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Protein

Alpha-amylase type A isozyme

Gene

AMY1.1

Organism
Hordeum vulgare (Barley)
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.3 Publications

Cofactori

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

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

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 A isozyme (EC:3.2.1.13 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
AMY1
Low pI alpha-amylase
Gene namesi
Name:AMY1.1
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

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.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi4513.MLOC_55142.1.

Structurei

Secondary structure

1438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Helixi36 – 38Combined sources3
Helixi43 – 48Combined sources6
Helixi51 – 56Combined sources6
Beta strandi61 – 64Combined sources4
Beta strandi70 – 72Combined sources3
Beta strandi75 – 78Combined sources4
Helixi84 – 86Combined sources3
Helixi92 – 104Combined sources13
Beta strandi108 – 113Combined sources6
Beta strandi121 – 123Combined sources3
Beta strandi129 – 131Combined sources3
Beta strandi135 – 139Combined sources5
Helixi145 – 147Combined sources3
Turni153 – 155Combined sources3
Helixi179 – 194Combined sources16
Beta strandi200 – 203Combined sources4
Helixi206 – 208Combined sources3
Helixi211 – 221Combined sources11
Beta strandi226 – 228Combined sources3
Beta strandi240 – 242Combined sources3
Helixi247 – 260Combined sources14
Helixi262 – 264Combined sources3
Beta strandi265 – 270Combined sources6
Helixi272 – 281Combined sources10
Turni282 – 284Combined sources3
Helixi286 – 289Combined sources4
Helixi299 – 302Combined sources4
Helixi304 – 306Combined sources3
Beta strandi307 – 311Combined sources5
Turni314 – 316Combined sources3
Turni318 – 320Combined sources3
Helixi327 – 329Combined sources3
Helixi330 – 339Combined sources10
Beta strandi340 – 347Combined sources8
Helixi348 – 352Combined sources5
Beta strandi353 – 355Combined sources3
Helixi357 – 369Combined sources13
Beta strandi378 – 384Combined sources7
Beta strandi387 – 392Combined sources6
Turni393 – 395Combined sources3
Beta strandi396 – 402Combined sources7
Helixi407 – 409Combined sources3
Beta strandi415 – 420Combined sources6
Beta strandi423 – 427Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HT6X-ray1.50A25-429[»]
1P6WX-ray2.00A25-429[»]
1RP8X-ray2.00A25-429[»]
1RP9X-ray2.00A25-429[»]
1RPKX-ray2.00A25-429[»]
2QPSX-ray2.20A25-429[»]
2QPUX-ray1.70A/B/C25-429[»]
3BSGX-ray1.95A25-438[»]
3BSHX-ray3.00A25-438[»]
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.
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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HT6X-ray1.50A25-429[»]
1P6WX-ray2.00A25-429[»]
1RP8X-ray2.00A25-429[»]
1RP9X-ray2.00A25-429[»]
1RPKX-ray2.00A25-429[»]
2QPSX-ray2.20A25-429[»]
2QPUX-ray1.70A/B/C25-429[»]
3BSGX-ray1.95A25-438[»]
3BSHX-ray3.00A25-438[»]
ProteinModelPortaliP00693.
SMRiP00693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4513.MLOC_55142.1.

Chemistry databases

ChEMBLiCHEMBL3616349.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.1. 2687.

Miscellaneous databases

EvolutionaryTraceiP00693.

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 nameiAMY1_HORVU
AccessioniPrimary (citable) accession number: P00693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 129 of the entry and version 1 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.
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.

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.