQNWWDN GSNQIAFSRG
     SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVSVGSD GRASIYLGSS
     EDDGVLAIHV NAKL
 
 
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