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Protein

Alpha-amylase

Gene

AMY1.1

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for breakdown of endosperm starch during germination.

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+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi122Calcium 1By similarity1
Metal bindingi139Calcium 2By similarity1
Metal bindingi142Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi144Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi148Calcium 2By similarity1
Metal bindingi158Calcium 3By similarity1
Metal bindingi168Calcium 1By similarity1
Metal bindingi171Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi172Calcium 3By similarity1
Metal bindingi173Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi176Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 1By similarity1
Metal bindingi178Calcium 3By similarity1
Active sitei209NucleophileBy similarity1
Metal bindingi213Calcium 1; via carbonyl oxygenBy similarity1
Active sitei234Proton donorBy similarity1
Binding sitei236SubstrateBy similarity1
Binding sitei238SubstrateBy similarity1
Binding sitei256SubstrateBy similarity1
Binding sitei263SubstrateBy similarity1
Binding sitei300SubstrateBy similarity1
Binding sitei319SubstrateBy similarity1
Sitei320Transition state stabilizerBy similarity1
Binding sitei325SubstrateBy similarity1
Binding sitei404SubstrateBy similarity1
Binding sitei431SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • starch catabolic process Source: Gramene
  • sucrose catabolic process Source: Gramene
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 4460.

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
Alpha-amylase isozyme 1B
Gene namesi
Name:AMY1.1
Synonyms:AMY1A
Ordered Locus Names:Os02g0765600, LOC_Os02g52710
ORF Names:OJ1004_A11.13, P0539D10.32
OrganismiOryza sativa subsp. japonica (Rice)
Taxonomic identifieri39947 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
Proteomesi
  • UP000059680 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31CuratedAdd BLAST31
ChainiPRO_000000140832 – 434Alpha-amylaseAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi271N-linked (GlcNAc...)Curated1

Post-translational modificationi

Only cereal amylase known to be glycosylated.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP17654.
PRIDEiP17654.

Expressioni

Tissue specificityi

More abundant in germinating seeds, than in callus, young roots and leaves.

Developmental stagei

Expressed at a high level during germination in the aleurones cells under the control of the plant hormone gibberellic acid and in the developing grains at a low level.

Gene expression databases

ExpressionAtlasiP17654. baseline and differential.
GenevisibleiP17654. OS.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi39947.LOC_Os02g52710.1.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Helixi42 – 44Combined sources3
Helixi49 – 54Combined sources6
Helixi57 – 62Combined sources6
Beta strandi67 – 70Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi81 – 84Combined sources4
Helixi90 – 92Combined sources3
Helixi98 – 110Combined sources13
Beta strandi114 – 119Combined sources6
Beta strandi127 – 129Combined sources3
Beta strandi135 – 137Combined sources3
Beta strandi141 – 145Combined sources5
Helixi151 – 153Combined sources3
Helixi184 – 199Combined sources16
Beta strandi205 – 208Combined sources4
Helixi211 – 213Combined sources3
Helixi216 – 226Combined sources11
Beta strandi231 – 233Combined sources3
Beta strandi245 – 247Combined sources3
Helixi252 – 264Combined sources13
Helixi267 – 269Combined sources3
Beta strandi272 – 275Combined sources4
Helixi277 – 286Combined sources10
Turni287 – 289Combined sources3
Helixi291 – 294Combined sources4
Helixi304 – 306Combined sources3
Helixi309 – 311Combined sources3
Turni319 – 321Combined sources3
Turni323 – 325Combined sources3
Helixi332 – 334Combined sources3
Helixi335 – 344Combined sources10
Beta strandi345 – 347Combined sources3
Beta strandi350 – 352Combined sources3
Helixi353 – 357Combined sources5
Helixi362 – 374Combined sources13
Beta strandi383 – 389Combined sources7
Beta strandi392 – 397Combined sources6
Turni398 – 400Combined sources3
Beta strandi401 – 407Combined sources7
Helixi412 – 414Combined sources3
Beta strandi419 – 425Combined sources7
Beta strandi428 – 433Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WN6X-ray2.16A/B/C/D31-434[»]
ProteinModelPortaliP17654.
SMRiP17654.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni75 – 77Substrate bindingBy similarity3
Regioni82 – 83Substrate bindingBy similarity2
Regioni207 – 212Substrate bindingBy similarity6
Regioni306 – 308Substrate bindingBy similarity3
Regioni409 – 411Substrate bindingBy similarity3
Regioni421 – 427Substrate bindingBy similarity7

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.
HOGENOMiHOG000239525.
InParanoidiP17654.
KOiK01176.
OMAiGEQGYMP.
OrthoDBiEOG093600FS.

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.

P17654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVLNTMVNK HFLSLSVLIV LLGLSSNLTA GQVLFQGFNW ESWKENGGWY
60 70 80 90 100
NFLMGKVDDI AAAGITHVWL PPPSHSVGEQ GYMPGRLYDL DASKYGNEAQ
110 120 130 140 150
LKSLIEAFHG KGVQVIADIV INHRTAEHKD GRGIYCLFEG GTPDSRLDWG
160 170 180 190 200
PHMICRDDPY GDGTGNPDTG ADFAAAPDID HLNKRVQREL IGWLDWLKMD
210 220 230 240 250
IGFDAWRLDF AKGYSADMAK IYIDATEPSF AVAEIWTSMA NGGDGKPNYD
260 270 280 290 300
QNAHRQELVN WVDRVGGANS NATAFDFTTK GILNVAVEGE LWRLRGEDGK
310 320 330 340 350
APGMIGWWPA KATTFVDNHD TGSTQHLWPF PSDKVMQGYA YILTHPGNPC
360 370 380 390 400
IFYDHFFDWG LKEEIERLVS IRNRQGIHPA SELRIMEADS DLYLAEIDGK
410 420 430
VITKIGPRYD VEHLIPEGFQ VVAHGDGYAI WEKI
Length:434
Mass (Da):48,457
Last modified:October 25, 2005 - v2
Checksum:i7B23B299A0AD3E37
GO

Sequence cautioni

The sequence CAA34516 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti272A → G in AAA33885 (PubMed:2370848).Curated1
Sequence conflicti272A → G in CAA34516 (PubMed:2102847).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24286 mRNA. Translation: AAA33885.1.
X16509 Genomic DNA. Translation: CAA34516.1. Different initiation.
AP004817 Genomic DNA. Translation: BAD17125.1.
AP005287 Genomic DNA. Translation: BAD17313.1.
AP014958 Genomic DNA. Translation: BAS81060.1.
PIRiS10013.
S12775.
RefSeqiXP_015622769.1. XM_015767283.1.
UniGeneiOs.49249.

Genome annotation databases

EnsemblPlantsiOS02T0765600-01; OS02T0765600-01; OS02G0765600.
GeneIDi4330832.
GrameneiOS02T0765600-01; OS02T0765600-01; OS02G0765600.
KEGGiosa:4330832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24286 mRNA. Translation: AAA33885.1.
X16509 Genomic DNA. Translation: CAA34516.1. Different initiation.
AP004817 Genomic DNA. Translation: BAD17125.1.
AP005287 Genomic DNA. Translation: BAD17313.1.
AP014958 Genomic DNA. Translation: BAS81060.1.
PIRiS10013.
S12775.
RefSeqiXP_015622769.1. XM_015767283.1.
UniGeneiOs.49249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WN6X-ray2.16A/B/C/D31-434[»]
ProteinModelPortaliP17654.
SMRiP17654.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os02g52710.1.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP17654.
PRIDEiP17654.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOS02T0765600-01; OS02T0765600-01; OS02G0765600.
GeneIDi4330832.
GrameneiOS02T0765600-01; OS02T0765600-01; OS02G0765600.
KEGGiosa:4330832.

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.
HOGENOMiHOG000239525.
InParanoidiP17654.
KOiK01176.
OMAiGEQGYMP.
OrthoDBiEOG093600FS.

Enzyme and pathway databases

BRENDAi3.2.1.1. 4460.

Gene expression databases

ExpressionAtlasiP17654. baseline and differential.
GenevisibleiP17654. OS.

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_ORYSJ
AccessioniPrimary (citable) accession number: P17654
Secondary accession number(s): Q6Z317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  4. 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.