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P29957

- AMY_PSEHA

UniProt

P29957 - AMY_PSEHA

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Protein
Alpha-amylase
Gene
amy
Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit.1 Publication
Binds 1 chloride ion per subunit.1 Publication

Enzyme regulationi

Requires chloride ions for optimal activity.1 Publication

Temperature dependencei

Thermolabile.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Calcium
Binding sitei113 – 1131Substrate
Metal bindingi159 – 1591Calcium; via carbonyl oxygen
Metal bindingi168 – 1681Calcium
Binding sitei196 – 1961Chloride
Binding sitei196 – 1961Substrate By similarity
Active sitei198 – 1981Nucleophile1 Publication
Metal bindingi202 – 2021Calcium; via carbonyl oxygen
Active sitei224 – 2241Proton donor1 Publication
Binding sitei229 – 2291Substrate; via amide nitrogen By similarity
Binding sitei286 – 2861Chloride
Binding sitei287 – 2871Substrate By similarity
Sitei288 – 2881Transition state stabilizer By similarity
Binding sitei293 – 2931Substrate
Binding sitei324 – 3241Chloride

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

SABIO-RKP29957.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:amy
OrganismiPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Taxonomic identifieri228 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi324 – 3241K → Q: Abolishes chloride binding and reduces catalytic rate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 Publication
Add
BLAST
Chaini25 – 477453Alpha-amylase
PRO_0000001328Add
BLAST
Propeptidei478 – 669192Removed in mature form
PRO_0000001329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 982 Publications
Disulfide bondi144 ↔ 1612 Publications
Disulfide bondi352 ↔ 3592 Publications
Disulfide bondi426 ↔ 4402 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324
Helixi37 – 4610
Helixi48 – 514
Beta strandi55 – 584
Beta strandi67 – 693
Helixi70 – 745
Beta strandi75 – 773
Beta strandi79 – 813
Helixi88 – 10013
Beta strandi104 – 1107
Beta strandi112 – 1143
Beta strandi119 – 1213
Beta strandi126 – 1283
Helixi137 – 1393
Helixi150 – 1534
Helixi155 – 1606
Beta strandi161 – 1633
Beta strandi167 – 1693
Helixi174 – 19017
Beta strandi194 – 1985
Helixi200 – 2023
Helixi205 – 2139
Beta strandi215 – 2173
Beta strandi220 – 2234
Helixi235 – 2417
Beta strandi242 – 2454
Helixi247 – 25913
Helixi262 – 2676
Helixi270 – 2723
Helixi277 – 2793
Beta strandi280 – 2823
Helixi289 – 2913
Turni292 – 2943
Helixi302 – 3054
Helixi306 – 31712
Beta strandi320 – 3278
Beta strandi344 – 3463
Beta strandi352 – 3576
Helixi360 – 3623
Helixi364 – 37512
Turni376 – 3783
Beta strandi383 – 3875
Beta strandi389 – 3968
Helixi398 – 4003
Beta strandi401 – 4066
Beta strandi408 – 4103
Beta strandi415 – 4173
Beta strandi422 – 4265
Turni428 – 4303
Beta strandi440 – 4423
Beta strandi444 – 4474
Beta strandi451 – 4544
Beta strandi461 – 4666

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP29957.
SMRiP29957. Positions 25-472.

Miscellaneous databases

EvolutionaryTraceiP29957.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni71 – 755Substrate binding
Regioni201 – 2022Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29957-1 [UniParc]FASTAAdd to Basket

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MKLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP    50
KGYAAVQVSP PNEHITGSQW WTRYQPVSYE LQSRGGNRAQ FIDMVNRCSA 100
AGVDIYVDTL INHMAAGSGT GTAGNSFGNK SFPIYSPQDF HESCTINNSD 150
YGNDRYRVQN CELVGLADLD TASNYVQNTI AAYINDLQAI GVKGFRFDAS 200
KHVAASDIQS LMAKVNGSPV VFQEVIDQGG EAVGASEYLS TGLVTEFKYS 250
TELGNTFRNG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI 300
TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGDTDAGGP NVPVHNNGNL 350
ECFASNWKCE HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQISFGRGSS 400
GHMAINKEDS TLTATVQTDM ASGQYCNVLK GELSADAKSC SGEVITVNSD 450
GTINLNIGAW DAMAIHKNAK LNTSSASSTE SDWQRTVIFI NAQTQSGQDM 500
FIRGGIDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT SPWKANDNYL 550
DWYGIENGQS SEAEGSATDW TTNVWPAGWG AEKTVNTDGF GVTPLNIWGE 600
HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQDNA PYTSTNHMAQ 650
CGKINKFEFN NSGVVIRSF 669
Length:669
Mass (Da):73,268
Last modified:May 30, 2000 - v3
Checksum:iE3DD316D92B91EB7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58627 Genomic DNA. Translation: CAA41481.1.
PIRiS23257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58627 Genomic DNA. Translation: CAA41481.1 .
PIRi S23257.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AQH X-ray 2.00 A 25-477 [» ]
1AQM X-ray 1.85 A 25-477 [» ]
1B0I X-ray 2.40 A 25-477 [» ]
1G94 X-ray 1.74 A 25-472 [» ]
1G9H X-ray 1.80 A 25-472 [» ]
1JD7 X-ray 2.25 A 25-477 [» ]
1JD9 X-ray 2.50 A 25-477 [» ]
1KXH X-ray 2.30 A 25-472 [» ]
1L0P X-ray 2.10 A 25-472 [» ]
ProteinModelPortali P29957.
SMRi P29957. Positions 25-472.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P29957.

Miscellaneous databases

EvolutionaryTracei P29957.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAMY_PSEHA
AccessioniPrimary (citable) accession number: P29957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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