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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Binding sitei175 – 1751SubstrateBy similarity
Active sitei259 – 2591Proton donorBy similarity
Binding sitei371 – 3711SubstrateBy similarity
Binding sitei376 – 3761SubstrateBy similarity
Binding sitei418 – 4181SubstrateBy similarity
Active sitei456 – 4561Proton acceptorBy similarity
Binding sitei489 – 4891SubstrateBy similarity

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
ProteomesiUP000006548 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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949ChloroplastSequence AnalysisAdd
BLAST
Chaini50 – 548499Beta-amylase 3, chloroplasticPRO_0000393418Add
BLAST

Proteomic databases

PaxDbiO23553.
PRIDEiO23553.

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

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G17090.1.

Structurei

3D structure databases

ProteinModelPortaliO23553.
SMRiO23553. Positions 86-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni457 – 4582Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG77898.
HOGENOMiHOG000238755.
KOiK01177.
OMAiRYDWEGY.
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 AAK96508.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.Curated
The sequence AAL31225.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.Curated
The sequence CAB46051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB80980.1 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_117813.2.
UniGeneiAt.22021.
At.23528.
At.47944.
At.67939.

Genome annotation databases

EnsemblPlantsiAT4G17090.1; AT4G17090.1; AT4G17090.
GeneIDi827419.
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_117813.2.
UniGeneiAt.22021.
At.23528.
At.47944.
At.67939.

3D structure databases

ProteinModelPortaliO23553.
SMRiO23553. Positions 86-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G17090.1.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PaxDbiO23553.
PRIDEiO23553.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT4G17090.

Phylogenomic databases

eggNOGiNOG77898.
HOGENOMiHOG000238755.
KOiK01177.
OMAiRYDWEGY.
PhylomeDBiO23553.

Enzyme and pathway databases

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

Miscellaneous databases

PROiO23553.

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...

Publicationsi

« Hide 'large scale' publications
  1. "An Arabidopsis gene encoding a chloroplast-targeted beta-amylase."
    Lao N.T., Schoneveld O., Mould R.M., Hibberd J.M., Gray J.C., Kavanagh T.A.
    Plant J. 20:519-527(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "RNA interference of Arabidopsis beta-amylase8 prevents maltose accumulation upon cold shock and increases sensitivity of PSII photochemical efficiency to freezing stress."
    Kaplan F., Guy C.L.
    Plant J. 44:730-743(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY COLD.
  8. "Daylength and circadian effects on starch degradation and maltose metabolism."
    Lu Y., Gehan J.P., Sharkey T.D.
    Plant Physiol. 138:2280-2291(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY CIRCADIAN DAYLENGTH.
  9. "Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis."
    Sparla F., Costa A., Lo Schiavo F., Pupillo P., Trost P.
    Plant Physiol. 141:840-850(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "ABI4 mediates the effects of exogenous trehalose on Arabidopsis growth and starch breakdown."
    Ramon M., Rolland F., Thevelein J.M., van Dijck P., Leyman B.
    Plant Mol. Biol. 63:195-206(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TREHALOSE.
  11. "Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases."
    Edner C., Li J., Albrecht T., Mahlow S., Hejazi M., Hussain H., Kaplan F., Guy C., Smith S.M., Steup M., Ritte G.
    Plant Physiol. 145:17-28(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts."
    Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P., Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K., Smith A.M., Smith S.M., Zeeman S.C.
    Plant Cell 20:1040-1058(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, GENE FAMILY, NOMENCLATURE.
  13. "Catalytically-inactive beta-amylase BAM4 required for starch breakdown in Arabidopsis leaves is a starch-binding-protein."
    Li J., Francisco P., Zhou W., Edner C., Steup M., Ritte G., Bond C.S., Smith S.M.
    Arch. Biochem. Biophys. 489:92-98(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  14. "The gene encoding the catalytically inactive beta-amylase BAM4 involved in starch breakdown in Arabidopsis leaves is expressed preferentially in vascular tissues in source and sink organs."
    Francisco P., Li J., Smith S.M.
    J. Plant Physiol. 167:890-895(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

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: June 24, 2015
This is version 95 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

External Data

Dasty 3

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 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.