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O23553

- BAM3_ARATH

UniProt

O23553 - BAM3_ARATH

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Protein
Beta-amylase 3, chloroplastic
Gene
BAM3, BMY8, CTBMY, At4g17090, dl4575c, FCAALL.5
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 – 1271Substrate By similarity
Binding sitei167 – 1671Substrate By similarity
Binding sitei175 – 1751Substrate By similarity
Active sitei259 – 2591Proton donor By similarity
Binding sitei371 – 3711Substrate By similarity
Binding sitei376 – 3761Substrate By similarity
Binding sitei418 – 4181Substrate By similarity
Active sitei456 – 4561Proton acceptor By similarity
Binding sitei489 – 4891Substrate By similarity

GO - Molecular functioni

  1. beta-amylase activity Source: TAIR
Complete GO annotation...

GO - Biological processi

  1. maltose biosynthetic process Source: TAIR
  2. response to cold Source: TAIR
  3. 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: Chromosome 4

Organism-specific databases

TAIRiAT4G17090.

Subcellular locationi

Plastidchloroplast 3 Publications

GO - Cellular componenti

  1. 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 – 4949Chloroplast Reviewed prediction
Add
BLAST
Chaini50 – 548499Beta-amylase 3, chloroplastic
PRO_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

Gene expression databases

GenevestigatoriO23553.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G17090.1-P.

Structurei

3D structure databases

ProteinModelPortaliO23553.
SMRiO23553. Positions 86-510.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG77898.
HOGENOMiHOG000238755.
InParanoidiQ9SMW0.
KOiK01177.
OMAiEHANCSP.
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

MELTLNSSSS LIKRKDAKSS RNQESSSNNM TFAKMKPPTY QFQAKNSVKE    50
MKFTHEKTFT PEGETLEKWE KLHVLSYPHS KNDASVPVFV MLPLDTVTMS 100
GHLNKPRAMN ASLMALKGAG VEGVMVDAWW GLVEKDGPMN YNWEGYAELI 150
QMVQKHGLKL QVVMSFHQCG GNVGDSCSIP LPPWVLEEIS KNPDLVYTDK 200
SGRRNPEYIS LGCDSVPVLR GRTPIQVYSD FMRSFRERFE GYIGGVIAEI 250
QVGMGPCGEL RYPSYPESNG TWRFPGIGEF QCYDKYMKSS LQAYAESIGK 300
TNWGTSGPHD AGEYKNLPED TEFFRRDGTW NSEYGKFFME WYSGKLLEHG 350
DQLLSSAKGI FQGSGAKLSG KVAGIHWHYN TRSHAAELTA GYYNTRNHDG 400
YLPIAKMFNK HGVVLNFTCM EMKDGEQPEH ANCSPEGLVK QVQNATRQAG 450
TELAGENALE RYDSSAFGQV VATNRSDSGN GLTAFTYLRM NKRLFEGQNW 500
QQLVEFVKNM KEGGHGRRLS KEDTTGSDLY VGFVKGKIAE NVEEAALV 548
Length:548
Mass (Da):61,353
Last modified:April 20, 2010 - v3
Checksum:iA5794EDC8427FE30
GO

Sequence cautioni

The sequence CAB46051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAB80980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAK96508.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.
The sequence AAL31225.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi D71439.
H85190.
T52556.
RefSeqi NP_567523.1. NM_117813.2.
UniGenei At.22021.
At.23528.
At.47944.
At.67939.

3D structure databases

ProteinModelPortali O23553.
SMRi O23553. Positions 86-510.
ModBasei Search...

Protein-protein interaction databases

STRINGi 3702.AT4G17090.1-P.

Protein family/group databases

CAZyi GH14. Glycoside Hydrolase Family 14.

Proteomic databases

PaxDbi O23553.
PRIDEi O23553.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G17090.1 ; AT4G17090.1 ; AT4G17090 .
GeneIDi 827419.
KEGGi ath:AT4G17090.

Organism-specific databases

TAIRi AT4G17090.

Phylogenomic databases

eggNOGi NOG77898.
HOGENOMi HOG000238755.
InParanoidi Q9SMW0.
KOi K01177.
OMAi EHANCSP.
PhylomeDBi O23553.

Enzyme and pathway databases

BioCyci ARA:AT4G17090-MONOMER.
MetaCyc:AT4G17090-MONOMER.
BRENDAi 3.2.1.2. 399.

Gene expression databases

Genevestigatori O23553.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF01373. Glyco_hydro_14. 1 hit.
[Graphical view ]
PRINTSi PR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 90 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