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P14898 (AMY2_DICT6) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 77. 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:
Alpha-amylase 2

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amyB
Ordered Locus Names:DICTH_0636.1
OrganismDictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) [Complete proteome] [HAMAP]
Taxonomic identifier309799 [NCBI]
Taxonomic lineageBacteriaDictyoglomiDictyoglomalesDictyoglomaceaeDictyoglomus

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 Potential.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

When compared to AmyA, AmyB produced larger amounts of reducing sugar.

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
Direct protein sequencing
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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Alpha-amylase 2
PRO_0000054285

Sites

Active site3091Nucleophile By similarity
Active site3381Proton donor By similarity
Metal binding2361Calcium Potential
Site4041Transition state stabilizer By similarity

Experimental info

Sequence conflict1241N → S in CAA31586. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14898 [UniParc].

Last modified January 20, 2009. Version 2.
Checksum: 368FF33D155FC3F4

FASTA56267,027
        10         20         30         40         50         60 
MIYDDKIFGD LCHKEFLVER EVKKLEEIYL EEVLPEDPKP EDEIEFTFNC PLKFHITSGK 

        70         80         90        100        110        120 
IVKDNREIYT FNIQERKTQW NDSIFNFSEI IKIKIPPLKE NGLYQIHLYE MNEKIYEQYL 

       130        140        150        160        170        180 
SIDNFEAPLW SEESIIYHIF IDRFAKDEKE VEYSENLKEK LGGNLKGILS RLDYIENLGI 

       190        200        210        220        230        240 
NTIWISPIFK STSYHGYDIE DYFEIDPIWG TKEDLKKLVR EAFNRGIRII LDFVPNHMSY 

       250        260        270        280        290        300 
KNPIFQKALK DKNSNLRSWF IFKGEDYETF FGVKSMPKIN LKNKEAIDYI INAAKYWIRE 

       310        320        330        340        350        360 
FGISGYRMDH ATGPDINFWS IFYYNLKSEF PETFYFGEIV ETPKETKKYV GKFDGTLDFY 

       370        380        390        400        410        420 
LFKIIRDFFI GKRWSTKEFV KMIDLEEKFY GNKFKRISFL ENHDSNRFLW VAKDKKLLRL 

       430        440        450        460        470        480 
ASIFQFSINA IPIIYNGQEM GCSQYRDILE GNRTLHEHAR LPIPWSDDKQ DKELIDFYRQ 

       490        500        510        520        530        540 
LVKIRKSHPA LYKGTFIPIF SDMISFIKET QEESILVLIN IEDKEEIFNL NGTYRDLFSG 

       550        560 
NIYTNSLKLG PMSAHLLLRI DH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression in Escherichia coli of two additional amylase genes of a strictly anaerobic thermophile, Dictyoglomus thermophilum, and their nucleotide sequences with extremely low guanine-plus-cytosine contents."
Horinouchi S., Fukusumi S., Ohshima T., Beppu T.
Eur. J. Biochem. 176:243-253(1988) [PubMed: 2458257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8.
[2]"The complete genome sequence of Dictyoglomus thermophilum strain ATCC 35947 / DSM 3960 / H-6-12."
Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35947 / DSM 3960 / H-6-12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13199 Genomic DNA. Translation: CAA31586.1.
CP001146 Genomic DNA. No translation available.
PIRS01312.

3D structure databases

ProteinModelPortalP14898.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus DICTH_0636.1 in contig CP001146_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG465660.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY2_DICT6
AccessionPrimary (citable) accession number: P14898
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 20, 2009
Last modified: December 14, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families