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Protein

Alpha-amylase

Gene
N/A
Organism
Pecten maximus (King scallop) (Pilgrim's clam)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161CalciumBy similarity
Metal bindingi173 – 1731Calcium; via carbonyl oxygenBy similarity
Metal bindingi182 – 1821CalciumBy similarity
Binding sitei210 – 2101ChlorideBy similarity
Active sitei212 – 2121NucleophileBy similarity
Metal bindingi216 – 2161Calcium; via carbonyl oxygenBy similarity
Active sitei248 – 2481Proton donorBy similarity
Binding sitei311 – 3111ChlorideBy similarity
Sitei313 – 3131Transition state stabilizerBy similarity
Binding sitei349 – 3491ChlorideBy similarity

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

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1By similarity)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiPecten maximus (King scallop) (Pilgrim's clam)
Taxonomic identifieri6579 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPectinoidaPectinoideaPectinidaePecten

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 508489Alpha-amylasePRO_0000001396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 102By similarity
Disulfide bondi156 ↔ 175By similarity
Disulfide bondi383 ↔ 389By similarity
Disulfide bondi455 ↔ 467By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP91778.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP91778.
SMRiP91778. Positions 22-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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/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.

P91778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSLIIAACC VTVALAGTFS NPTCAPGRNT IVHLFEWKWT DIAKECERFL
60 70 80 90 100
GPNGFCGVQI SPPNENRLVN NRPWWERYQP VSYKLQTRSG SEDQLRDMIS
110 120 130 140 150
RCNRVNVRIY SDTVINHMTG VGGSGTGTAG SHWNGDTLSY PGVPFSAWDF
160 170 180 190 200
NTGNECHSSD MNIHDYNNAE EIRNCRLVSL ADLKLSKNYV REEITQYMNH
210 220 230 240 250
LIDLGVAGFR IDAAKHMWPG DLRAMFGTLH DLNSAVFGSG RKPFIFQEVI
260 270 280 290 300
DMGGEPISAS EYTGIGRVTN FIFGVKLGQV FRNENKASNL HNWGEAWGMP
310 320 330 340 350
NSNDVVVFID NHDNQRGHGG GGGPLTHFEP RPYKLATAFM LAHPYGFTRL
360 370 380 390 400
MSSYNFDRSN TDQGPPHNGD NINDVTINAD LTCGNGWTCE HRWREIYNMV
410 420 430 440 450
AFRNIVMGQN LQHWWDNGNY QIAFGRGNKG FIAMNMDNHN LDQTLQTGLP
460 470 480 490 500
AGTYCDVISG SYDGSSCSGT EIQVGNDGNA HFSISNSSDD PMIAIHVGAK

KGQPKVTT
Length:508
Mass (Da):56,354
Last modified:May 1, 1997 - v1
Checksum:i8824405C3949B465
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99729 mRNA. Translation: CAA68065.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99729 mRNA. Translation: CAA68065.1.

3D structure databases

ProteinModelPortaliP91778.
SMRiP91778. Positions 22-500.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP91778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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...

Publicationsi

  1. "Amylase on Pecten maximus (Mollusca, bivalves): protein and cDNA characterization; quantification of the expression in the digestive gland."
    Le Moine S., Sellos D., Moal J., Daniel J.Y., San Juan Serrano F., Samain J.F., Van Wormhoudt A.
    Mol. Mar. Biol. Biotechnol. 6:228-237(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Digestive gland.

Entry informationi

Entry nameiAMY_PECMA
AccessioniPrimary (citable) accession number: P91778
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.