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   24-JAN-2024, entry version 143.
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.Q9LIR6; -.
DR   CAZy; GH14; Glycoside Hydrolase Family 14.
DR   iPTMnet; Q9LIR6; -.
DR   PaxDb; 3702-AT3G23920-1; -.
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; AT3G23920; BAM1.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_1_1_1; -.
DR   InParanoid; Q9LIR6; -.
DR   OMA; WGRRNCE; -.
DR   OrthoDB; 46229at2759; -.
DR   PhylomeDB; Q9LIR6; -.
DR   BioCyc; MetaCyc:AT3G23920-MONOMER; -.
DR   BRENDA; 3.2.1.2; 399.
DR   PRO; PR:Q9LIR6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIR6; baseline and differential.
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   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:SF31; BETA-AMYLASE 1, 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.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
DR   Genevisible; Q9LIR6; AT.
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
//