BAM2_ARATH
ID BAM2_ARATH Reviewed; 542 AA.
AC O65258;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-amylase 2, chloroplastic;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-amylase 9;
DE Flags: Precursor;
GN Name=BAM2; Synonyms=BMY9; OrderedLocusNames=At4g00490; ORFNames=F6N23.1;
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=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 [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 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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [6]
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).
CC -!- FUNCTION: Low beta-amylase activity. Interacts poorly with starch or
CC other alpha-1,4-glucan. {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. {ECO:0000269|PubMed:18390594,
CC ECO:0000269|PubMed:19664588};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18390594, ECO:0000269|PubMed:18431481}.
CC -!- INDUCTION: Slightly by cold stress. {ECO:0000269|PubMed:16297066}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF058919; AAC13634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80858.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81889.1; -; Genomic_DNA.
DR PIR; T01213; T01213.
DR RefSeq; NP_191958.3; NM_116273.5.
DR AlphaFoldDB; O65258; -.
DR SASBDB; O65258; -.
DR SMR; O65258; -.
DR BioGRID; 13250; 1.
DR STRING; 3702.AT4G00490.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; O65258; -.
DR PaxDb; O65258; -.
DR PRIDE; O65258; -.
DR ProteomicsDB; 240739; -.
DR EnsemblPlants; AT4G00490.1; AT4G00490.1; AT4G00490.
DR GeneID; 827959; -.
DR Gramene; AT4G00490.1; AT4G00490.1; AT4G00490.
DR KEGG; ath:AT4G00490; -.
DR Araport; AT4G00490; -.
DR TAIR; locus:2127033; AT4G00490.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_5_1_1; -.
DR OMA; TRFFCDG; -.
DR OrthoDB; 533202at2759; -.
DR PhylomeDB; O65258; -.
DR PRO; PR:O65258; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65258; baseline and differential.
DR Genevisible; O65258; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Glycosidase; Hydrolase; Plastid;
KW Polysaccharide degradation; Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..542
FT /note="Beta-amylase 2, chloroplastic"
FT /id="PRO_0000393417"
FT ACT_SITE 269
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 61398 MW; 892C9202CD34E1A9 CRC64;
MAIRLNHSVI PVSVKLGAPT RVSARSSLPF SVGDWRGVST FSGARPLVLA KVKLRAESTE
EDRVPIDDDD DSTDQLVDEE IVHFEERDFA GTACVPVYVM LPLGVIDMNS EVVEPEELLD
QLRTLKSVNV DGVMVDCWWG IVESHTPQVY NWSGYKKLFQ MIRELGLKIQ VVMSFHECGG
NVGDDVHIQI PEWVREIGQS NPDIYFTDSA GRRNTECLTW GIDKQRVLRG RTALEVYFDY
MRSFRVEFDE FFEEKIIPEI EVGLGPCGEL RYPSYPAQFG WKYPGIGEFQ CYDKYLMNSL
KEAAEVRGHS FWGRGPDNTE TYNSTPHGTG FFRDGGDYDS YYGRFFLNWY SRVLIDHGDR
VLAMANLAFE GTCIAAKLSG IHWWYKTASH AAELTAGFYN SSNRDGYGPI AAMFKKHDAA
LNFTCVELRT LDQHEDFPEA LADPEGLVWQ VLNAAWDASI PVASENALPC YDREGYNKIL
ENAKPLTDPD GRHLSCFTYL RLNPTLMESQ NFKEFERFLK RMHGEAVPDL GLAPGTQETN
PE
