ID AMY_STRLM Reviewed; 566 AA.
AC P09794;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 28-JUN-2023, entry version 113.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=aml;
OS Streptomyces limosus (Streptomyces albidoflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=1947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3500166; DOI=10.1128/jb.169.12.5745-5754.1987;
RA Long C.M., Virolle M.-J., Chang S.-Y., Chang S., Bibb M.J.;
RT "Alpha-amylase gene of Streptomyces limosus: nucleotide sequence,
RT expression motifs, and amino acid sequence homology to mammalian and
RT invertebrate alpha-amylases.";
RL J. Bacteriol. 169:5745-5754(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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18244; AAA88554.1; -; Genomic_DNA.
DR AlphaFoldDB; P09794; -.
DR SMR; P09794; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd05808; CBM20_alpha_amylase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW Signal.
FT SIGNAL 1..28
FT CHAIN 29..566
FT /note="Alpha-amylase"
FT /id="PRO_0000001342"
FT DOMAIN 465..566
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 296
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 566 AA; 59670 MW; FB2AE73C147DC26C CRC64;
MARRLATASL AVLAAAATAL TAPTPAAAAP PGAKDVTAVL FEWKFASVAR ACTDSLGPAG
YGYVQVSPPQ EHIQGSQWWT SYQPVSYKIA GRLGDRAAFK SMVDTCHAAG VKVVADSVIN
HMAAGSGTGT GGSAYQKYDY PGIWSGADMD DCRSEINDYG NRANVQNCEL VGLADLDTGE
SYVRDRIAAY LNDLLSLGVD GFRIDAAKHM PAADLTAIKA KVGNGSTYWK QEAIHGAGEA
VQPSEYLGTG DVQEFRYARD LKRVFQNENL AHLKNFGEDW GYMASGKSAV FVDNHDTERG
GDTLNYKNGS AYTLAGVFML AWPYGSPDVH SGYEFTDHDA GPPNGGTVNA CYSDGWKCQH
AWPELSSMVG LRNTASGQPV TNWWDNGGDQ IAFGRGDKAY VAINHEGSAL NRTFQSGLPG
GAYCDVQSGR SVTVGSDGTF TATVAAGTAL ALHTGARTCS GGGTGPGTGQ TSASFHVNAT
TAWGENIYVT GDQAALGNWD PARALKLDPA AYPVWKLDVP LAAGTPFQYK YLRKDAAGKA
VWESGANRTA TVGTTGALTL NDTWRG
//
