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Protein

Beta-amylase 3, chloroplastic

Gene

BAM3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.6 Publications

Catalytic activityi

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

Enzyme regulationi

Redox regulation; active in reducing conditions, inactive in oxidizing conditions.By similarity

pH dependencei

Optimum pH is 6-7.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei127SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Binding sitei175SubstrateBy similarity1
Active sitei259Proton donorBy similarity1
Binding sitei371SubstrateBy similarity1
Binding sitei376SubstrateBy similarity1
Binding sitei418SubstrateBy similarity1
Active sitei456Proton acceptorBy similarity1
Binding sitei489SubstrateBy similarity1

GO - Molecular functioni

  • beta-amylase activity Source: TAIR

GO - Biological processi

  • maltose biosynthetic process Source: TAIR
  • response to cold Source: TAIR
  • starch catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyciARA:AT4G17090-MONOMER.
MetaCyc:AT4G17090-MONOMER.
BRENDAi3.2.1.2. 399.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-amylase 3, chloroplastic (EC:3.2.1.2)
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Beta-amylase 8
Chloroplast beta-amylase
Short name:
CT-BMY
Gene namesi
Name:BAM3
Synonyms:BMY8, CTBMY
Ordered Locus Names:At4g17090
ORF Names:dl4575c, FCAALL.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G17090.

Subcellular locationi

GO - Cellular componenti

  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Slightly retarded growth rate and reduced starch breakdown in leaves during the night.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 49ChloroplastSequence analysisAdd BLAST49
ChainiPRO_000039341850 – 548Beta-amylase 3, chloroplasticAdd BLAST499

Proteomic databases

PaxDbiO23553.
PRIDEiO23553.

PTM databases

iPTMnetiO23553.

Expressioni

Tissue specificityi

Expressed in vascular tissue of cotyledons, leaves, petioles, stems, petals, siliques and roots, particularly in phloem, as well as in photosynthetic tissues.1 Publication

Inductioni

By cold stress. Light-mediated circadian regulation; highest levels at dawn and at dusk in long days (LD) but only at dusk in short days (SD). Repressed by trehalose in a ABI4-dependent manner, this effect is reversed in the presence of sucrose.3 Publications

Gene expression databases

GenevisibleiO23553. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G17090.1.

Structurei

3D structure databases

ProteinModelPortaliO23553.
SMRiO23553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni457 – 458Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IE4H. Eukaryota.
ENOG410XRH5. LUCA.
HOGENOMiHOG000238755.
KOiK01177.
OMAiEMKFTHE.
OrthoDBiEOG093605C7.
PhylomeDBiO23553.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O23553-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELTLNSSSS LIKRKDAKSS RNQESSSNNM TFAKMKPPTY QFQAKNSVKE
60 70 80 90 100
MKFTHEKTFT PEGETLEKWE KLHVLSYPHS KNDASVPVFV MLPLDTVTMS
110 120 130 140 150
GHLNKPRAMN ASLMALKGAG VEGVMVDAWW GLVEKDGPMN YNWEGYAELI
160 170 180 190 200
QMVQKHGLKL QVVMSFHQCG GNVGDSCSIP LPPWVLEEIS KNPDLVYTDK
210 220 230 240 250
SGRRNPEYIS LGCDSVPVLR GRTPIQVYSD FMRSFRERFE GYIGGVIAEI
260 270 280 290 300
QVGMGPCGEL RYPSYPESNG TWRFPGIGEF QCYDKYMKSS LQAYAESIGK
310 320 330 340 350
TNWGTSGPHD AGEYKNLPED TEFFRRDGTW NSEYGKFFME WYSGKLLEHG
360 370 380 390 400
DQLLSSAKGI FQGSGAKLSG KVAGIHWHYN TRSHAAELTA GYYNTRNHDG
410 420 430 440 450
YLPIAKMFNK HGVVLNFTCM EMKDGEQPEH ANCSPEGLVK QVQNATRQAG
460 470 480 490 500
TELAGENALE RYDSSAFGQV VATNRSDSGN GLTAFTYLRM NKRLFEGQNW
510 520 530 540
QQLVEFVKNM KEGGHGRRLS KEDTTGSDLY VGFVKGKIAE NVEEAALV
Length:548
Mass (Da):61,353
Last modified:April 20, 2010 - v3
Checksum:iA5794EDC8427FE30
GO

Sequence cautioni

The sequence AAK96508 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.Curated
The sequence AAL31225 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.Curated
The sequence CAB46051 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB80980 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250341 mRNA. Translation: CAB58423.1.
Z97342 Genomic DNA. Translation: CAB46051.1. Different initiation.
AL161545 Genomic DNA. Translation: CAB80980.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83848.1.
AY052315 mRNA. Translation: AAK96508.1. Sequence problems.
AY061898 mRNA. Translation: AAL31225.1. Sequence problems.
AY087592 mRNA. Translation: AAM65134.1.
PIRiD71439.
H85190.
T52556.
RefSeqiNP_567523.1. NM_117813.3.
UniGeneiAt.22021.
At.23528.
At.47944.
At.67939.

Genome annotation databases

EnsemblPlantsiAT4G17090.1; AT4G17090.1; AT4G17090.
GeneIDi827419.
GrameneiAT4G17090.1; AT4G17090.1; AT4G17090.
KEGGiath:AT4G17090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250341 mRNA. Translation: CAB58423.1.
Z97342 Genomic DNA. Translation: CAB46051.1. Different initiation.
AL161545 Genomic DNA. Translation: CAB80980.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83848.1.
AY052315 mRNA. Translation: AAK96508.1. Sequence problems.
AY061898 mRNA. Translation: AAL31225.1. Sequence problems.
AY087592 mRNA. Translation: AAM65134.1.
PIRiD71439.
H85190.
T52556.
RefSeqiNP_567523.1. NM_117813.3.
UniGeneiAt.22021.
At.23528.
At.47944.
At.67939.

3D structure databases

ProteinModelPortaliO23553.
SMRiO23553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G17090.1.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

PTM databases

iPTMnetiO23553.

Proteomic databases

PaxDbiO23553.
PRIDEiO23553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G17090.1; AT4G17090.1; AT4G17090.
GeneIDi827419.
GrameneiAT4G17090.1; AT4G17090.1; AT4G17090.
KEGGiath:AT4G17090.

Organism-specific databases

TAIRiAT4G17090.

Phylogenomic databases

eggNOGiENOG410IE4H. Eukaryota.
ENOG410XRH5. LUCA.
HOGENOMiHOG000238755.
KOiK01177.
OMAiEMKFTHE.
OrthoDBiEOG093605C7.
PhylomeDBiO23553.

Enzyme and pathway databases

BioCyciARA:AT4G17090-MONOMER.
MetaCyc:AT4G17090-MONOMER.
BRENDAi3.2.1.2. 399.

Miscellaneous databases

PROiO23553.

Gene expression databases

GenevisibleiO23553. AT.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAM3_ARATH
AccessioniPrimary (citable) accession number: O23553
Secondary accession number(s): Q941A5, Q9SMW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: November 30, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.