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Protein

Alpha-amylase type A isozyme

Gene

AMY1.1

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

Functioni

Alpha-amylase displaying a robust amylolytic activity toward p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin (PubMed:24089528).1 Publication

Miscellaneous

There are at least 4 types of alpha-amylase in barley.
Mutagenesis experiments indicate that His-117 and His-314 participate in transition state stabilization but not directly in catalysis.
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.4 Publications

Cofactori

Ca2+4 PublicationsNote: Binds 3 Ca2+ ions per subunit.4 Publications

Activity regulationi

Redox-insensitive.1 Publication

pH dependencei

Optimum pH is 5.5 with p-nitrophenyl maltoheptaoside or amylopectin as substrate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi116Calcium 14 Publications1
Metal bindingi133Calcium 24 Publications1
Metal bindingi136Calcium 2; via carbonyl oxygen4 Publications1
Metal bindingi138Calcium 2; via carbonyl oxygen4 Publications1
Metal bindingi142Calcium 24 Publications1
Metal bindingi152Calcium 34 Publications1
Metal bindingi163Calcium 14 Publications1
Metal bindingi166Calcium 1; via carbonyl oxygen4 Publications1
Metal bindingi167Calcium 34 Publications1
Metal bindingi168Calcium 3; via carbonyl oxygen4 Publications1
Metal bindingi171Calcium 3; via carbonyl oxygen4 Publications1
Metal bindingi173Calcium 14 Publications1
Metal bindingi173Calcium 34 Publications1
Active sitei204Nucleophile2 Publications1
Metal bindingi208Calcium 1; via carbonyl oxygen4 Publications1
Active sitei229Proton donor1 Publication1
Binding sitei231Substrate1 Publication1
Binding sitei233Substrate1 Publication1
Binding sitei251Substrate2 Publications1
Binding sitei258Substrate2 Publications1
Binding sitei295Substrate1 Publication1
Binding sitei314Substrate1 Publication1
Sitei315Transition state stabilizer1 Publication1
Binding sitei320Substrate1 Publication1
Binding sitei399Substrate2 Publications1
Binding sitei426Substrate1 Publication1

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 A isozyme (EC:3.2.1.14 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
HvAMY1
Low pI alpha-amylase
Gene namesi
Name:AMY1.1
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117H → N: 20-fold decrease in activity. 1 Publication1
Mutagenesisi129Y → A: Reduces affinity for starch granules 3-fold. 1 Publication1
Mutagenesisi204D → A or N: Loss of activity. 2 Publications1
Mutagenesisi229E → Q: Loss of activity. 1 Publication1
Mutagenesisi302W → A: Over 10-fold decrease in affinity for starch granules. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-303 and A-404. 1 Publication1
Mutagenesisi303W → A: Over 10-fold decrease in affinity for starch granules. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-302 and A-404. 2 Publications1
Mutagenesisi314H → N: 10-fold decrease in activity. 1 Publication1
Mutagenesisi315D → N: Loss of activity. 1 Publication1
Mutagenesisi404Y → A: Reduces affinity for starch granules 9-fold and reduces activity by 90%. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-302 and A-303. 3 Publications1
Mutagenesisi404Y → M: Abolishes binding to cyclodextrin-Sepharose and strongly reduces enzyme activity. 3 Publications1
Mutagenesisi419H → A: Slightly decreased catalytic activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3616349

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
ChainiPRO_000000140425 – 438Alpha-amylase type A isozymeAdd BLAST414

Proteomic databases

PRIDEiP00693

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.

Gene expression databases

ExpressionAtlasiP00693 baseline and differential

Interactioni

Subunit structurei

Monomer.2 Publications

Chemistry databases

BindingDBiP00693

Structurei

Secondary structure

1438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP00693
SMRiP00693
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00693

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 71Substrate binding1 Publication3
Regioni76 – 77Substrate binding1 Publication2
Regioni202 – 207Substrate binding1 Publication6
Regioni301 – 303Substrate binding2 Publications3
Regioni404 – 406Substrate binding4 Publications3
Regioni416 – 422Substrate binding2 Publications7

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0471 Eukaryota
COG0366 LUCA

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.

P00693-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKNGSLCCF SLLLLLLLAG LASGHQVLFQ GFNWESWKQS GGWYNMMMGK
60 70 80 90 100
VDDIAAAGVT HVWLPPPSHS VSNEGYMPGR LYDIDASKYG NAAELKSLIG
110 120 130 140 150
ALHGKGVQAI ADIVINHRCA DYKDSRGIYC IFEGGTSDGR LDWGPHMICR
160 170 180 190 200
DDTKYSDGTA NLDTGADFAA APDIDHLNDR VQRELKEWLL WLKSDLGFDA
210 220 230 240 250
WRLDFARGYS PEMAKVYIDG TSPSLAVAEV WDNMATGGDG KPNYDQDAHR
260 270 280 290 300
QNLVNWVDKV GGAASAGMVF DFTTKGILNA AVEGELWRLI DPQGKAPGVM
310 320 330 340 350
GWWPAKAATF VDNHDTGSTQ AMWPFPSDKV MQGYAYILTH PGIPCIFYDH
360 370 380 390 400
FFNWGFKDQI AALVAIRKRN GITATSALKI LMHEGDAYVA EIDGKVVVKI
410 420 430
GSRYDVGAVI PAGFVTSAHG NDYAVWEKNG AAATLQRS
Length:438
Mass (Da):47,796
Last modified:July 21, 1986 - v1
Checksum:i2393FDAC51E80F51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01236 mRNA Translation: AAA32929.1
PIRiA00846 ALBH
UniGeneiHv.68

Similar proteinsi

Entry informationi

Entry nameiAMY1_HORVU
AccessioniPrimary (citable) accession number: P00693
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 12, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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