BAM1_ARATH
ID BAM1_ARATH Reviewed; 575 AA.
AC Q9LIR6; Q0WWR5;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Beta-amylase 1, chloroplastic;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 7;
DE AltName: Full=Thioredoxin-regulated beta-amylase;
DE Short=TR-BAMY;
DE Flags: Precursor;
GN Name=BAM1; Synonyms=BMY7, TRBAMY; OrderedLocusNames=At3g23920;
GN ORFNames=F14O13.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-407.
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, DISULFIDE BOND, TRANSIT PEPTIDE CLEAVAGE SITE, AND
RP MUTAGENESIS OF CYS-73; CYS-189; CYS-247; CYS-302; CYS-440; CYS-454; CYS-511
RP AND CYS-547.
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Beta-amylase activity. Can use p-nitrophenyl maltopentaoside
CC (PNPG5) as substrate only in reduced form. Can play a minor role in the
CC starch degradation and maltose metabolism in chloroplasts during the
CC night. More active on phosphorylated glucan. Interacts directly with
CC starch or other alpha-1,4-glucan. {ECO:0000269|PubMed:17631522,
CC ECO:0000269|PubMed:18390594, 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. Thioredoxins f1, m1, and y1 mediate
CC the reversible reductive activation of oxidized BAM1.
CC {ECO:0000269|PubMed:16698902}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8. {ECO:0000269|PubMed:16698902,
CC ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:19664588};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers, pollen, and
CC seeds. {ECO:0000269|PubMed:16698902}.
CC -!- DISRUPTION PHENOTYPE: Normal growth rate and starch breakdown in leaves
CC during the night. {ECO:0000269|PubMed:18390594}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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DR EMBL; AP001297; BAB03009.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76832.1; -; Genomic_DNA.
DR EMBL; AF367293; AAK56281.1; -; mRNA.
DR EMBL; AY074393; AAL67089.1; -; mRNA.
DR EMBL; AY078046; AAL77747.1; -; mRNA.
DR EMBL; AY096517; AAM20167.1; -; mRNA.
DR EMBL; AK226274; BAE98433.1; -; mRNA.
DR RefSeq; NP_189034.1; NM_113297.3.
DR AlphaFoldDB; Q9LIR6; -.
DR SASBDB; Q9LIR6; -.
DR SMR; Q9LIR6; -.
DR STRING; 3702.AT3G23920.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; Q9LIR6; -.
DR PaxDb; Q9LIR6; -.
DR PRIDE; Q9LIR6; -.
DR ProteomicsDB; 240813; -.
DR EnsemblPlants; AT3G23920.1; AT3G23920.1; AT3G23920.
DR GeneID; 821975; -.
DR Gramene; AT3G23920.1; AT3G23920.1; AT3G23920.
DR KEGG; ath:AT3G23920; -.
DR Araport; AT3G23920; -.
DR TAIR; locus:2076086; AT3G23920.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_1_1_1; -.
DR OMA; PGSYNWG; -.
DR OrthoDB; 533202at2759; -.
DR PhylomeDB; Q9LIR6; -.
DR BioCyc; MetaCyc:AT3G23920-MON; -.
DR BRENDA; 3.2.1.2; 399.
DR PRO; PR:Q9LIR6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIR6; baseline and differential.
DR Genevisible; Q9LIR6; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016161; F:beta-amylase activity; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; 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 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Disulfide bond; Glycosidase;
KW Hydrolase; Phosphoprotein; Plastid; Polysaccharide degradation;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16698902"
FT CHAIN 42..575
FT /note="Beta-amylase 1, chloroplastic"
FT /id="PRO_0000393416"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 477
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 478..479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT DISULFID 73..511
FT /note="Inhibitory under oxidizing conditions"
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 73
FT /note="C->S: Impaired redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 189
FT /note="C->S: Normal redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 247
FT /note="C->S: Normal redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 302
FT /note="C->S: Normal redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 440
FT /note="C->S: Normal redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 454
FT /note="C->S: Normal redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 511
FT /note="C->S: Impaired redox inactivation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT MUTAGEN 547
FT /note="C->S: Normal redox enzyme activation under oxidizing
FT conditions."
FT /evidence="ECO:0000269|PubMed:16698902"
FT CONFLICT 405
FT /note="H -> N (in Ref. 4; BAE98433)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 63762 MW; CDCF1007217789A0 CRC64;
MALNLSHQLG VLAGTPIKSG EMTDSSLLSI SPPSARMMTP KAMNRNYKAH GTDPSPPMSP
ILGATRADLS VACKAFAVEN GIGTIEEQRT YREGGIGGKK EGGGGVPVFV MMPLDSVTMG
NTVNRRKAMK ASLQALKSAG VEGIMIDVWW GLVEKESPGT YNWGGYNELL ELAKKLGLKV
QAVMSFHQCG GNVGDSVTIP LPQWVVEEVD KDPDLAYTDQ WGRRNHEYIS LGADTLPVLK
GRTPVQCYAD FMRAFRDNFK HLLGETIVEI QVGMGPAGEL RYPSYPEQEG TWKFPGIGAF
QCYDKYSLSS LKAAAETYGK PEWGSTGPTD AGHYNNWPED TQFFKKEGGG WNSEYGDFFL
SWYSQMLLDH GERILSSAKS IFENMGVKIS VKIAGIHWHY GTRSHAPELT AGYYNTRFRD
GYLPIAQMLA RHNAIFNFTC IEMRDHEQPQ DALCAPEKLV NQVALATLAA EVPLAGENAL
PRYDDYAHEQ ILKASALNLD QNNEGEPREM CAFTYLRMNP ELFQADNWGK FVAFVKKMGE
GRDSHRCREE VEREAEHFVH VTQPLVQEAA VALTH
