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Protein

Alpha-amylase

Gene

amy

Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed-Annotation score: 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.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Requires chloride ions for optimal activity.1 Publication

Temperature dependencei

Thermolabile.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi112CalciumCombined sources3 Publications1
Binding sitei113Substrate1 Publication1
Metal bindingi159Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi168CalciumCombined sources3 Publications1
Binding sitei196ChlorideCombined sources2 Publications1
Binding sitei196SubstrateBy similarity1
Active sitei198Nucleophile1 Publication1
Metal bindingi202Calcium; via carbonyl oxygenCombined sources3 Publications1
Active sitei224Proton donor1 Publication1
Binding sitei231Substrate1 Publication1
Binding sitei286ChlorideCombined sources1 Publication1
Binding sitei288Substrate1 Publication1
Sitei288Transition state stabilizerBy similarity1
Binding sitei293Substrate1 Publication1
Binding sitei324ChlorideCombined sources2 Publications1

GO - Molecular functioni

GO - Biological processi

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:3.2.1.11 Publication)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:amy
OrganismiPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Taxonomic identifieri228 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi324K → Q: Abolishes chloride binding and reduces catalytic rate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000000132825 – 477Alpha-amylaseAdd BLAST453
PropeptideiPRO_0000001329478 – 669Removed in mature formAdd BLAST192

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 98Combined sources3 Publications
Disulfide bondi144 ↔ 161Combined sources3 Publications
Disulfide bondi352 ↔ 359Combined sources3 Publications
Disulfide bondi426 ↔ 440Combined sources3 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi722419.PH505_bq00240.

Structurei

Secondary structure

1669
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 32Combined sources4
Helixi37 – 46Combined sources10
Helixi48 – 51Combined sources4
Beta strandi55 – 58Combined sources4
Beta strandi67 – 69Combined sources3
Helixi70 – 74Combined sources5
Beta strandi75 – 77Combined sources3
Beta strandi79 – 81Combined sources3
Helixi88 – 100Combined sources13
Beta strandi104 – 110Combined sources7
Beta strandi112 – 114Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi126 – 128Combined sources3
Helixi137 – 139Combined sources3
Helixi150 – 153Combined sources4
Helixi155 – 160Combined sources6
Beta strandi161 – 163Combined sources3
Beta strandi167 – 169Combined sources3
Helixi174 – 190Combined sources17
Beta strandi194 – 198Combined sources5
Helixi200 – 202Combined sources3
Helixi205 – 213Combined sources9
Beta strandi215 – 217Combined sources3
Beta strandi220 – 223Combined sources4
Helixi235 – 241Combined sources7
Beta strandi242 – 245Combined sources4
Helixi247 – 259Combined sources13
Helixi262 – 267Combined sources6
Helixi270 – 272Combined sources3
Helixi277 – 279Combined sources3
Beta strandi280 – 282Combined sources3
Helixi289 – 291Combined sources3
Turni292 – 294Combined sources3
Helixi302 – 305Combined sources4
Helixi306 – 317Combined sources12
Beta strandi320 – 327Combined sources8
Beta strandi344 – 346Combined sources3
Beta strandi352 – 357Combined sources6
Helixi360 – 362Combined sources3
Helixi364 – 375Combined sources12
Turni376 – 378Combined sources3
Beta strandi383 – 387Combined sources5
Beta strandi389 – 396Combined sources8
Helixi398 – 400Combined sources3
Beta strandi401 – 406Combined sources6
Beta strandi408 – 410Combined sources3
Beta strandi415 – 417Combined sources3
Beta strandi422 – 426Combined sources5
Turni428 – 430Combined sources3
Beta strandi440 – 442Combined sources3
Beta strandi444 – 447Combined sources4
Beta strandi451 – 454Combined sources4
Beta strandi461 – 466Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP29957.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni71 – 75Substrate binding1 Publication5
Regioni201 – 202Substrate binding1 Publication2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E54. Bacteria.
COG0366. LUCA.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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.
PIRiS23257.

3D structure databases

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

Protein-protein interaction databases

STRINGi722419.PH505_bq00240.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105E54. Bacteria.
COG0366. LUCA.

Enzyme and pathway databases

SABIO-RKP29957.

Miscellaneous databases

EvolutionaryTraceiP29957.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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.
ProtoNetiSearch...

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 2, 2016
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.