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Protein

Alpha-amylase

Gene
N/A
Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed-Annotation score: 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.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi133Calcium 1Combined sources2 Publications1
Metal bindingi190Calcium 2Combined sources2 Publications1
Metal bindingi190SodiumCombined sources1 Publication1
Metal bindingi212Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi214Calcium 2Combined sources2 Publications1
Metal bindingi214SodiumCombined sources1 Publication1
Metal bindingi225Calcium 1Combined sources2 Publications1
Metal bindingi225SodiumCombined sources1 Publication1
Metal bindingi231Calcium 1Combined sources2 Publications1
Metal bindingi231SodiumCombined sources1 Publication1
Metal bindingi233Calcium 2Combined sources2 Publications1
Metal bindingi235Calcium 2Combined sources2 Publications1
Active sitei262Nucleophile1
Metal bindingi266Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Active sitei292Proton donor1
Metal bindingi331Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Sitei359Transition state stabilizerBy similarity1
Metal bindingi438Calcium 3Combined sources1 Publication1
Metal bindingi461Calcium 3Combined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 630.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1By similarity)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000000133032 – 514Alpha-amylaseAdd BLAST483

Proteomic databases

PRIDEiP00692.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Beta strandi46 – 48Combined sources3
Helixi50 – 64Combined sources15
Beta strandi68 – 71Combined sources4
Beta strandi75 – 79Combined sources5
Beta strandi84 – 89Combined sources6
Beta strandi101 – 103Combined sources3
Helixi109 – 121Combined sources13
Beta strandi125 – 130Combined sources6
Beta strandi133 – 135Combined sources3
Beta strandi139 – 150Combined sources12
Beta strandi153 – 157Combined sources5
Beta strandi162 – 170Combined sources9
Turni173 – 177Combined sources5
Helixi186 – 188Combined sources3
Beta strandi189 – 195Combined sources7
Turni196 – 199Combined sources4
Beta strandi200 – 206Combined sources7
Beta strandi208 – 210Combined sources3
Beta strandi215 – 217Combined sources3
Beta strandi228 – 232Combined sources5
Helixi237 – 254Combined sources18
Beta strandi258 – 261Combined sources4
Helixi264 – 266Combined sources3
Helixi269 – 283Combined sources15
Beta strandi288 – 291Combined sources4
Helixi298 – 307Combined sources10
Turni308 – 310Combined sources3
Beta strandi312 – 315Combined sources4
Helixi317 – 328Combined sources12
Turni329 – 331Combined sources3
Helixi335 – 337Combined sources3
Turni338 – 341Combined sources4
Helixi343 – 346Combined sources4
Helixi348 – 350Combined sources3
Beta strandi351 – 355Combined sources5
Turni358 – 360Combined sources3
Turni372 – 374Combined sources3
Helixi375 – 383Combined sources9
Beta strandi384 – 393Combined sources10
Helixi394 – 398Combined sources5
Helixi412 – 424Combined sources13
Beta strandi430 – 433Combined sources4
Beta strandi436 – 444Combined sources9
Beta strandi455 – 462Combined sources8
Beta strandi465 – 470Combined sources6
Helixi473 – 475Combined sources3
Beta strandi479 – 482Combined sources4
Beta strandi490 – 492Combined sources3
Beta strandi497 – 503Combined sources7
Beta strandi508 – 513Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti54L → I AA sequence (PubMed:6156671).Curated1
Sequence conflicti64I → L AA sequence (PubMed:6156671).Curated1
Sequence conflicti79S → D AA sequence (PubMed:6156671).Curated1
Sequence conflicti84G → S AA sequence (PubMed:6156671).Curated1

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.
PIRiA92389. ALBSN.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP00692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.1. 630.

Miscellaneous databases

EvolutionaryTraceiP00692.

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.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
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.
ProtoNetiSearch...

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 2, 2016
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.