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P00692

- AMY_BACAM

UniProt

P00692 - AMY_BACAM

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Protein

Alpha-amylase

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 3 Ca(2+) ions per subunit.
  • Na(+)Note: 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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MIQKRKRTVS FRLVLMCTLL FVSLPITKTS AVNGTLMQYF EWYTPNDGQH
60 70 80 90 100
WKRLQNDAEH LSDIGITAVW IPPAYKGLSQ SDNGYGPYDL YDLGEFQQKG
110 120 130 140 150
TVRTKYGTKS ELQDAIGSLH SRNVQVYGDV VLNHKAGADA TEDVTAVEVN
160 170 180 190 200
PANRNQETSE EYQIKAWTDF RFPGRGNTYS DFKWHWYHFD GADWDESRKI
210 220 230 240 250
SRIFKFRGEG KAWDWEVSSE NGNYDYLMYA DVDYDHPDVV AETKKWGIWY
260 270 280 290 300
ANELSLDGFR IDAAKHIKFS FLRDWVQAVR QATGKEMFTV AEYWQNNAGK
310 320 330 340 350
LENYLNKTSF NQSVFDVPLH FNLQAASSQG GGYDMRRLLD GTVVSRHPEK
360 370 380 390 400
AVTFVENHDT QPGQSLESTV QTWFKPLAYA FILTRESGYP QVFYGDMYGT
410 420 430 440 450
KGTSPKEIPS LKDNIEPILK ARKEYAYGPQ HDYIDHPDVI GWTREGDSSA
460 470 480 490 500
AKSGLAALIT DGPGGSKRMY AGLKNAGETW YDITGNRSDT VKIGSDGWGE
510
FHVNDGSVSI YVQK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 114 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