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BACLI:AMY

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Species (Taxon ID) Bacillus licheniformis. (1402)
Gene Name(s) amyS (synonyms: amyL)
Protein Name(s) Alpha-amylase

1,4-alpha-D-glucan glucanohydrolase BLA

External Links
UniProt P06278
EMBL X03236
M38570
M13256
AF438149
K01984
M62637
M26412
PIR A91997
PDB 1BLI
1BPL
1E3X
1E3Z
1E40
1E43
1OB0
1VJS
PDBsum 1BLI
1BPL
1E3X
1E3Z
1E40
1E43
1OB0
1VJS
ProteinModelPortal P06278
SMR P06278
BindingDB P06278
ChEMBL CHEMBL4215
Allergome 8255
CAZy GH13
PRIDE P06278
EvolutionaryTrace P06278
GO GO:0004556
GO:0005509
GO:0005975
Gene3D 2.60.40.1180
3.20.20.80
InterPro IPR013776
IPR015237
IPR015902
IPR013780
IPR006047
IPR006589
IPR013781
IPR017853
PANTHER PTHR10357
Pfam PF00128
PF09154
PIRSF PIRSF001021
SMART SM00642
SUPFAM SSF51445

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004556

alpha-amylase activity

PMID:2540150[1]

ECO:0000314

F

Figure 1: The alpha-amylase is measured from B. licheniformis grown on media with starch and with or without glucose. Alpha-amylase activity greatly increased when starch was the main carbon source.

complete
CACAO 5000

enables

GO:0004556

alpha-amylase activity

PMID:2540150[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006047

F

Seeded From UniProt

complete

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013776
InterPro:IPR015237

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013776

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006047
InterPro:IPR013776

P

Seeded From UniProt

complete

enables

GO:0004556

alpha-amylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.1

F

Seeded From UniProt

complete

enables

GO:0103025

alpha-amylase activity (releasing maltohexaose)

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.1

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0119

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Laoide, BM et al. (1989) Bacillus licheniformis alpha-amylase gene, amyL, is subject to promoter-independent catabolite repression in Bacillus subtilis. J. Bacteriol. 171 2435-42 PubMed GONUTS page