AMY1_SACFI
ID AMY1_SACFI Reviewed; 494 AA.
AC P21567;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1;
DE Flags: Precursor;
GN Name=ALP1;
OS Saccharomycopsis fibuligera (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycopsidaceae; Saccharomycopsis.
OX NCBI_TaxID=4944;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3497057; DOI=10.1016/0014-5793(87)80248-x;
RA Itoh T., Yamashita I., Fukui S.;
RT "Nucleotide sequence of the alpha-amylase gene (ALP1) in the yeast
RT Saccharomycopsis fibuligera.";
RL FEBS Lett. 219:339-342(1987).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X05791; CAA29233.1; -; Genomic_DNA.
DR PIR; S00064; ALBYAF.
DR AlphaFoldDB; P21567; -.
DR SMR; P21567; -.
DR ChEMBL; CHEMBL5596; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..494
FT /note="Alpha-amylase"
FT /id="PRO_0000001351"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 324
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 57..65
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 177..191
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 267..310
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 462..493
FT /evidence="ECO:0000250|UniProtKB:P56271"
SQ SEQUENCE 494 AA; 54387 MW; 7F7D8FFD6BF58B67 CRC64;
MQISKAALLA SLAALVYAQP VTLFKRETNA DKWRSQSIYQ IVTDRFARTD GDTSASCNTE
DRLYCGGSFQ GIIKKLDYIK DMGFTAIWIS PVVENIPDNT AYGYAYHGYW MKNIYKINEN
FGTADDLKSL AQELHDRDML LMVDIVTNHY GSDGSGDSID YSEYTPFNDQ KYFHNYCLIS
NYDDQAQVQS CWEGDSSVAL PDLRTEDSDV ASVFNSWVKD FVGNYSIDGL RIDSAKHVDQ
GFFPDFVSAS GVYSVGEVFQ GDPAYTCPYQ NYIPGVSNYP LYYPTTRFFK TTDSSSSELT
QMISSVASSC SDPTLLTNFV ENHDNERFAS MTSDQSLISN AIAFVLLGDG IPVIYYGQEQ
GLSGKSDPNN REALWLSGYN KESDYYKLIA KANAARNAAV YQDSSYATSQ LSVIFSNDHV
IATKRGSVVS VFNNLGSSGS SDVTISNTGY SSGEDLVEVL TCSTVSGSSD LQVSIQGGQP
QIFVPAKYAS DICS
