(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 163.
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;
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;
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}.
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   SMR; P00691; -.
DR   STRING; 224308.BSU03040; -.
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; BSU03040.
DR   GeneID; 938356; -.
DR   KEGG; bsu:BSU03040; -.
DR   PATRIC; fig|224308.179.peg.317; -.
DR   HOGENOM; HOG000008732; -.
DR   InParanoid; P00691; -.
DR   KO; K01176; -.
DR   OMA; FHNAMVG; -.
DR   BioCyc; BSUB:BSU03040-MONOMER; -.
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:0103025; F:alpha-amylase activity (releasing maltohexaose); 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;
DR   PRODOM; P00691.
DR   SWISS-2DPAGE; P00691.
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   METAL           142
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000269|PubMed:9514750"
FT   METAL           178
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:9514750"
FT   METAL           187
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000269|PubMed:9514750"
FT   METAL           210
FT                   /note="Calcium 2; via carbonyl oxygen"
FT                   /evidence="ECO:0000269|PubMed:9514750"
FT   METAL           212
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000269|PubMed:9514750"
FT   METAL           221
FT                   /note="Calcium 1; via carbonyl oxygen"
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:0000244|PDB:1UA7"
FT   STRAND          52..54
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           60..65
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           67..72
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          76..80
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          84..86
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           90..92
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           96..103
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          105..112
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   TURN            113..115
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           118..129
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   TURN            130..132
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          134..139
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   TURN            148..150
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           153..156
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           174..179
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          180..182
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           193..208
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          213..216
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           219..221
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           228..230
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           234..238
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          244..248
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           258..262
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          265..268
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           270..282
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           287..290
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          294..297
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           299..301
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          302..304
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           309..313
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   TURN            318..321
FT                   /evidence="ECO:0000244|PDB:1BAG"
FT   HELIX           324..335
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          337..345
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          359..361
FT                   /evidence="ECO:0000244|PDB:1BAG"
FT   HELIX           369..372
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           374..386
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   HELIX           396..398
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          402..407
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   TURN            408..410
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          411..416
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          418..420
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          422..427
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          432..436
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          438..441
FT                   /evidence="ECO:0000244|PDB:1BAG"
FT   STRAND          443..447
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          450..455
FT                   /evidence="ECO:0000244|PDB:1UA7"
FT   STRAND          459..463
FT                   /evidence="ECO:0000244|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
//

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