Alpha amylase - Pyrococcus furiosus

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O08452 (O08452_9EURY) Unreviewed, UniProtKB/TrEMBL

Last modified July 27, 2011. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Alpha amylase EMBL AAC45663.1
EC=3.2.1.1 EMBL AAC45663.1

Submitted name:
Alpha-amylase EMBL AAB67705.1

Gene names

Name:

amyA EMBL AAC45663.1

Organism

Pyrococcus furiosus EMBL AAC45663.1

Taxonomic identifier

2261 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	460 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1MWO PDB 1MXD PDB 1MXG Magnesium PDB 1MXG Metal-binding PDB 1MWO PDB 1MXD PDB 1MXG Zinc PDB 1MWO PDB 1MXD PDB 1MXG
Molecular function	Glycosidase EMBL AAC45663.1 Hydrolase
Technical term	3D-structure PDB 1MWO PDB 1MXD PDB 1MXG
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

316 – 321

Glucose binding PDB 1MXD

Sites

Metal binding

Zinc 1 PDB 1MWO

Metal binding

Zinc 1 PDB 1MWO PDB 1MXD

Metal binding

Zinc 2 PDB 1MXD

Metal binding

Zinc 3 PDB 1MXD

Metal binding

105

Zinc 1 PDB 1MXD

Metal binding

105

Zinc 2 PDB 1MXD

Metal binding

105

Zinc 3 PDB 1MXD

Metal binding

113

Zinc 1 PDB 1MXD

Metal binding

113

Zinc 2 PDB 1MXD

Metal binding

113

Zinc 3 PDB 1MXD

Metal binding

135

Calcium PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

172

Zinc 1; via tele nitrogen PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

177

Zinc 1; via tele nitrogen PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

180

Calcium PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

182

Calcium; via carbonyl oxygen PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

189

Calcium PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

191

Zinc 1 PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

227

Calcium; via carbonyl oxygen PDB 1MWO PDB 1MXD PDB 1MXG

Metal binding

277

Magnesium PDB 1MXG

Metal binding

277

Zinc 2 PDB 1MWO PDB 1MXD

Metal binding

281

Magnesium PDB 1MXG

Metal binding

281

Zinc 2 PDB 1MWO PDB 1MXD

Metal binding

317

Magnesium; via carbonyl oxygen PDB 1MXG

Metal binding

317

Zinc 2 PDB 1MWO PDB 1MXD

Metal binding

343

Zinc 1 PDB 1MWO PDB 1MXD

Metal binding

343

Zinc 2 PDB 1MXD

Metal binding

343

Zinc 3 PDB 1MXD

Metal binding

348

Zinc 1 PDB 1MWO PDB 1MXD

Metal binding

348

Zinc 2 PDB 1MXD

Metal binding

348

Zinc 3 PDB 1MXD

Metal binding

372

Zinc 1 PDB 1MXD

Metal binding

372

Zinc 3 PDB 1MWO PDB 1MXD

Metal binding

374

Zinc 1 PDB 1MXD

Metal binding

374

Zinc 3 PDB 1MWO PDB 1MXD

Metal binding

375

Zinc 1 PDB 1MXD

Metal binding

375

Zinc 3 PDB 1MWO PDB 1MXD

Binding site

345

Glucose PDB 1MXD

Sequences

Sequence

Length

Mass (Da)

Tools

O08452 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 0E0A2AEB5FCAF541
Show »

FASTA

460

52,910

        10         20         30         40         50         60 
MNIKKLTPLL TLLLFFIVLA SPVSAAKYLE LEEGGVIMQA FYWDVPGGGI WWDHIRSKIP 

        70         80         90        100        110        120 
EWYEAGISAI WLPPPSKGMS GGYSMGYDPY DYFDLGEYYQ KGTVETRFGS KEELVRLIQT 

       130        140        150        160        170        180 
AHAYGIKVIA DVVINHRAGG DLEWNPFVGD YTWTDFSKVA SGKYTANYLD FHPNELHCCD 

       190        200        210        220        230        240 
EGTFGGFPDI CHHKEWDQYW LWKSNESYAA YLRSIGFDGW RFDYVKGYGA WVVRDWLNWW 

       250        260        270        280        290        300 
GGWAVGEYWD TNVDALLSWA YESGAKVFDF PLYYKMDEAF DNNNIPALVY ALQNGQTVVS 

       310        320        330        340        350        360 
RDPFKAVTFV ANHDTDIIWN KYPAYAFILT YEGQPVIFYR DFEEWLNKDK LINLIWIHDH 

       370        380        390        400        410        420 
LAGGSTTIVY YDNDELIFVR NGDSRRPGLI TYINLSPNWV GRWVYVPKFA GACIHEYTGN 

       430        440        450        460 
LGGWVDKRVD SSGWVYLEAP PHDPANGYYG YSVWSYCGVG

« Hide

References

[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: 9293008] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM 3638 EMBL AAC45663.1.
[2]	"Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc." Linden A., Mayans O., Meyer-Klaucke W., Antranikian G., Wilmanns M. J. Biol. Chem. 278:9875-9884(2003) [PubMed: 12482867] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-460 IN COMPLEX WITH CALCIUM; GLUCOSE; MAGNESIUM AND ZINC.
[3]	"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: 9195939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM3638 EMBL AAB67705.1.
[4]	Joergensen S.T., Vorgias C.E., Antranikian G. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM3638 EMBL AAB67705.1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U96622 Genomic DNA. Translation: AAB67705.1.
AF001268 Genomic DNA. Translation: AAC45663.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MWO	X-ray	2.20	A	26-460	[»]
1MXD	X-ray	2.00	A	26-460	[»]
1MXG	X-ray	1.60	A	26-460	[»]

ProteinModelPortal

O08452.

SMR

O08452. Positions 26-460.

ModBase

Search...

Protein family/group databases

CAZy

GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR013776. A-amylase_thermo.
IPR015237. Alpha-amylase_C_pro.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF09154. DUF1939. 1 hit.
[Graphical view]

PIRSF

PIRSF001021. Alph-amls_thrmst. 1 hit.

PRINTS

PR00110. ALPHAAMYLASE.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

O08452_9EURY

Accession

Primary (citable) accession number: O08452

Entry history

Integrated into UniProtKB/TrEMBL:	July 1, 1997
Last sequence update:	July 1, 1997
Last modified:	July 27, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Entry information