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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

Protein has several cofactor binding sites:
  • Ca2+1 PublicationNote: Binds 1 Ca(2+) ion per subunit.1 Publication
  • chloride1 PublicationNote: Binds 1 Cl(-) 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 – 1961SubstrateBy similarity
Active sitei198 – 1981Nucleophile1 Publication
Metal bindingi202 – 2021Calcium; via carbonyl oxygen
Active sitei224 – 2241Proton donor1 Publication
Binding sitei229 – 2291Substrate; via amide nitrogenBy similarity
Binding sitei286 – 2861Chloride
Binding sitei287 – 2871SubstrateBy similarity
Sitei288 – 2881Transition state stabilizerBy 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 PublicationAdd
BLAST
Chaini25 – 477453Alpha-amylasePRO_0000001328Add
BLAST
Propeptidei478 – 669192Removed in mature formPRO_0000001329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 98
Disulfide bondi144 ↔ 161
Disulfide bondi352 ↔ 359
Disulfide bondi426 ↔ 440

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
669
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 324Combined sources
Helixi37 – 4610Combined sources
Helixi48 – 514Combined sources
Beta strandi55 – 584Combined sources
Beta strandi67 – 693Combined sources
Helixi70 – 745Combined sources
Beta strandi75 – 773Combined sources
Beta strandi79 – 813Combined sources
Helixi88 – 10013Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi126 – 1283Combined sources
Helixi137 – 1393Combined sources
Helixi150 – 1534Combined sources
Helixi155 – 1606Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi167 – 1693Combined sources
Helixi174 – 19017Combined sources
Beta strandi194 – 1985Combined sources
Helixi200 – 2023Combined sources
Helixi205 – 2139Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi220 – 2234Combined sources
Helixi235 – 2417Combined sources
Beta strandi242 – 2454Combined sources
Helixi247 – 25913Combined sources
Helixi262 – 2676Combined sources
Helixi270 – 2723Combined sources
Helixi277 – 2793Combined sources
Beta strandi280 – 2823Combined sources
Helixi289 – 2913Combined sources
Turni292 – 2943Combined sources
Helixi302 – 3054Combined sources
Helixi306 – 31712Combined sources
Beta strandi320 – 3278Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi352 – 3576Combined sources
Helixi360 – 3623Combined sources
Helixi364 – 37512Combined sources
Turni376 – 3783Combined sources
Beta strandi383 – 3875Combined sources
Beta strandi389 – 3968Combined sources
Helixi398 – 4003Combined sources
Beta strandi401 – 4066Combined sources
Beta strandi408 – 4103Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi422 – 4265Combined sources
Turni428 – 4303Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi444 – 4474Combined sources
Beta strandi451 – 4544Combined sources
Beta strandi461 – 4666Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29957.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

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

« Hide

        10         20         30         40         50
MKLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP
60 70 80 90 100
KGYAAVQVSP PNEHITGSQW WTRYQPVSYE LQSRGGNRAQ FIDMVNRCSA
110 120 130 140 150
AGVDIYVDTL INHMAAGSGT GTAGNSFGNK SFPIYSPQDF HESCTINNSD
160 170 180 190 200
YGNDRYRVQN CELVGLADLD TASNYVQNTI AAYINDLQAI GVKGFRFDAS
210 220 230 240 250
KHVAASDIQS LMAKVNGSPV VFQEVIDQGG EAVGASEYLS TGLVTEFKYS
260 270 280 290 300
TELGNTFRNG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI
310 320 330 340 350
TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGDTDAGGP NVPVHNNGNL
360 370 380 390 400
ECFASNWKCE HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQISFGRGSS
410 420 430 440 450
GHMAINKEDS TLTATVQTDM ASGQYCNVLK GELSADAKSC SGEVITVNSD
460 470 480 490 500
GTINLNIGAW DAMAIHKNAK LNTSSASSTE SDWQRTVIFI NAQTQSGQDM
510 520 530 540 550
FIRGGIDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT SPWKANDNYL
560 570 580 590 600
DWYGIENGQS SEAEGSATDW TTNVWPAGWG AEKTVNTDGF GVTPLNIWGE
610 620 630 640 650
HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQDNA PYTSTNHMAQ
660
CGKINKFEFN NSGVVIRSF
Length:669
Mass (Da):73,268
Last modified:May 30, 2000 - v3
Checksum:iE3DD316D92B91EB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58627 Genomic DNA. Translation: CAA41481.1.
PIRiS23257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58627 Genomic DNA. Translation: CAA41481.1 .
PIRi S23257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 96 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