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Protein

Alpha-amylase type B isozyme

Gene

AMY1.2

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Cofactori

Ca2+3 PublicationsNote: Binds 3 Ca2+ ions per subunit.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115Calcium 1Combined sources3 Publications1
Metal bindingi132Calcium 2Combined sources3 Publications1
Metal bindingi135Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi137Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi141Calcium 2Combined sources3 Publications1
Metal bindingi151Calcium 3Combined sources3 Publications1
Metal bindingi162Calcium 1Combined sources3 Publications1
Metal bindingi165Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi166Calcium 3Combined sources3 Publications1
Metal bindingi167Calcium 3; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi170Calcium 3; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi172Calcium 1Combined sources3 Publications1
Metal bindingi172Calcium 3Combined sources3 Publications1
Active sitei203Nucleophile1 Publication1
Metal bindingi207Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Active sitei228Proton donor1 Publication1
Binding sitei230Substrate1 Publication1
Binding sitei232Substrate1 Publication1
Binding sitei250Substrate1 Publication1
Binding sitei257Substrate1 Publication1
Binding sitei293SubstrateBy similarity1
Binding sitei312Substrate1 Publication1
Sitei313Transition state stabilizer1 Publication1
Binding sitei318SubstrateBy similarity1
Binding sitei397SubstrateBy similarity1
Binding sitei424SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Germination

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 2687.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase type B isozyme (EC:3.2.1.1By similarity)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
AMY2-2
High pI alpha-amylase
Gene namesi
Name:AMY1.2
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000000140525 – 427Alpha-amylase type B isozymeAdd BLAST403

Proteomic databases

PRIDEiP04063.

Expressioni

Developmental stagei

Production of alpha-amylase is hormonally regulated. Germinating embryos produce the hormone gibberellic acid, which within 10 hours stimulates the aleurone cells covering the endosperm of the seed to produce alpha-amylase. The enzyme then degrades the starch within the endosperm for use by the developing plant embryo.

Inductioni

Type B isozyme mRNA is undetectable in unstimulated cells and increases a hundred-fold after stimulation with gibberellic acid.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

DIPiDIP-6097N.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 29Combined sources3
Helixi35 – 37Combined sources3
Helixi42 – 47Combined sources6
Helixi50 – 56Combined sources7
Beta strandi60 – 63Combined sources4
Beta strandi69 – 71Combined sources3
Beta strandi74 – 77Combined sources4
Helixi83 – 85Combined sources3
Helixi91 – 104Combined sources14
Beta strandi107 – 112Combined sources6
Beta strandi120 – 122Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi134 – 138Combined sources5
Helixi144 – 146Combined sources3
Turni152 – 154Combined sources3
Beta strandi163 – 165Combined sources3
Beta strandi168 – 170Combined sources3
Helixi178 – 193Combined sources16
Beta strandi199 – 202Combined sources4
Helixi205 – 207Combined sources3
Helixi210 – 220Combined sources11
Beta strandi223 – 227Combined sources5
Beta strandi239 – 241Combined sources3
Helixi246 – 260Combined sources15
Beta strandi263 – 268Combined sources6
Helixi270 – 279Combined sources10
Turni280 – 282Combined sources3
Helixi284 – 287Combined sources4
Helixi297 – 299Combined sources3
Helixi302 – 304Combined sources3
Beta strandi305 – 309Combined sources5
Turni312 – 314Combined sources3
Turni316 – 318Combined sources3
Helixi325 – 327Combined sources3
Helixi328 – 337Combined sources10
Beta strandi338 – 345Combined sources8
Helixi346 – 350Combined sources5
Helixi355 – 367Combined sources13
Beta strandi376 – 382Combined sources7
Beta strandi385 – 390Combined sources6
Turni391 – 393Combined sources3
Beta strandi394 – 400Combined sources7
Helixi405 – 407Combined sources3
Beta strandi410 – 418Combined sources9
Beta strandi421 – 426Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMYX-ray2.80A25-427[»]
1AVAX-ray1.90A/B25-427[»]
1BG9X-ray2.80A25-427[»]
ProteinModelPortaliP04063.
SMRiP04063.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04063.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni75 – 76Substrate binding1 Publication2
Regioni201 – 206Substrate binding1 Publication6
Regioni299 – 301Substrate binding1 Publication3
Regioni414 – 420Substrate bindingBy similarity7

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.
InterProiIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
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.
PfamiPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFiPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P04063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANKHLSLSL FLVLLGLSAS LASGQVLFQG FNWESWKHNG GWYNFLMGKV
60 70 80 90 100
DDIAAAGITH VWLPPASQSV AEQGYMPGRL YDLDASKYGN KAQLKSLIGA
110 120 130 140 150
LHGKGVKAIA DIVINHRTAE HKDGRGIYCI FEGGTPDARL DWGPHMICRD
160 170 180 190 200
DRPYADGTGN PDTGADFGAA PDIDHLNLRV QKELVEWLNW LKADIGFDGW
210 220 230 240 250
RFDFAKGYSA DVAKIYIDRS EPSFAVAEIW TSLAYGGDGK PNLNQDQHRQ
260 270 280 290 300
ELVNWVDKVG GKGPATTFDF TTKGILNVAV EGELWRLRGT DGKAPGMIGW
310 320 330 340 350
WPAKAVTFVD NHDTGSTQHM WPFPSDRVMQ GYAYILTHPG TPCIFYDHFF
360 370 380 390 400
DWGLKEEIDR LVSVRTRHGI HNESKLQIIE ADADLYLAEI DGKVIVKLGP
410 420
RYDVGNLIPG GFKVAAHGND YAVWEKI
Length:427
Mass (Da):47,356
Last modified:July 15, 1998 - v3
Checksum:i957C0B16621BF748
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti134G → D in CAA33298 (Ref. 1) Curated1
Sequence conflicti425E → Q in CAA33298 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15226 Genomic DNA. Translation: CAA33298.1.
K02637 Genomic DNA. Translation: AAA98790.1.
PIRiA31960. ALBHB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15226 Genomic DNA. Translation: CAA33298.1.
K02637 Genomic DNA. Translation: AAA98790.1.
PIRiA31960. ALBHB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMYX-ray2.80A25-427[»]
1AVAX-ray1.90A/B25-427[»]
1BG9X-ray2.80A25-427[»]
ProteinModelPortaliP04063.
SMRiP04063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6097N.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP04063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.1. 2687.

Miscellaneous databases

EvolutionaryTraceiP04063.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
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.
PfamiPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFiPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMY2_HORVU
AccessioniPrimary (citable) accession number: P04063
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

There are at least 4 types of alpha-amylase in barley.
Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity.

Keywords - Technical termi

3D-structure

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.