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P29957 (AMY_PSEHA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:amy
OrganismPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Taxonomic identifier228 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit. Ref.5

Binds 1 chloride ion per subunit. Ref.5

Enzyme regulation

Requires chloride ions for optimal activity. Ref.5

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Biophysicochemical properties

Temperature dependence:

Thermolabile.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionalpha-amylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1
Chain25 – 477453Alpha-amylase
PRO_0000001328
Propeptide478 – 669192Removed in mature form
PRO_0000001329

Regions

Region71 – 755Substrate binding
Region201 – 2022Substrate binding By similarity

Sites

Active site1981Nucleophile Ref.4
Active site2241Proton donor Ref.4
Metal binding1121Calcium
Metal binding1591Calcium; via carbonyl oxygen
Metal binding1681Calcium
Metal binding2021Calcium; via carbonyl oxygen
Binding site1131Substrate
Binding site1961Chloride
Binding site1961Substrate By similarity
Binding site2291Substrate; via amide nitrogen By similarity
Binding site2861Chloride
Binding site2871Substrate By similarity
Binding site2931Substrate
Binding site3241Chloride
Site2881Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond44 ↔ 98 Ref.4 Ref.5
Disulfide bond144 ↔ 161 Ref.4 Ref.5
Disulfide bond352 ↔ 359 Ref.4 Ref.5
Disulfide bond426 ↔ 440 Ref.4 Ref.5

Experimental info

Mutagenesis3241K → Q: Abolishes chloride binding and reduces catalytic rate. Ref.5

Secondary structure

.................................................................................................. 669
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29957 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: E3DD316D92B91EB7

FASTA66973,268
        10         20         30         40         50         60 
MKLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP KGYAAVQVSP 

        70         80         90        100        110        120 
PNEHITGSQW WTRYQPVSYE LQSRGGNRAQ FIDMVNRCSA AGVDIYVDTL INHMAAGSGT 

       130        140        150        160        170        180 
GTAGNSFGNK SFPIYSPQDF HESCTINNSD YGNDRYRVQN CELVGLADLD TASNYVQNTI 

       190        200        210        220        230        240 
AAYINDLQAI GVKGFRFDAS KHVAASDIQS LMAKVNGSPV VFQEVIDQGG EAVGASEYLS 

       250        260        270        280        290        300 
TGLVTEFKYS TELGNTFRNG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI 

       310        320        330        340        350        360 
TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGDTDAGGP NVPVHNNGNL ECFASNWKCE 

       370        380        390        400        410        420 
HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQISFGRGSS GHMAINKEDS TLTATVQTDM 

       430        440        450        460        470        480 
ASGQYCNVLK GELSADAKSC SGEVITVNSD GTINLNIGAW DAMAIHKNAK LNTSSASSTE 

       490        500        510        520        530        540 
SDWQRTVIFI NAQTQSGQDM FIRGGIDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT 

       550        560        570        580        590        600 
SPWKANDNYL DWYGIENGQS SEAEGSATDW TTNVWPAGWG AEKTVNTDGF GVTPLNIWGE 

       610        620        630        640        650        660 
HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQDNA PYTSTNHMAQ CGKINKFEFN 


NSGVVIRSF 

« Hide

References

[1]"Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23."
Feller G., Lonhienne T., Deroanne C., Libioulle C., van Beeumen J., Gerday C.
J. Biol. Chem. 267:5217-5221(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64 AND 471-477.
Strain: A23.
[2]"Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis."
Feller G., D'Amico S., Benotmane A.M., Joly F., van Beeumen J., Gerday C.
J. Biol. Chem. 273:12109-12115(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
Strain: A23.
[3]"Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor."
Aghajari N., Feller G., Gerday C., Haser R.
Protein Sci. 7:564-572(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-477.
Strain: A23.
[4]"Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase."
Aghajari N., Roth M., Haser R.
Biochemistry 41:4273-4280(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 25-472 IN COMPLEX WITH OLIGOSACCHARIDE, ACTIVE SITE, DISULFIDE BONDS.
[5]"Structural basis of alpha-amylase activation by chloride."
Aghajari N., Feller G., Gerday C., Haser R.
Protein Sci. 11:1435-1441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-472 IN COMPLEXES WITH CALCIUM, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF LYS-324, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58627 Genomic DNA. Translation: CAA41481.1.
PIRS23257.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQHX-ray2.00A25-477[»]
1AQMX-ray1.85A25-477[»]
1B0IX-ray2.40A25-477[»]
1G94X-ray1.74A25-472[»]
1G9HX-ray1.80A25-472[»]
1JD7X-ray2.25A25-477[»]
1JD9X-ray2.50A25-477[»]
1KXHX-ray2.30A25-472[»]
1L0PX-ray2.10A25-472[»]
ProteinModelPortalP29957.
SMRP29957. Positions 25-472.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP29957.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP29957.

Entry information

Entry nameAMY_PSEHA
AccessionPrimary (citable) accession number: P29957
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: October 16, 2013
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries