ID BAM3_ARATH Reviewed; 548 AA.
AC O23553; Q941A5; Q9SMW0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Beta-amylase 3, chloroplastic;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 8;
DE AltName: Full=Chloroplast beta-amylase;
DE Short=CT-BMY;
DE Flags: Precursor;
GN Name=BAM3; Synonyms=BMY8, CTBMY; OrderedLocusNames=At4g17090;
GN ORFNames=dl4575c, FCAALL.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10652124; DOI=10.1046/j.1365-313x.1999.00625.x;
RA Lao N.T., Schoneveld O., Mould R.M., Hibberd J.M., Gray J.C.,
RA Kavanagh T.A.;
RT "An Arabidopsis gene encoding a chloroplast-targeted beta-amylase.";
RL Plant J. 20:519-527(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INDUCTION BY COLD.
RX PubMed=16297066; DOI=10.1111/j.1365-313x.2005.02565.x;
RA Kaplan F., Guy C.L.;
RT "RNA interference of Arabidopsis beta-amylase8 prevents maltose
RT accumulation upon cold shock and increases sensitivity of PSII
RT photochemical efficiency to freezing stress.";
RL Plant J. 44:730-743(2005).
RN [8]
RP FUNCTION, AND INDUCTION BY CIRCADIAN DAYLENGTH.
RX PubMed=16055686; DOI=10.1104/pp.105.061903;
RA Lu Y., Gehan J.P., Sharkey T.D.;
RT "Daylength and circadian effects on starch degradation and maltose
RT metabolism.";
RL Plant Physiol. 138:2280-2291(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16698902; DOI=10.1104/pp.106.079186;
RA Sparla F., Costa A., Lo Schiavo F., Pupillo P., Trost P.;
RT "Redox regulation of a novel plastid-targeted beta-amylase of
RT Arabidopsis.";
RL Plant Physiol. 141:840-850(2006).
RN [10]
RP INDUCTION BY TREHALOSE.
RX PubMed=17031512; DOI=10.1007/s11103-006-9082-2;
RA Ramon M., Rolland F., Thevelein J.M., van Dijck P., Leyman B.;
RT "ABI4 mediates the effects of exogenous trehalose on Arabidopsis growth and
RT starch breakdown.";
RL Plant Mol. Biol. 63:195-206(2007).
RN [11]
RP FUNCTION.
RX PubMed=17631522; DOI=10.1104/pp.107.104224;
RA Edner C., Li J., Albrecht T., Mahlow S., Hejazi M., Hussain H., Kaplan F.,
RA Guy C., Smith S.M., Steup M., Ritte G.;
RT "Glucan, water dikinase activity stimulates breakdown of starch granules by
RT plastidial beta-amylases.";
RL Plant Physiol. 145:17-28(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18390594; DOI=10.1105/tpc.107.056507;
RA Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P.,
RA Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K.,
RA Smith A.M., Smith S.M., Zeeman S.C.;
RT "Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts
RT upstream of three active beta-amylases in Arabidopsis chloroplasts.";
RL Plant Cell 20:1040-1058(2008).
RN [13]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19664588; DOI=10.1016/j.abb.2009.07.024;
RA Li J., Francisco P., Zhou W., Edner C., Steup M., Ritte G., Bond C.S.,
RA Smith S.M.;
RT "Catalytically-inactive beta-amylase BAM4 required for starch breakdown in
RT Arabidopsis leaves is a starch-binding-protein.";
RL Arch. Biochem. Biophys. 489:92-98(2009).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=20153546; DOI=10.1016/j.jplph.2010.01.006;
RA Francisco P., Li J., Smith S.M.;
RT "The gene encoding the catalytically inactive beta-amylase BAM4 involved in
RT starch breakdown in Arabidopsis leaves is expressed preferentially in
RT vascular tissues in source and sink organs.";
RL J. Plant Physiol. 167:890-895(2010).
CC -!- FUNCTION: Beta-amylase activity. No alpha-amylase activity. Involved in
CC cold resistance. Mediates the accumulation of maltose upon freezing
CC stress, thus contributing to the protection of the photosynthetic
CC electron transport chain. Plays a role in the circadian-regulated
CC starch degradation and maltose metabolism in chloroplasts, especially
CC at night. More active on phosphorylated glucan. Interacts directly with
CC starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:10652124,
CC ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066,
CC ECO:0000269|PubMed:17631522, ECO:0000269|PubMed:18390594,
CC ECO:0000269|PubMed:19664588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides so as to remove successive maltose units from the
CC non-reducing ends of the chains.; EC=3.2.1.2;
CC -!- ACTIVITY REGULATION: Redox regulation; active in reducing conditions,
CC inactive in oxidizing conditions. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:18390594,
CC ECO:0000269|PubMed:19664588};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10652124, ECO:0000269|PubMed:16698902,
CC ECO:0000269|PubMed:18390594}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissue of cotyledons, leaves,
CC petioles, stems, petals, siliques and roots, particularly in phloem, as
CC well as in photosynthetic tissues. {ECO:0000269|PubMed:20153546}.
CC -!- INDUCTION: By cold stress. Light-mediated circadian regulation; highest
CC levels at dawn and at dusk in long days (LD) but only at dusk in short
CC days (SD). Repressed by trehalose in a ABI4-dependent manner, this
CC effect is reversed in the presence of sucrose.
CC {ECO:0000269|PubMed:16055686, ECO:0000269|PubMed:16297066,
CC ECO:0000269|PubMed:17031512}.
CC -!- DISRUPTION PHENOTYPE: Slightly retarded growth rate and reduced starch
CC breakdown in leaves during the night. {ECO:0000269|PubMed:18390594}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK96508.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL31225.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB46051.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ250341; CAB58423.1; -; mRNA.
DR EMBL; Z97342; CAB46051.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161545; CAB80980.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE83848.1; -; Genomic_DNA.
DR EMBL; AY052315; AAK96508.1; ALT_SEQ; mRNA.
DR EMBL; AY061898; AAL31225.1; ALT_SEQ; mRNA.
DR EMBL; AY087592; AAM65134.1; -; mRNA.
DR PIR; D71439; D71439.
DR PIR; H85190; H85190.
DR PIR; T52556; T52556.
DR RefSeq; NP_567523.1; NM_117813.3.
DR AlphaFoldDB; O23553; -.
DR SMR; O23553; -.
DR BioGRID; 12712; 1.
DR STRING; 3702.O23553; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; O23553; -.
DR PaxDb; 3702-AT4G17090-1; -.
DR ProteomicsDB; 241123; -.
DR EnsemblPlants; AT4G17090.1; AT4G17090.1; AT4G17090.
DR GeneID; 827419; -.
DR Gramene; AT4G17090.1; AT4G17090.1; AT4G17090.
DR KEGG; ath:AT4G17090; -.
DR Araport; AT4G17090; -.
DR TAIR; AT4G17090; CT-BMY.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_1_1_1; -.
DR InParanoid; O23553; -.
DR OMA; WNSEYGR; -.
DR OrthoDB; 46229at2759; -.
DR PhylomeDB; O23553; -.
DR BioCyc; ARA:AT4G17090-MONOMER; -.
DR BioCyc; MetaCyc:AT4G17090-MONOMER; -.
DR BRENDA; 3.2.1.2; 399.
DR PRO; PR:O23553; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23553; baseline and differential.
DR Genevisible; O23553; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IDA:TAIR.
DR GO; GO:0000024; P:maltose biosynthetic process; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IDA:TAIR.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001554; Glyco_hydro_14.
DR InterPro; IPR018238; Glyco_hydro_14_CS.
DR InterPro; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF1; BETA-AMYLASE 3, CHLOROPLASTIC; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase; Plastid;
KW Polysaccharide degradation; Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..548
FT /note="Beta-amylase 3, chloroplastic"
FT /id="PRO_0000393418"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 456
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457..458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 61353 MW; A5794EDC8427FE30 CRC64;
MELTLNSSSS LIKRKDAKSS RNQESSSNNM TFAKMKPPTY QFQAKNSVKE MKFTHEKTFT
PEGETLEKWE KLHVLSYPHS KNDASVPVFV MLPLDTVTMS GHLNKPRAMN ASLMALKGAG
VEGVMVDAWW GLVEKDGPMN YNWEGYAELI QMVQKHGLKL QVVMSFHQCG GNVGDSCSIP
LPPWVLEEIS KNPDLVYTDK SGRRNPEYIS LGCDSVPVLR GRTPIQVYSD FMRSFRERFE
GYIGGVIAEI QVGMGPCGEL RYPSYPESNG TWRFPGIGEF QCYDKYMKSS LQAYAESIGK
TNWGTSGPHD AGEYKNLPED TEFFRRDGTW NSEYGKFFME WYSGKLLEHG DQLLSSAKGI
FQGSGAKLSG KVAGIHWHYN TRSHAAELTA GYYNTRNHDG YLPIAKMFNK HGVVLNFTCM
EMKDGEQPEH ANCSPEGLVK QVQNATRQAG TELAGENALE RYDSSAFGQV VATNRSDSGN
GLTAFTYLRM NKRLFEGQNW QQLVEFVKNM KEGGHGRRLS KEDTTGSDLY VGFVKGKIAE
NVEEAALV
//
