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P00691

- AMY_BACSU

UniProt

P00691 - AMY_BACSU

Protein

Alpha-amylase

Gene

amyE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

    Cofactori

    Binds 2 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi142 – 1421Calcium 1
    Metal bindingi178 – 1781Calcium 1; via carbonyl oxygen
    Metal bindingi187 – 1871Calcium 1
    Metal bindingi210 – 2101Calcium 2; via carbonyl oxygen
    Metal bindingi212 – 2121Calcium 2
    Active sitei217 – 2171NucleophileBy similarity
    Metal bindingi221 – 2211Calcium 1; via carbonyl oxygen
    Active sitei249 – 2491Proton donorBy similarity
    Sitei310 – 3101Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU03040-MONOMER.

    Protein family/group databases

    CAZyiCBM26. Carbohydrate-Binding Module Family 26.
    GH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Gene namesi
    Name:amyE
    Synonyms:amyA
    Ordered Locus Names:BSU03040
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU03040. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Add
    BLAST
    Propeptidei28 – 4114PRO_0000001335Add
    BLAST
    Chaini42 – 659618Alpha-amylasePRO_0000001336Add
    BLAST

    Proteomic databases

    PaxDbiP00691.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi224308.BSU03040.

    Structurei

    Secondary structure

    1
    659
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni47 – 493
    Beta strandi52 – 543
    Helixi60 – 656
    Helixi67 – 726
    Beta strandi76 – 805
    Beta strandi84 – 863
    Helixi90 – 923
    Helixi96 – 1038
    Beta strandi105 – 1128
    Turni113 – 1153
    Helixi118 – 12912
    Turni130 – 1323
    Beta strandi134 – 1396
    Turni148 – 1503
    Helixi153 – 1564
    Beta strandi162 – 1643
    Helixi174 – 1796
    Beta strandi180 – 1823
    Helixi193 – 20816
    Beta strandi213 – 2164
    Helixi219 – 2213
    Helixi228 – 2303
    Helixi234 – 2385
    Beta strandi244 – 2485
    Helixi258 – 2625
    Beta strandi265 – 2684
    Helixi270 – 28213
    Helixi287 – 2904
    Beta strandi294 – 2974
    Helixi299 – 3013
    Beta strandi302 – 3043
    Helixi309 – 3135
    Turni318 – 3214
    Helixi324 – 33512
    Beta strandi337 – 3459
    Beta strandi359 – 3613
    Helixi369 – 3724
    Helixi374 – 38613
    Helixi396 – 3983
    Beta strandi402 – 4076
    Turni408 – 4103
    Beta strandi411 – 4166
    Beta strandi418 – 4203
    Beta strandi422 – 4276
    Beta strandi432 – 4365
    Beta strandi438 – 4414
    Beta strandi443 – 4475
    Beta strandi450 – 4556
    Beta strandi459 – 4635

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BAGX-ray2.50A42-466[»]
    1UA7X-ray2.21A45-466[»]
    ProteinModelPortaliP00691.
    SMRiP00691. Positions 42-466, 560-650.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00691.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000008732.
    KOiK01176.
    OrthoDBiEOG6F55CH.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00632. Aamy_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00691-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG    50
    TILHAWNWSF NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY 100
    WLYQPTSYQI GNRYLGTEQE FKEMCAAAEE YGIKVIVDAV INHTTSDYAA 150
    ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN SLLGLYDWNT QNTQVQSYLK 200
    RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN TSAEFQYGEI 250
    LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD 300
    KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG 350
    GGNGVRFPGK SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN 400
    QIFMNQRGSH GVVLANAGSS SVSINTATKL PDGRYDNKAG AGSFQVNDGK 450
    LTGTINARSV AVLYPDDIAK APHVFLENYK TGVTHSFNDQ LTITLRADAN 500
    TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG TNSDGVTRTE 550
    KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM 600
    TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND 650
    SGLSGSLPH 659
    Length:659
    Mass (Da):72,378
    Last modified:June 16, 2009 - v2
    Checksum:i16BD6CB1E7C67BD6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221H → Y in CAA26086. (PubMed:6099357)Curated
    Sequence conflicti22 – 221H → Y in AAA22234. (PubMed:6413492)Curated
    Sequence conflicti22 – 221H → Y in CAA23436. (PubMed:6189486)Curated
    Sequence conflicti22 – 221H → Y in AAA22230. 1 PublicationCurated
    Sequence conflicti146 – 1461S → F in CAA26086. (PubMed:6099357)Curated
    Sequence conflicti146 – 1461S → F in AAA22234. (PubMed:6413492)Curated
    Sequence conflicti204 – 2041D → E in CAA26086. (PubMed:6099357)Curated
    Sequence conflicti204 – 2041D → E in AAA22234. (PubMed:6413492)Curated
    Sequence conflicti284 – 2841N → K in CAA26086. (PubMed:6099357)Curated
    Sequence conflicti332 – 3321A → S in AAA22234. (PubMed:6413492)Curated
    Sequence conflicti513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in CAA23437. (PubMed:6186986)CuratedAdd
    BLAST
    Sequence conflicti513 – 52917ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in BAA08938. (PubMed:8969502)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti469 – 4779AKAPHVFLE → EMRCNTFFQ in strain: N7 AMYEN+.
    Natural varianti478 – 659182Missing in strain: N7 AMYEN+.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00101 Genomic DNA. Translation: CAA23437.1.
    V00100 Genomic DNA. Translation: CAA23436.1.
    D50453 Genomic DNA. Translation: BAA08938.1.
    AL009126 Genomic DNA. Translation: CAB12098.2.
    K00563 Genomic DNA. Translation: AAA22234.1.
    X02150 Genomic DNA. Translation: CAA26086.1.
    M35517 Genomic DNA. Translation: AAA22230.1.
    PIRiA00842. ALBS.
    A91793. ALBSNA.
    RefSeqiNP_388186.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12098; CAB12098; BSU03040.
    GeneIDi938356.
    KEGGibsu:BSU03040.
    PATRICi18972167. VBIBacSub10457_0312.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00101 Genomic DNA. Translation: CAA23437.1 .
    V00100 Genomic DNA. Translation: CAA23436.1 .
    D50453 Genomic DNA. Translation: BAA08938.1 .
    AL009126 Genomic DNA. Translation: CAB12098.2 .
    K00563 Genomic DNA. Translation: AAA22234.1 .
    X02150 Genomic DNA. Translation: CAA26086.1 .
    M35517 Genomic DNA. Translation: AAA22230.1 .
    PIRi A00842. ALBS.
    A91793. ALBSNA.
    RefSeqi NP_388186.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BAG X-ray 2.50 A 42-466 [» ]
    1UA7 X-ray 2.21 A 45-466 [» ]
    ProteinModelPortali P00691.
    SMRi P00691. Positions 42-466, 560-650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU03040.

    Protein family/group databases

    CAZyi CBM26. Carbohydrate-Binding Module Family 26.
    GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbi P00691.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12098 ; CAB12098 ; BSU03040 .
    GeneIDi 938356.
    KEGGi bsu:BSU03040.
    PATRICi 18972167. VBIBacSub10457_0312.

    Organism-specific databases

    GenoListi BSU03040. [Micado ]

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000008732.
    KOi K01176.
    OrthoDBi EOG6F55CH.

    Enzyme and pathway databases

    BioCyci BSUB:BSU03040-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00691.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00632. Aamy_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the amylase gene from Bacillus subtilis."
      Yang M., Galizzi A., Henner D.J.
      Nucleic Acids Res. 11:237-249(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Changes in the properties and molecular weights of Bacillus subtilis M-type and N-type alpha-amylases resulting from a spontaneous deletion."
      Yamane K., Hirata Y., Furusato T., Yamazaki H., Nakayama A.
      J. Biochem. 96:1849-1858(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: N7 AMYEN+.
    3. "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
      Yamane K., Kumano M., Kurita K.
      Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    5. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 513-529.
    6. "Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences."
      Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., Tamura G., Yamane K.
      J. Bacteriol. 156:327-337(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-557.
    7. "Nucleotide sequence of the promoter and NH2-terminal signal peptide region of Bacillus subtilis alpha-amylase gene cloned in pUB110."
      Ohmura K., Yamazaki H., Takeichi Y., Nakayama A., Otozai K., Yamane K., Yamasaki M., Tamura G.
      Biochem. Biophys. Res. Commun. 112:678-683(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
    8. "Molecular cloning and expression of an alpha-amylase gene from an alpha-amylase extrahyper producing Bacillus subtilis."
      Emori M., Tojo T., Maruo B.
      Agric. Biol. Chem. 52:399-406(1988)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
      Strain: 168 / 2633.
    9. "Membrane-bound and soluble extracellular alpha-amylase from Bacillus subtilis."
      Mantsala P., Zalkin H.
      J. Biol. Chem. 254:8540-8547(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-58.
    10. "Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose."
      Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T., Mizuno H.
      J. Mol. Biol. 277:393-407(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 42-466.

    Entry informationi

    Entry nameiAMY_BACSU
    AccessioniPrimary (citable) accession number: P00691
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3