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O08452

- O08452_9EURY

UniProt

O08452 - O08452_9EURY

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Protein
Submitted name:

Alpha amylase

Gene

amyA

Organism
Pyrococcus furiosus
Status
Unreviewed - 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

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

Structurei

3D structure databases

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

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        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

ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O08452.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR013776. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view ]
PIRSFi PIRSF001021. Alph-amls_thrmst. 1 hit.
PRINTSi PR00110. ALPHAAMYLASE.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)