O23553 (BAM3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-amylase 3, chloroplastic
EC=3.2.1.2

Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Beta-amylase 8
Chloroplast beta-amylase
Short name=CT-BMY

Gene names

Name:	BAM3
Synonyms:	BMY8, CTBMY
Ordered Locus Names:	At4g17090
ORF Names:	dl4575c, FCAALL.5

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Beta-amylase activity. No alpha-amylase activity. Involved in cold resistance. Mediates the accumulation of maltose upon freezing stress, thus contributing to the protection of the photosynthetic electron transport chain. Plays a role in the circadian-regulated starch degradation and maltose metabolism in chloroplasts, especially at night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan. Ref.1 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13
Catalytic activity	Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
Enzyme regulation	Redox regulation; active in reducing conditions, inactive in oxidizing conditions By similarity.
Subcellular location	Plastid › chloroplast Ref.1 Ref.9 Ref.12.
Tissue specificity	Expressed in vascular tissue of cotyledons, leaves, petioles, stems, petals, siliques and roots, particularly in phloem, as well as in photosynthetic tissues. Ref.14
Induction	By cold stress. Light-mediated circadian regulation; highest levels at dawn and at dusk in long days (LD) but only at dusk in short days (SD). Repressed by trehalose in a ABI4-dependent manner, this effect is reversed in the presence of sucrose. Ref.7 Ref.8 Ref.10
Disruption phenotype	Slightly retarded growth rate and reduced starch breakdown in leaves during the night. Ref.12
Sequence similarities	Belongs to the glycosyl hydrolase 14 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6-7. Ref.12 Ref.13
Sequence caution	The sequence AAK96508.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp. The sequence AAL31225.1 differs from that shown. Reason: Erroneous termination at position 377. Translated as Trp. The sequence CAB46051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB80980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 49	49	Chloroplast Potential
	Chain	50 – 548	499	Beta-amylase 3, chloroplastic		PRO_0000393418
Regions
	Region	457 – 458	2	Substrate binding By similarity
Sites
	Active site	259	1	Proton donor By similarity
	Active site	456	1	Proton acceptor By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity
	Binding site	371	1	Substrate By similarity
	Binding site	376	1	Substrate By similarity
	Binding site	418	1	Substrate By similarity
	Binding site	489	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O23553 [UniParc]. Last modified April 20, 2010. Version 3. Checksum: A5794EDC8427FE30	FASTA	548	61,353
	10 20 30 40 50 60 MELTLNSSSS LIKRKDAKSS RNQESSSNNM TFAKMKPPTY QFQAKNSVKE MKFTHEKTFT 70 80 90 100 110 120 PEGETLEKWE KLHVLSYPHS KNDASVPVFV MLPLDTVTMS GHLNKPRAMN ASLMALKGAG 130 140 150 160 170 180 VEGVMVDAWW GLVEKDGPMN YNWEGYAELI QMVQKHGLKL QVVMSFHQCG GNVGDSCSIP 190 200 210 220 230 240 LPPWVLEEIS KNPDLVYTDK SGRRNPEYIS LGCDSVPVLR GRTPIQVYSD FMRSFRERFE 250 260 270 280 290 300 GYIGGVIAEI QVGMGPCGEL RYPSYPESNG TWRFPGIGEF QCYDKYMKSS LQAYAESIGK 310 320 330 340 350 360 TNWGTSGPHD AGEYKNLPED TEFFRRDGTW NSEYGKFFME WYSGKLLEHG DQLLSSAKGI 370 380 390 400 410 420 FQGSGAKLSG KVAGIHWHYN TRSHAAELTA GYYNTRNHDG YLPIAKMFNK HGVVLNFTCM 430 440 450 460 470 480 EMKDGEQPEH ANCSPEGLVK QVQNATRQAG TELAGENALE RYDSSAFGQV VATNRSDSGN 490 500 510 520 530 540 GLTAFTYLRM NKRLFEGQNW QQLVEFVKNM KEGGHGRRLS KEDTTGSDLY VGFVKGKIAE NVEEAALV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An Arabidopsis gene encoding a chloroplast-targeted beta-amylase." Lao N.T., Schoneveld O., Mould R.M., Hibberd J.M., Gray J.C., Kavanagh T.A. Plant J. 20:519-527(1999) [PubMed: 10652124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"RNA interference of Arabidopsis beta-amylase8 prevents maltose accumulation upon cold shock and increases sensitivity of PSII photochemical efficiency to freezing stress." Kaplan F., Guy C.L. Plant J. 44:730-743(2005) [PubMed: 16297066] [Abstract] Cited for: FUNCTION, INDUCTION BY COLD.
[8]	"Daylength and circadian effects on starch degradation and maltose metabolism." Lu Y., Gehan J.P., Sharkey T.D. Plant Physiol. 138:2280-2291(2005) [PubMed: 16055686] [Abstract] Cited for: FUNCTION, INDUCTION BY CIRCADIAN DAYLENGTH.
[9]	"Redox regulation of a novel plastid-targeted beta-amylase of Arabidopsis." Sparla F., Costa A., Lo Schiavo F., Pupillo P., Trost P. Plant Physiol. 141:840-850(2006) [PubMed: 16698902] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"ABI4 mediates the effects of exogenous trehalose on Arabidopsis growth and starch breakdown." Ramon M., Rolland F., Thevelein J.M., van Dijck P., Leyman B. Plant Mol. Biol. 63:195-206(2007) [PubMed: 17031512] [Abstract] Cited for: INDUCTION BY TREHALOSE.
[11]	"Glucan, water dikinase activity stimulates breakdown of starch granules by plastidial beta-amylases." Edner C., Li J., Albrecht T., Mahlow S., Hejazi M., Hussain H., Kaplan F., Guy C., Smith S.M., Steup M., Ritte G. Plant Physiol. 145:17-28(2007) [PubMed: 17631522] [Abstract] Cited for: FUNCTION.
[12]	"Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts." Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P., Gil M., Reinhold H., Eicke S., Messerli G., Dorken G., Halliday K., Smith A.M., Smith S.M., Zeeman S.C. Plant Cell 20:1040-1058(2008) [PubMed: 18390594] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, GENE FAMILY, NOMENCLATURE.
[13]	"Catalytically-inactive beta-amylase BAM4 required for starch breakdown in Arabidopsis leaves is a starch-binding-protein." Li J., Francisco P., Zhou W., Edner C., Steup M., Ritte G., Bond C.S., Smith S.M. Arch. Biochem. Biophys. 489:92-98(2009) [PubMed: 19664588] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[14]	"The gene encoding the catalytically inactive beta-amylase BAM4 involved in starch breakdown in Arabidopsis leaves is expressed preferentially in vascular tissues in source and sink organs." Francisco P., Li J., Smith S.M. J. Plant Physiol. 167:890-895(2010) [PubMed: 20153546] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ250341 mRNA. Translation: CAB58423.1. Z97342 Genomic DNA. Translation: CAB46051.1. Different initiation. AL161545 Genomic DNA. Translation: CAB80980.1. Different initiation. CP002687 Genomic DNA. Translation: AEE83848.1. AY052315 mRNA. Translation: AAK96508.1. Sequence problems. AY061898 mRNA. Translation: AAL31225.1. Sequence problems. AY087592 mRNA. Translation: AAM65134.1.
IPI	IPI00524115.
PIR	D71439. H85190. T52556.
RefSeq	NP_567523.1. NM_117813.2.
UniGene	At.22021. At.23528. At.47944. At.67939.
3D structure databases
HSSP	HSSP built from PDB template 1BYB based on UniProtKB P10538.
ProteinModelPortal	O23553.
SMR	O23553. Positions 82-512.
ModBase	Search...
Protein-protein interaction databases
STRING	O23553.
Protein family/group databases
CAZy	GH14. Glycoside Hydrolase Family 14.
Proteomic databases
PRIDE	O23553.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G17090.1; AT4G17090.1; AT4G17090.
GeneID	827419.
GenomeReviews	Gene locus AT4G17090 in contig CT486007_GR.
KEGG	ath:AT4G17090.
NMPDR	fig|3702.1.peg.19495.
Organism-specific databases
TAIR	At4g17090.
Phylogenomic databases
eggNOG	NOG77898.
GeneTree	EPGT00070000028196.
OMA	PHDAGEY.
PhylomeDB	O23553.
ProtClustDB	PLN02803.
Enzyme and pathway databases
BioCyc	MetaCyc:AT4G17090-MONOMER.
BRENDA	3.2.1.2. 399.
Gene expression databases
Genevestigator	O23553.
Family and domain databases
InterPro	IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR001371. Glyco_hydro_14B_pln. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01177.
Pfam	PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00842. GLHYDLASE14B.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAM3_ARATH

Accession

Primary (citable) accession number: O23553
Secondary accession number(s): Q941A5, Q9SMW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	April 20, 2010
Last modified:	December 14, 2011
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program