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Reviewed, UniProtKB/Swiss-Prot P26613 (AMY2_SALTY)

Last modified November 3, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

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
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: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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
Active site3321 By similarity
Metal binding1041Calcium By similarity
Metal binding2391Calcium; via carbonyl oxygen By similarity

Experimental info

Sequence conflict4621L → S in AAA27110. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26613-1 [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: 1400215] [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: 11677609] [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: 1527488] [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: 8371104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-494.

Cross-references

Sequence databases

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.

3D structure databases

HSSPHSSP built from PDB template 1HVX based on UniProtKB P06279.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Genome annotation databases

GeneID1253484.
GenomeReviewsGene locus STM1963 in contig AE006468_GR.
KEGGstm:STM1963.
NMPDRfig|99287.1.peg.1897.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP26613.
OMAVWIPPAY.

Enzyme and pathway databases

BioCycSTYP99287:STM1963-MON.
BRENDA3.2.1.1. 2.

Family and domain databases

InterProIPR013776. A-amylase_thermo.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001021. Alph-amls_thrmst. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
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: November 3, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents