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Protein

Beta-amylase 3, chloroplastic

Gene

BAM3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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

  • amylopectin maltohydrolase activity Source: UniProtKB-EC
  • beta-amylase activity Source: TAIR

GO - Biological processi

  • maltose biosynthetic process Source: TAIR
  • response to cold Source: TAIR
  • starch catabolic process Source: TAIR

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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

AraportiAT4G17090
TAIRilocus:2130504 AT4G17090

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

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

ExpressionAtlasiO23553 baseline and differential
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
OMAiDNWRQFV
OrthoDBiEOG093605C7
PhylomeDBiO23553

Family and domain databases

InterProiView protein in InterPro
IPR001554 Glyco_hydro_14
IPR018238 Glyco_hydro_14_CS
IPR001371 Glyco_hydro_14B_pln
IPR017853 Glycoside_hydrolase_SF
PANTHERiPTHR31352 PTHR31352, 1 hit
PfamiView protein in Pfam
PF01373 Glyco_hydro_14, 1 hit
PRINTSiPR00750 BETAAMYLASE
PR00842 GLHYDLASE14B
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00506 BETA_AMYLASE_1, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiBAM3_ARATH
AccessioniPrimary (citable) accession number: O23553
Secondary accession number(s): Q941A5, Q9SMW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: April 25, 2018
This is version 111 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

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

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