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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: 2 out of 5 - Protein predictedi

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491Magnesium 1; via carbonyl oxygen
Metal bindingi105 – 1051Magnesium 1
Metal bindingi113 – 1131Magnesium 1
Metal bindingi277 – 2771Magnesium 2
Metal bindingi281 – 2811Magnesium 2
Metal bindingi317 – 3171Magnesium 2; via carbonyl oxygen
Metal bindingi372 – 3721Magnesium 3
Metal bindingi374 – 3741Magnesium 3
Metal bindingi375 – 3751Magnesium 3

GO - Molecular functioni

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

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

PTM / Processingi

Proteomic databases

PRIDEiO08452.

Structurei

3D structure databases

ProteinModelPortaliO08452.
SMRiO08452. Positions 26-460.

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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MNIKKLTPLL TLLLFFIVLA SPVSAAKYLE LEEGGVIMQA FYWDVPGGGI    50
WWDHIRSKIP EWYEAGISAI WLPPPSKGMS GGYSMGYDPY DYFDLGEYYQ 100
KGTVETRFGS KEELVRLIQT AHAYGIKVIA DVVINHRAGG DLEWNPFVGD 150
YTWTDFSKVA SGKYTANYLD FHPNELHCCD EGTFGGFPDI CHHKEWDQYW 200
LWKSNESYAA YLRSIGFDGW RFDYVKGYGA WVVRDWLNWW GGWAVGEYWD 250
TNVDALLSWA YESGAKVFDF PLYYKMDEAF DNNNIPALVY ALQNGQTVVS 300
RDPFKAVTFV ANHDTDIIWN KYPAYAFILT YEGQPVIFYR DFEEWLNKDK 350
LINLIWIHDH LAGGSTTIVY YDNDELIFVR NGDSRRPGLI TYINLSPNWV 400
GRWVYVPKFA GACIHEYTGN LGGWVDKRVD SSGWVYLEAP PHDPANGYYG 450
YSVWSYCGVG 460
Length:460
Mass (Da):52,910
Last modified:July 1, 1997 - v1
Checksum:i0E0A2AEB5FCAF541
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96622 Genomic DNA. Translation: AAB67705.1.
AF001268 Genomic DNA. Translation: AAC45663.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96622 Genomic DNA. Translation: AAB67705.1 .
AF001268 Genomic DNA. Translation: AAC45663.1 .

3D structure databases

ProteinModelPortali O08452.
SMRi O08452. Positions 26-460.
ModBasei Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEi O08452.

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: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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