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Protein

Alpha-amylase type B isozyme

Gene

AMY1.2

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Germination
LigandCalcium, 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.

Gene expression databases

ExpressionAtlasiP04063 baseline

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

DIPiDIP-6097N
IntActiP04063, 1 interactor

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
InterProiView protein in InterPro
IPR012850 A-amylase_bs_C
IPR013775 A-amylase_pln
IPR006046 Alpha_amylase
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF07821 Alpha-amyl_C2, 1 hit
PF00128 Alpha-amylase, 1 hit
PIRSFiPIRSF001028 Alph-amls_plant, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00810 Alpha-amyl_C2, 1 hit
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

Similar proteinsi

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
IntActiP04063, 1 interactor

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

Gene expression databases

ExpressionAtlasiP04063 baseline

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR012850 A-amylase_bs_C
IPR013775 A-amylase_pln
IPR006046 Alpha_amylase
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF07821 Alpha-amyl_C2, 1 hit
PF00128 Alpha-amylase, 1 hit
PIRSFiPIRSF001028 Alph-amls_plant, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00810 Alpha-amyl_C2, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAMY2_HORVU
AccessioniPrimary (citable) accession number: P04063
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: July 15, 1998
Last modified: May 23, 2018
This is version 126 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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