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Protein

Alpha-amylase

Gene

amyE

Organism
Bacillus subtilis (strain 168)
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

Ca2+1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi142Calcium 11 Publication1
Metal bindingi178Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi187Calcium 11 Publication1
Metal bindingi210Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi212Calcium 21 Publication1
Active sitei217Nucleophile1 Publication1
Metal bindingi221Calcium 1; via carbonyl oxygen1 Publication1
Active sitei249Proton donor1 Publication1
Sitei310Transition state stabilizer1 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

BioCyciBSUB:BSU03040-MONOMER.
SABIO-RKP00691.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1By similarity)
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
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
PropeptideiPRO_000000133528 – 41Add BLAST14
ChainiPRO_000000133642 – 659Alpha-amylaseAdd BLAST618

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1659
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni47 – 49Combined sources3
Beta strandi52 – 54Combined sources3
Helixi60 – 65Combined sources6
Helixi67 – 72Combined sources6
Beta strandi76 – 80Combined sources5
Beta strandi84 – 86Combined sources3
Helixi90 – 92Combined sources3
Helixi96 – 103Combined sources8
Beta strandi105 – 112Combined sources8
Turni113 – 115Combined sources3
Helixi118 – 129Combined sources12
Turni130 – 132Combined sources3
Beta strandi134 – 139Combined sources6
Turni148 – 150Combined sources3
Helixi153 – 156Combined sources4
Beta strandi162 – 164Combined sources3
Helixi174 – 179Combined sources6
Beta strandi180 – 182Combined sources3
Helixi193 – 208Combined sources16
Beta strandi213 – 216Combined sources4
Helixi219 – 221Combined sources3
Helixi228 – 230Combined sources3
Helixi234 – 238Combined sources5
Beta strandi244 – 248Combined sources5
Helixi258 – 262Combined sources5
Beta strandi265 – 268Combined sources4
Helixi270 – 282Combined sources13
Helixi287 – 290Combined sources4
Beta strandi294 – 297Combined sources4
Helixi299 – 301Combined sources3
Beta strandi302 – 304Combined sources3
Helixi309 – 313Combined sources5
Turni318 – 321Combined sources4
Helixi324 – 335Combined sources12
Beta strandi337 – 345Combined sources9
Beta strandi359 – 361Combined sources3
Helixi369 – 372Combined sources4
Helixi374 – 386Combined sources13
Helixi396 – 398Combined sources3
Beta strandi402 – 407Combined sources6
Turni408 – 410Combined sources3
Beta strandi411 – 416Combined sources6
Beta strandi418 – 420Combined sources3
Beta strandi422 – 427Combined sources6
Beta strandi432 – 436Combined sources5
Beta strandi438 – 441Combined sources4
Beta strandi443 – 447Combined sources5
Beta strandi450 – 455Combined sources6
Beta strandi459 – 463Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAGX-ray2.50A42-466[»]
1UA7X-ray2.21A45-466[»]
ProteinModelPortaliP00691.
SMRiP00691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00691.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000008732.
InParanoidiP00691.
KOiK01176.
OMAiIKSIPNW.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR031965. CBM26.
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. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16738. CBM26. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. 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

        10         20         30         40         50
MFAKRFKTSL LPLFAGFLLL FHLVLAGPAA ASAETANKSN ELTAPSIKSG
60 70 80 90 100
TILHAWNWSF NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGDKSMSNWY
110 120 130 140 150
WLYQPTSYQI GNRYLGTEQE FKEMCAAAEE YGIKVIVDAV INHTTSDYAA
160 170 180 190 200
ISNEVKSIPN WTHGNTQIKN WSDRWDVTQN SLLGLYDWNT QNTQVQSYLK
210 220 230 240 250
RFLDRALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN TSAEFQYGEI
260 270 280 290 300
LQDSASRDAA YANYMDVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD
310 320 330 340 350
KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG
360 370 380 390 400
GGNGVRFPGK SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN
410 420 430 440 450
QIFMNQRGSH GVVLANAGSS SVSINTATKL PDGRYDNKAG AGSFQVNDGK
460 470 480 490 500
LTGTINARSV AVLYPDDIAK APHVFLENYK TGVTHSFNDQ LTITLRADAN
510 520 530 540 550
TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIMLKG TNSDGVTRTE
560 570 580 590 600
KYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGSRVIE LTGSWPGKPM
610 620 630 640 650
TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVLNGLYND

SGLSGSLPH
Length:659
Mass (Da):72,378
Last modified:June 16, 2009 - v2
Checksum:i16BD6CB1E7C67BD6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22H → Y in CAA26086 (PubMed:6099357).Curated1
Sequence conflicti22H → Y in AAA22234 (PubMed:6413492).Curated1
Sequence conflicti22H → Y in CAA23436 (PubMed:6189486).Curated1
Sequence conflicti22H → Y in AAA22230 (Ref. 8) Curated1
Sequence conflicti146S → F in CAA26086 (PubMed:6099357).Curated1
Sequence conflicti146S → F in AAA22234 (PubMed:6413492).Curated1
Sequence conflicti204D → E in CAA26086 (PubMed:6099357).Curated1
Sequence conflicti204D → E in AAA22234 (PubMed:6413492).Curated1
Sequence conflicti284N → K in CAA26086 (PubMed:6099357).Curated1
Sequence conflicti332A → S in AAA22234 (PubMed:6413492).Curated1
Sequence conflicti513 – 529ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in CAA23437 (PubMed:6186986).CuratedAdd BLAST17
Sequence conflicti513 – 529ETAFK…GKGDP → DDRRLRMEINSQSEKEIQ in BAA08938 (PubMed:8969502).CuratedAdd BLAST17

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti469 – 477AKAPHVFLE → EMRCNTFFQ in strain: N7 AMYEN+. 9
Natural varianti478 – 659Missing in strain: N7 AMYEN+. Add BLAST182

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003234692.1. NZ_JNCM01000030.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_003234692.1. NZ_JNCM01000030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BAGX-ray2.50A42-466[»]
1UA7X-ray2.21A45-466[»]
ProteinModelPortaliP00691.
SMRiP00691.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000008732.
InParanoidiP00691.
KOiK01176.
OMAiIKSIPNW.

Enzyme and pathway databases

BioCyciBSUB:BSU03040-MONOMER.
SABIO-RKP00691.

Miscellaneous databases

EvolutionaryTraceiP00691.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR031965. CBM26.
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. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16738. CBM26. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 149 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

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.