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Protein
Submitted name:

Alpha amylase

Gene

amyA

Organism
Pyrococcus furiosus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseImported, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.1. 5243.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha amylaseImported (EC:3.2.1.1Imported)
Submitted name:
Alpha-amylaseImported
Gene namesi
Name:amyAImported
OrganismiPyrococcus furiosusImported
Taxonomic identifieri2261 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

PTM / Processingi

Proteomic databases

PRIDEiO08452.

Structurei

3D structure databases

SMRiO08452. Positions 26-460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08452.

Family & Domainsi

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

O08452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIKKLTPLL TLLLFFIVLA SPVSAAKYLE LEEGGVIMQA FYWDVPGGGI
60 70 80 90 100
WWDHIRSKIP EWYEAGISAI WLPPPSKGMS GGYSMGYDPY DYFDLGEYYQ
110 120 130 140 150
KGTVETRFGS KEELVRLIQT AHAYGIKVIA DVVINHRAGG DLEWNPFVGD
160 170 180 190 200
YTWTDFSKVA SGKYTANYLD FHPNELHCCD EGTFGGFPDI CHHKEWDQYW
210 220 230 240 250
LWKSNESYAA YLRSIGFDGW RFDYVKGYGA WVVRDWLNWW GGWAVGEYWD
260 270 280 290 300
TNVDALLSWA YESGAKVFDF PLYYKMDEAF DNNNIPALVY ALQNGQTVVS
310 320 330 340 350
RDPFKAVTFV ANHDTDIIWN KYPAYAFILT YEGQPVIFYR DFEEWLNKDK
360 370 380 390 400
LINLIWIHDH LAGGSTTIVY YDNDELIFVR NGDSRRPGLI TYINLSPNWV
410 420 430 440 450
GRWVYVPKFA GACIHEYTGN LGGWVDKRVD SSGWVYLEAP PHDPANGYYG
460
YSVWSYCGVG
Length:460
Mass (Da):52,910
Last modified:July 1, 1997 - v1
Checksum:i0E0A2AEB5FCAF541
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96622 Genomic DNA. Translation: AAB67705.1.
AF001268 Genomic DNA. Translation: AAC45663.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96622 Genomic DNA. Translation: AAB67705.1.
AF001268 Genomic DNA. Translation: AAC45663.1.

3D structure databases

SMRiO08452. Positions 26-460.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiO08452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.1. 5243.

Miscellaneous databases

EvolutionaryTraceiO08452.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]
PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme."
    Dong G., Vieille C., Savchenko A., Zeikus J.G.
    Appl. Environ. Microbiol. 63:3569-3576(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 3638Imported.
  2. "Cloning, sequencing, characterization, and expression of an extracellular alpha-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis."
    Jorgensen S., Vorgias C.E., Antranikian G.
    J. Biol. Chem. 272:16335-16342(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM3638Imported.
  3. Joergensen S.T., Vorgias C.E., Antranikian G.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM3638Imported.

Entry informationi

Entry nameiO08452_9EURY
AccessioniPrimary (citable) accession number: O08452
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: April 1, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.