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O23553

- BAM3_ARATH

UniProt

O23553 - BAM3_ARATH

Protein

Beta-amylase 3, chloroplastic

Gene

BAM3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (20 Apr 2010)
      Previous versions | rss
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    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

    1. beta-amylase activity Source: TAIR

    GO - Biological processi

    1. maltose biosynthetic process Source: TAIR
    2. response to cold Source: TAIR
    3. starch catabolic process Source: TAIR

    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

    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

    Gene expression databases

    GenevestigatoriO23553.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G17090.1-P.

    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.
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 91 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