AMY_BACSU
ID AMY_BACSU Reviewed; 659 AA.
AC P00691;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P06278};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=amyE; Synonyms=amyA; OrderedLocusNames=BSU03040;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=6186986; DOI=10.1093/nar/11.2.237;
RA Yang M., Galizzi A., Henner D.J.;
RT "Nucleotide sequence of the amylase gene from Bacillus subtilis.";
RL Nucleic Acids Res. 11:237-249(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N7 AMYEN+;
RX PubMed=6099357; DOI=10.1093/oxfordjournals.jbchem.a135019;
RA Yamane K., Hirata Y., Furusato T., Yamazaki H., Nakayama A.;
RT "Changes in the properties and molecular weights of Bacillus subtilis M-
RT type and N-type alpha-amylases resulting from a spontaneous deletion.";
RL J. Biochem. 96:1849-1858(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP SEQUENCE REVISION TO 513-529.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-557.
RX PubMed=6413492; DOI=10.1128/jb.156.1.327-337.1983;
RA Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M.,
RA Tamura G., Yamane K.;
RT "Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing
RT Bacillus subtilis strain: molecular cloning and nucleotide sequences.";
RL J. Bacteriol. 156:327-337(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RX PubMed=6189486; DOI=10.1016/0006-291x(83)91516-4;
RA Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K.,
RA Yamasaki M., Tamura G.;
RT "Nucleotide sequence of the promoter and NH2-terminal signal peptide region
RT of Bacillus subtilis alpha-amylase gene cloned in pUB110.";
RL Biochem. Biophys. Res. Commun. 112:678-683(1983).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RC STRAIN=168 / 2633;
RA Emori M., Tojo T., Maruo B.;
RT "Molecular cloning and expression of an alpha-amylase gene from an alpha-
RT amylase extrahyper producing Bacillus subtilis.";
RL Agric. Biol. Chem. 52:399-406(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-58.
RX PubMed=112102; DOI=10.1016/s0021-9258(19)86926-0;
RA Mantsala P., Zalkin H.;
RT "Membrane-bound and soluble extracellular alpha-amylase from Bacillus
RT subtilis.";
RL J. Biol. Chem. 254:8540-8547(1979).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 42-466 IN COMPLEX WITH CALCIUM
RP AND MALTOPENTAOSE, AND COFACTOR.
RX PubMed=9514750; DOI=10.1006/jmbi.1997.1599;
RA Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., Mizuno H.;
RT "Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus
RT subtilis complexed with maltopentaose.";
RL J. Mol. Biol. 277:393-407(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:P06278};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9514750};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:9514750};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; V00101; CAA23437.1; -; Genomic_DNA.
DR EMBL; V00100; CAA23436.1; -; Genomic_DNA.
DR EMBL; D50453; BAA08938.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12098.2; -; Genomic_DNA.
DR EMBL; K00563; AAA22234.1; -; Genomic_DNA.
DR EMBL; X02150; CAA26086.1; -; Genomic_DNA.
DR EMBL; M35517; AAA22230.1; -; Genomic_DNA.
DR PIR; A00842; ALBS.
DR PIR; A91793; ALBSNA.
DR RefSeq; NP_388186.2; NC_000964.3.
DR RefSeq; WP_003234692.1; NZ_JNCM01000030.1.
DR PDB; 1BAG; X-ray; 2.50 A; A=42-466.
DR PDB; 1UA7; X-ray; 2.21 A; A=45-466.
DR PDBsum; 1BAG; -.
DR PDBsum; 1UA7; -.
DR AlphaFoldDB; P00691; -.
DR SMR; P00691; -.
DR STRING; 224308.BSU03040; -.
DR BindingDB; P00691; -.
DR ChEMBL; CHEMBL3739249; -.
DR DrugBank; DB01841; 4,6-Dideoxyglucose.
DR DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; CBM26; Carbohydrate-Binding Module Family 26.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P00691; -.
DR EnsemblBacteria; CAB12098; CAB12098; BSU_03040.
DR GeneID; 938356; -.
DR KEGG; bsu:BSU03040; -.
DR PATRIC; fig|224308.179.peg.317; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; P00691; -.
DR OMA; FHNAMVG; -.
DR BioCyc; BSUB:BSU03040-MON; -.
DR SABIO-RK; P00691; -.
DR EvolutionaryTrace; P00691; -.
DR Proteomes; UP000001570; Chromosome.
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; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR031965; CBM26.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16738; CBM26; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT PROPEP 28..41
FT /id="PRO_0000001335"
FT CHAIN 42..659
FT /note="Alpha-amylase"
FT /id="PRO_0000001336"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:9514750"
FT ACT_SITE 249
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:9514750"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9514750"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9514750"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9514750"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9514750"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:9514750"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:9514750"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:9514750"
FT VARIANT 469..477
FT /note="AKAPHVFLE -> EMRCNTFFQ (in strain: N7 AMYEN+)"
FT VARIANT 478..659
FT /note="Missing (in strain: N7 AMYEN+)"
FT CONFLICT 22
FT /note="H -> Y (in Ref. 2; CAA26086, 6; AAA22234, 7;
FT CAA23436 and 8; AAA22230)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> F (in Ref. 2; CAA26086 and 6; AAA22234)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="D -> E (in Ref. 2; CAA26086 and 6; AAA22234)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="N -> K (in Ref. 2; CAA26086)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> S (in Ref. 6; AAA22234)"
FT /evidence="ECO:0000305"
FT CONFLICT 513..529
FT /note="ETAFKDGDQFTIGKGDP -> DDRRLRMEINSQSEKEIQ (in Ref. 1;
FT CAA23437 and 3; BAA08938)"
FT /evidence="ECO:0000305"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1UA7"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:1UA7"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1UA7"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 193..208
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1UA7"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1BAG"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1BAG"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 374..386
FT /evidence="ECO:0007829|PDB:1UA7"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:1UA7"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1BAG"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:1UA7"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:1UA7"
SQ SEQUENCE 659 AA; 72378 MW; 16BD6CB1E7C67BD6 CRC64;
MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG TILHAWNWSF
NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY WLYQPTSYQI GNRYLGTEQE
FKEMCAAAEE YGIKVIVDAV INHTTSDYAA ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN
SLLGLYDWNT QNTQVQSYLK RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN
TSAEFQYGEI LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD
KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK
SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN QIFMNQRGSH GVVLANAGSS
SVSINTATKL PDGRYDNKAG AGSFQVNDGK LTGTINARSV AVLYPDDIAK APHVFLENYK
TGVTHSFNDQ LTITLRADAN TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG
TNSDGVTRTE KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM
TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND SGLSGSLPH
