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AMYB_ASPAW
ID   AMYB_ASPAW              Reviewed;         499 AA.
AC   Q02906;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Alpha-amylase B;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase B;
DE   Flags: Precursor;
GN   Name=amyB;
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UVK143F;
RX   PubMed=2340591; DOI=10.1007/bf00312611;
RA   Korman D.R., Bayliss F.T., Barnett C.C., Carmona C.L., Kodama K.H.,
RA   Royer T.J., Thompson S.A., Ward M., Wilson L.J., Berka R.M.;
RT   "Cloning, characterization, and expression of two alpha-amylase genes from
RT   Aspergillus niger var. awamori.";
RL   Curr. Genet. 17:203-212(1990).
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;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P0C1B3};
CC       Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC       concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X52756; CAA36967.1; -; Genomic_DNA.
DR   PIR; B48305; B48305.
DR   AlphaFoldDB; Q02906; -.
DR   SMR; Q02906; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR015340; A_amylase_C_dom.
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; PF09260; DUF1966; 1.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW   Glycosidase; Hydrolase; Metal-binding; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..499
FT                   /note="Alpha-amylase B"
FT                   /id="PRO_0000001348"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   ACT_SITE        251
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         227
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         251
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   SITE            318
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   DISULFID        261..304
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
FT   DISULFID        461..496
FT                   /evidence="ECO:0000250|UniProtKB:P56271"
SQ   SEQUENCE   499 AA;  54921 MW;  740B96B11BC01A8A CRC64;
     MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG
     GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD
     LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT
     QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY
     NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV
     KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN
     DPANREATWL SGYPTDSELY KLIASRNAIR NYAISKDTGF VTYKNWPIYK DDTTIPMRKG
     TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL
     PRVLYPTEKL AGSKICSSS
 
 
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