BAM5_ARATH
ID BAM5_ARATH Reviewed; 498 AA.
AC P25853; O23375; Q0WWJ7; Q3EA19;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Beta-amylase 5;
DE Short=AtBeta-Amy;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Protein REDUCED BETA AMYLASE 1;
GN Name=BAM5; Synonyms=BMY1, RAM1; OrderedLocusNames=At4g15210;
GN ORFNames=dl3650c, FCAALL.97;
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] (ISOFORM 1).
RX PubMed=16668593; DOI=10.1104/pp.97.4.1599;
RA Monroe J.D., Salminen M.D., Preiss J.;
RT "Nucleotide sequence of a cDNA clone encoding a beta-amylase from
RT Arabidopsis thaliana.";
RL Plant Physiol. 97:1599-1601(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7716246; DOI=10.1104/pp.107.3.895;
RA Mita S., Suzuki-Fujii K., Nakamura K.;
RT "Sugar-inducible expression of a gene for beta-amylase in Arabidopsis
RT thaliana.";
RL Plant Physiol. 107:895-904(1995).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8552713; DOI=10.1104/pp.109.3.743;
RA Wang Q., Monroe J., Sjoelund R.D.;
RT "Identification and characterization of a phloem-specific beta-amylase.";
RL Plant Physiol. 109:743-750(1995).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11743123; DOI=10.1104/pp.010723;
RA Laby R.J., Kim D., Gibson S.I.;
RT "The ram1 mutant of Arabidopsis exhibits severely decreased beta-amylase
RT activity.";
RL Plant Physiol. 127:1798-1807(2001).
RN [11]
RP 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).
CC -!- FUNCTION: Beta-amylase activity. Major cytosolic beta-amylase isoform
CC in rosette leaves and inflorescences stems.
CC {ECO:0000269|PubMed:11743123}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8552713}.
CC Note=Present in the continuous phloem cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P25853-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P25853-2; Sequence=VSP_038978, VSP_038979;
CC -!- TISSUE SPECIFICITY: Detected in phloem sieve elements.
CC {ECO:0000269|PubMed:8552713}.
CC -!- INDUCTION: Circadian-regulated, with a peak in expression just before
CC the light period in short day conditions.
CC -!- DISRUPTION PHENOTYPE: Almost complete loss of beta-amylase activity in
CC rosette leaves and inflorescences (stems).
CC {ECO:0000269|PubMed:11743123}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; M73467; AAA32737.1; -; mRNA.
DR EMBL; D43783; BAA07842.1; -; Genomic_DNA.
DR EMBL; S77076; AAB34026.1; -; Genomic_DNA.
DR EMBL; Z97338; CAB10300.1; -; Genomic_DNA.
DR EMBL; AL161540; CAB78563.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83568.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83569.1; -; Genomic_DNA.
DR EMBL; AF424573; AAL11567.1; -; mRNA.
DR EMBL; AY142024; AAM98288.1; -; mRNA.
DR EMBL; AK316869; BAH19577.1; -; mRNA.
DR EMBL; AK226353; BAE98501.1; -; mRNA.
DR PIR; B71416; S36094.
DR RefSeq; NP_567460.1; NM_117609.3. [P25853-1]
DR RefSeq; NP_849389.1; NM_179058.1. [P25853-2]
DR AlphaFoldDB; P25853; -.
DR SMR; P25853; -.
DR STRING; 3702.AT4G15210.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; P25853; -.
DR PaxDb; P25853; -.
DR PRIDE; P25853; -.
DR ProteomicsDB; 241124; -. [P25853-1]
DR EnsemblPlants; AT4G15210.1; AT4G15210.1; AT4G15210. [P25853-1]
DR EnsemblPlants; AT4G15210.2; AT4G15210.2; AT4G15210. [P25853-2]
DR GeneID; 827185; -.
DR Gramene; AT4G15210.1; AT4G15210.1; AT4G15210. [P25853-1]
DR Gramene; AT4G15210.2; AT4G15210.2; AT4G15210. [P25853-2]
DR KEGG; ath:AT4G15210; -.
DR Araport; AT4G15210; -.
DR TAIR; locus:2129810; AT4G15210.
DR eggNOG; ENOG502QUU5; Eukaryota.
DR InParanoid; P25853; -.
DR OMA; VFSGAWR; -.
DR OrthoDB; 533202at2759; -.
DR PhylomeDB; P25853; -.
DR PRO; PR:P25853; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P25853; baseline and differential.
DR Genevisible; P25853; AT.
DR GO; GO:0099503; C:secretory vesicle; 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:0080027; P:response to herbivore; IEP:TAIR.
DR GO; GO:0005983; P:starch catabolic process; IDA:TAIR.
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; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Cytoplasm; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome.
FT CHAIN 1..498
FT /note="Beta-amylase 5"
FT /id="PRO_0000153932"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384..385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 411..420
FT /note="KPKLRMYGFT -> LLWRRSEVRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038978"
FT VAR_SEQ 421..498
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038979"
FT CONFLICT 155
FT /note="Q -> QV (in Ref. 3; CAB10300 and 4; CAB78563)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="F -> L (in Ref. 2; BAA07842/AAB34026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56063 MW; 0589DE69CD825C64 CRC64;
MATNYNEKLL LNYVPVYVML PLGVVNVENV FADPETLETQ LKRLKEEAGV DGVMVDVWWG
IIESKGPKQY DWTAYKTLFQ LIARLGLKIQ AIMSFHQCGG NVGDIVTIPI PQWVRDVGDN
DPDIYYTNRK GTRDIEYLSI GVDNLPLFAG RTAVQLYSDY MSSFKENMAD LIEAGVIVDI
EVGLGPAGEL RYPSYPQSQG WVFPGIGEFQ CYDKYLKKDF KEAAAKAGHP EWDLPEDAGE
YNDKPEETGF FKKDGTYVSE KGKFFMTWYS NKLIFHGDQI LGEANKIFAG LKVNLAAKVS
GIHWLYNHHS HAAELTAGYY NLFKRDGYRP IARMLSKHYG ILNFTCLEMK DTDNTAEALS
APQELVQEVL SKAWKEGIEV AGENALETYG AKGYNQILLN ARPNGVNPNG KPKLRMYGFT
YLRLSDTVFQ ENNFELFKKL VRKMHADQDY CGDAAKYGHE IVPLKTSNSQ LTLEDIADAA
QPSGAFKWDS ETDLKVDG
