Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00692

- AMY_BACAM

UniProt

P00692 - AMY_BACAM

Protein

Alpha-amylase

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 3 calcium ions per subunit.
    Binds 1 sodium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi133 – 1331Calcium 1
    Metal bindingi190 – 1901Calcium 2
    Metal bindingi190 – 1901Sodium
    Metal bindingi212 – 2121Calcium 2; via carbonyl oxygen
    Metal bindingi214 – 2141Calcium 2
    Metal bindingi214 – 2141Sodium
    Metal bindingi225 – 2251Calcium 1
    Metal bindingi225 – 2251Sodium
    Metal bindingi231 – 2311Calcium 1
    Metal bindingi231 – 2311Sodium
    Metal bindingi233 – 2331Calcium 2
    Metal bindingi235 – 2351Calcium 2
    Active sitei262 – 2621Nucleophile
    Metal bindingi266 – 2661Calcium 1; via carbonyl oxygen
    Active sitei292 – 2921Proton donor
    Metal bindingi331 – 3311Calcium 3; via carbonyl oxygen
    Sitei359 – 3591Transition state stabilizerBy similarity
    Metal bindingi438 – 4381Calcium 3By similarity
    Metal bindingi461 – 4611Calcium 3By similarity

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. calcium ion binding Source: InterPro

    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

    Protein family/group databases

    CAZyiGH13. 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
    OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
    Taxonomic identifieri1390 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    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 – 31311 PublicationAdd
    BLAST
    Chaini32 – 514483Alpha-amylasePRO_0000001330Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 383
    Beta strandi46 – 483
    Helixi50 – 6415
    Beta strandi68 – 714
    Beta strandi75 – 795
    Beta strandi84 – 896
    Beta strandi101 – 1033
    Helixi109 – 12113
    Beta strandi125 – 1306
    Beta strandi133 – 1353
    Beta strandi139 – 15012
    Beta strandi153 – 1575
    Beta strandi162 – 1709
    Turni173 – 1775
    Helixi186 – 1883
    Beta strandi189 – 1957
    Turni196 – 1994
    Beta strandi200 – 2067
    Beta strandi208 – 2103
    Beta strandi215 – 2173
    Beta strandi228 – 2325
    Helixi237 – 25418
    Beta strandi258 – 2614
    Helixi264 – 2663
    Helixi269 – 28315
    Beta strandi288 – 2914
    Helixi298 – 30710
    Turni308 – 3103
    Beta strandi312 – 3154
    Helixi317 – 32812
    Turni329 – 3313
    Helixi335 – 3373
    Turni338 – 3414
    Helixi343 – 3464
    Helixi348 – 3503
    Beta strandi351 – 3555
    Turni358 – 3603
    Turni372 – 3743
    Helixi375 – 3839
    Beta strandi384 – 39310
    Helixi394 – 3985
    Helixi412 – 42413
    Beta strandi430 – 4334
    Beta strandi436 – 4449
    Beta strandi455 – 4628
    Beta strandi465 – 4706
    Helixi473 – 4753
    Beta strandi479 – 4824
    Beta strandi490 – 4923
    Beta strandi497 – 5037
    Beta strandi508 – 5136

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E3XX-ray1.90A32-331[»]
    1E3ZX-ray1.93A32-331[»]
    1E40X-ray2.20A32-331[»]
    1E43X-ray1.70A32-331[»]
    3BH4X-ray1.40A/B32-514[»]
    ProteinModelPortaliP00692.
    SMRiP00692. Positions 32-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00692.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR013776. A-amylase_thermo.
    IPR015237. Alpha-amylase_C_pro.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF09154. DUF1939. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P00692-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQKRKRTVS FRLVLMCTLL FVSLPITKTS AVNGTLMQYF EWYTPNDGQH    50
    WKRLQNDAEH LSDIGITAVW IPPAYKGLSQ SDNGYGPYDL YDLGEFQQKG 100
    TVRTKYGTKS ELQDAIGSLH SRNVQVYGDV VLNHKAGADA TEDVTAVEVN 150
    PANRNQETSE EYQIKAWTDF RFPGRGNTYS DFKWHWYHFD GADWDESRKI 200
    SRIFKFRGEG KAWDWEVSSE NGNYDYLMYA DVDYDHPDVV AETKKWGIWY 250
    ANELSLDGFR IDAAKHIKFS FLRDWVQAVR QATGKEMFTV AEYWQNNAGK 300
    LENYLNKTSF NQSVFDVPLH FNLQAASSQG GGYDMRRLLD GTVVSRHPEK 350
    AVTFVENHDT QPGQSLESTV QTWFKPLAYA FILTRESGYP QVFYGDMYGT 400
    KGTSPKEIPS LKDNIEPILK ARKEYAYGPQ HDYIDHPDVI GWTREGDSSA 450
    AKSGLAALIT DGPGGSKRMY AGLKNAGETW YDITGNRSDT VKIGSDGWGE 500
    FHVNDGSVSI YVQK 514
    Length:514
    Mass (Da):58,403
    Last modified:January 1, 1988 - v1
    Checksum:i3DE66B3FB5CCDE7E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541L → I AA sequence (PubMed:6156671)Curated
    Sequence conflicti64 – 641I → L AA sequence (PubMed:6156671)Curated
    Sequence conflicti79 – 791S → D AA sequence (PubMed:6156671)Curated
    Sequence conflicti84 – 841G → S AA sequence (PubMed:6156671)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01542 mRNA. Translation: AAA22191.1.
    V00092 Genomic DNA. Translation: CAA23430.1.
    M18424 Genomic DNA. Translation: AAA22192.1.
    PIRiA92389. ALBSN.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01542 mRNA. Translation: AAA22191.1 .
    V00092 Genomic DNA. Translation: CAA23430.1 .
    M18424 Genomic DNA. Translation: AAA22192.1 .
    PIRi A92389. ALBSN.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E3X X-ray 1.90 A 32-331 [» ]
    1E3Z X-ray 1.93 A 32-331 [» ]
    1E40 X-ray 2.20 A 32-331 [» ]
    1E43 X-ray 1.70 A 32-331 [» ]
    3BH4 X-ray 1.40 A/B 32-514 [» ]
    ProteinModelPortali P00692.
    SMRi P00692. Positions 32-514.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00692.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR013776. A-amylase_thermo.
    IPR015237. Alpha-amylase_C_pro.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF09154. DUF1939. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001021. Alph-amls_thrmst. 1 hit.
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene."
      Takkinen K., Pettersson R.F., Kalkkinen N., Palva I., Soederlund H., Kaeaeriaeinen L.
      J. Biol. Chem. 258:1007-1013(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IH.
    2. "Nucleotide sequence of the promoter and NH2-terminal signal peptide region of the alpha-amylase gene from Bacillus amyloliquefaciens."
      Palva I., Pettersson R.F., Kalkkinen N., Lehtovaara P., Sarvas M., Soederlund H., Takkinen K., Kaeaeriaeinen L.
      Gene 15:43-51(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
    3. "Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by its own signal peptide from Saccharomyces cerevisiae host cells."
      Ruohonen L., Hackman P., Lehtovaara P., Knowles J.K.C., Karaenen S.
      Gene 59:161-170(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
    4. "Sequence of the N-terminal half of Bacillus amyloliquefaciens alpha-amylase."
      Chung H.S., Friedberg F.
      Biochem. J. 185:387-395(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-222.
    5. "Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes."
      Brzozowski A.M., Lawson D.M., Turkenburg J.P., Bisgaard-Frantzen H., Svendsen A., Borchert T.V., Dauter Z., Wilson K.S., Davies G.J.
      Biochemistry 39:9099-9107(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-331.

    Entry informationi

    Entry nameiAMY_BACAM
    AccessioniPrimary (citable) accession number: P00692
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3