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P49067 (AMYA_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. 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

EC=3.2.1.1
Gene names
Name:amyA
Ordered Locus Names:PF0272
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays a broad range of substrate specificity, with the capacity to hydrolyze carbohydrates as simple as maltotriose.

Catalytic activity

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

Subunit structure

Homodimer.

Sequence similarities

Belongs to the glycosyl hydrolase 57 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5-7.5.

Temperature dependence:

Optimum temperature is 100 degrees Celsius. Inactive below 40 degrees Celsius. Extremely thermostable.

Sequence caution

The sequence AAL80396.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 649648Alpha-amylase
PRO_0000184573

Sites

Active site1241Nucleophile By similarity
Active site2151Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P49067 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B75840D33D17146F

FASTA64976,309
        10         20         30         40         50         60 
MGDKINFIFG IHNHQPLGNF GWVFEEAYEK CYWPFLETLE EYPNMKVAIH TSGPLIEWLQ 

        70         80         90        100        110        120 
DNRPEYIDLL RSLVKRGQVE IVVAGFYEPV LASIPKEDRI EQIRLMKEWA KSIGFDARGV 

       130        140        150        160        170        180 
WLTERVWQPE LVKTLKESGI DYVIVDDYHF MSAGLSKEEL YWPYYTEDGG EVIAVFPIDE 

       190        200        210        220        230        240 
KLRYLIPFRP VDKVLEYLHS LIDGDESKVA VFHDDGEKFG IWPGTYEWVY EKGWLREFFD 

       250        260        270        280        290        300 
RISSDEKINL MLYTEYLEKY KPRGLVYLPI ASYFEMSEWS LPAKQARLFV EFVNELKVKG 

       310        320        330        340        350        360 
IFEKYRVFVR GGIWKNFFYK YPESNYMHKR MLMVSKLVRN NPEARKYLLR AQCNDAYWHG 

       370        380        390        400        410        420 
LFGGVYLPHL RRAIWNNLIK ANSYVSLGKV IRDIDYDGFE EVLIENDNFY AVFKPSYGGS 

       430        440        450        460        470        480 
LVEFSSKNRL VNYVDVLARR WEHYHGYVES QFDGVASIHE LEKKIPDEIR KEVAYDKYRR 

       490        500        510        520        530        540 
FMLQDHVVPL GTTLEDFMFS RQQEIGEFPR VPYSYELLDG GIRLKREHLG IEVEKTVKLV 

       550        560        570        580        590        600 
NDGFEVEYIV NNKTGNPVLF AVELNVAVQS IMESPGVLRG KEIVVDDKYA VGKFALKFED 

       610        620        630        640 
EMEVWKYPVK TLSQSESGWD LIQQGVSYIV PIRLEDKIRF KLKFEEASG 

« Hide

References

« Hide 'large scale' references
[1]"Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli."
Laderman K.A., Asada K., Uemori T., Mukai H., Taguchi Y., Kato I., Anfinsen C.B.
J. Biol. Chem. 268:24402-24407(1993) [PubMed: 8226990] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus."
Laderman K.A., Davis B.R., Krutzsch H.C., Lewis M.S., Griko Y.V., Privalov P.L., Anfinsen C.B.
J. Biol. Chem. 268:24394-24401(1993) [PubMed: 8226989] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22346 Unassigned DNA. Translation: AAA72035.1.
AE009950 Genomic DNA. Translation: AAL80396.1. Different initiation.
PIRA49512.
RefSeqNP_578001.1. NC_003413.1.

3D structure databases

ProteinModelPortalP49067.
SMRP49067. Positions 3-646.
ModBaseSearch...

Protein family/group databases

CAZyGH57. Glycoside Hydrolase Family 57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000005619; EBPYRP00000005480; EBPYRG00000005618.
GeneID1468106.
GenomeReviewsGene locus PF0272 in contig AE009950_GR.
KEGGpfu:PF0272.
NMPDRfig|186497.1.peg.277.

Phylogenomic databases

GeneTreeEBGT00050000023113.
HOGENOMHBG460637.
OMALTERVWE.
ProtClustDBCLSK2459743.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16304.

Family and domain databases

InterProIPR015179. A-amylase/a-glucTrfase_C.
IPR015178. A-amylase/a-glucTrfase_central.
IPR011013. Glyco_hydro-type_carb-bd.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR000602. Glyco_hydro_38_core.
IPR004300. Glyco_hydro_57_N.
[Graphical view]
Gene3DG3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit.
KOK07405.
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. Gal_mut_like. 1 hit.
SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMYA_PYRFU
AccessionPrimary (citable) accession number: P49067
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 74 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