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P26613 (AMY2_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic alpha-amylase

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amyA
Ordered Locus Names:STM1963
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-amylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Cytoplasmic alpha-amylase
PRO_0000054288

Sites

Active site2351Nucleophile By similarity
Active site2651Proton donor By similarity
Metal binding1041Calcium By similarity
Metal binding2391Calcium; via carbonyl oxygen By similarity
Site3321Transition state stabilizer By similarity

Experimental info

Sequence conflict4621L → S in AAA27110. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26613 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: 5C1E862FEDD5E47C

FASTA49456,522
        10         20         30         40         50         60 
MKNPTLLQYF HWYYPDGGKL WSELAERADG LNDIGINMVW LPPACKGASG GYSVGYDTYD 

        70         80         90        100        110        120 
LFDLGEFDQK GTIATKYGDK RQLLTAIDAL KKNNIAVLLD VVVNHKMGAD EKERIRVQRV 

       130        140        150        160        170        180 
NQDDRTQIDD NIIECEGWTR YTFPARAGQY SNFIWDYHCF SGIDHIENPD EDGIFKIVND 

       190        200        210        220        230        240 
YTGDGWNDQV DDEMGNFDYL MGENIDFRNH AVTEEIKYWA RWVMEQTHCD GFRLDAVKHI 

       250        260        270        280        290        300 
PAWFYKEWIE HVQAVAPKPL FIVAEYWSHE VDKLQTYIDQ VDGKTMLFDA PLQMKFHEAS 

       310        320        330        340        350        360 
RQGAEYDMRH IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL AYALILLREN 

       370        380        390        400        410        420 
GVPSVFYPDL YGASYEDSGE NGETCRVDMP VINQLDRLIL ARQRFAHGIQ TLFFDHPNCI 

       430        440        450        460        470        480 
AFSRSGTEEN PGCVVVLSNG DDGEKTLLLG DNYANKTWRD FLGNRDEYVV TNDQGEATFF 

       490 
CNAGSVSVWV IEDV 

« Hide

References

« Hide 'large scale' references
[1]"Escherichia coli produces a cytoplasmic alpha-amylase, AmyA."
Raha M., Kawagishi I., Mueller V., Kihara M., Macnab R.M.
J. Bacteriol. 174:6644-6652(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SJW1103.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Subdivision of flagellar region III of the Escherichia coli and Salmonella typhimurium chromosomes and identification of two additional flagellar genes."
Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.
J. Gen. Microbiol. 138:1051-1065(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
Strain: SJW1103.
[4]"Organization of the Escherichia coli and Salmonella typhimurium chromosomes between flagellar regions IIIa and IIIb, including a large non-coding region."
Raha M., Kihara M., Kawagishi I., Macnab R.M.
J. Gen. Microbiol. 139:1401-1407(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-494.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01643 Genomic DNA. Translation: AAA27110.1.
AE006468 Genomic DNA. Translation: AAL20875.1.
M85241 Genomic DNA. Translation: AAA27079.1.
L13280 Unassigned DNA. Translation: AAA71970.1.
PIRB45738.
RefSeqNP_460916.1. NC_003197.1.

3D structure databases

ProteinModelPortalP26613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1963.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20875; AAL20875; STM1963.
GeneID1253484.
KEGGstm:STM1963.
PATRIC32382487. VBISalEnt20916_2079.

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000094847.
KOK01176.
OMARATKYGD.
OrthoDBEOG65QWH3.
PhylomeDBP26613.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1974-MONOMER.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013776. A-amylase_thermo.
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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY2_SALTY
AccessionPrimary (citable) accession number: P26613
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries