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P09961 (AMY1_DICT6) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. 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 1

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amyA
Ordered Locus Names:DICTH_0745
OrganismDictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) [Complete proteome] [HAMAP]
Taxonomic identifier309799 [NCBI]
Taxonomic lineageBacteriaDictyoglomiDictyoglomalesDictyoglomaceaeDictyoglomus

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This amylase is a highly liquefying-type: oligomers appeared at the beginning of incubation, followed by a graded decrease in the amounts of maltotriose, maltose and glucose in prolonged incubation.

Catalytic activity

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5. Stable above pH 5.5.

Temperature dependence:

Optimum temperature is about 90 degrees Celsius. Highly thermostable. Retains 70% of its maximal activity after heating 1 hour at 90 degrees Celsius, but no decrease in activity was observed within the same time at 80 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   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: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 686685Alpha-amylase 1
PRO_0000184571

Sites

Active site1251Nucleophile By similarity
Active site2161Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P09961 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DFF73F94A439E187

FASTA68681,192
        10         20         30         40         50         60 
MTKSIYFSLG IHNHQPVGNF DFVIERAYEM SYKPLINFFF KHPDFPINVH FSGFLLLWLE 

        70         80         90        100        110        120 
KNHPEYFEKL KIMAERGQIE FVSGGFYEPI LPIIPDKDKV QQIKKLNKYI YDKFGQTPKG 

       130        140        150        160        170        180 
MWLAERVWEP HLVKYIAEAG IEYVVVDDAH FFSVGLKEED LFGYYLMEEQ GYKLAVFPIS 

       190        200        210        220        230        240 
MKLRYLIPFA DPEETITYLD KFASEDKSKI ALLFDDGEKF GLWPDTYRTV YEEGWLETFV 

       250        260        270        280        290        300 
SKIKENFLLV TPVNLYTYMQ RVKPKGRIYL PTASYREMME WVLFPEAQKE LEELVEKLKT 

       310        320        330        340        350        360 
ENLWDKFSPY VKGGFWRNFL AKYDESNHMQ KKMLYVWKKV QDSPNEEVKE KAMEEVFQGQ 

       370        380        390        400        410        420 
ANDAYWHGIF GGLYLPHLRT AIYEHLIKAE NYLENSEIRF NIFDFDCDGN DEIIVESPFF 

       430        440        450        460        470        480 
NLYLSPNHGG SVLEWDFKTK AFNLTNVLTR RKEAYHSKLS YVTSEAQGKS IHERWTAKEE 

       490        500        510        520        530        540 
GLENILFYDN HRRVSFTEKI FESEPVLEDL WKDSSRLEVD SFYENYDYEI NKDENKIRVL 

       550        560        570        580        590        600 
FSGVFRGFEL CKSYILYKDK SFVDVVYEIK NVSETPISLN FGWEINLNFL APNHPDYYFL 

       610        620        630        640        650        660 
IGDQKYPLSS FGIEKVNNWK IFSGIGIELE CVLDVEASLY RYPIETVSLS EEGFERVYQG 

       670        680 
SALIHFYKVD LPVGSTWRTT IRFWVK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of a heat-stable amylase gene from an anaerobic thermophile, Dictyoglomus thermophilum."
Fukusumi S., Kamizono A., Horinouchi S., Beppu T.
Eur. J. Biochem. 174:15-21(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07896 Genomic DNA. Translation: CAA30735.1.
CP001146 Genomic DNA. Translation: ACI18637.1.
PIRALDYAT. S00628.
RefSeqYP_002250612.1. NC_011297.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309799.DICTH_0745.

Protein family/group databases

CAZyGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI18637; ACI18637; DICTH_0745.
GeneID6945629.
KEGGdth:DICTH_0745.
PATRIC21806130. VBIDicThe33784_0734.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1449.
HOGENOMHOG000223207.
KOK07405.
OMAHFMSAGL.
OrthoDBEOG6KT2JZ.
ProtClustDBCLSK2480645.

Enzyme and pathway databases

BioCycDTHE309799:GHF9-738-MONOMER.

Family and domain databases

Gene3D2.70.98.10. 1 hit.
3.20.110.10. 1 hit.
InterProIPR015179. A-amylase/a-glucTrfase_C.
IPR015178. A-amylase/a-glucTrfase_central.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR027291. Glyco_hydro_38/57_N.
IPR004300. Glyco_hydro_57_N.
[Graphical view]
PfamPF09094. DUF1925. 1 hit.
PF09095. DUF1926. 1 hit.
PF03065. Glyco_hydro_57. 1 hit.
[Graphical view]
ProDomPD014405. DUF1925. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF74650. SSF74650. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY1_DICT6
AccessionPrimary (citable) accession number: P09961
Secondary accession number(s): B5YDK4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 83 of the entry and version 2 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