P25853 (BAM5_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-amylase 5
Short name=AtBeta-Amy
EC=3.2.1.2

Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Protein REDUCED BETA AMYLASE 1

Gene names

Name:	BAM5
Synonyms:	BMY1, RAM1
Ordered Locus Names:	At4g15210
ORF Names:	dl3650c, FCAALL.97

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Beta-amylase activity. Major cytosolic beta-amylase isoform in rosette leaves and inflorescences stems. Ref.10
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.
Subcellular location	Cytoplasm. Note: Present in the continuous phloem cytoplasm. Ref.9
Tissue specificity	Detected in phloem sieve elements. Ref.9
Induction	Circadian-regulated, with a peak in expression just before the light period in short day conditions.
Disruption phenotype	Almost complete loss of beta-amylase activity in rosette leaves and inflorescences (stems). Ref.10
Sequence similarities	Belongs to the glycosyl hydrolase 14 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to herbivore Inferred from expression pattern PubMed 19251652. Source: TAIR starch catabolic process Inferred from direct assay Ref.2. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	beta-amylase activity Inferred from direct assay Ref.2. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25853-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P25853-2)

The sequence of this isoform differs from the canonical sequence as follows:
     411-420: KPKLRMYGFT → LLWRRSEVRA
     421-498: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 498	498	Beta-amylase 5		PRO_0000153932
Regions
	Region	384 – 385	2	Substrate binding By similarity
Sites
	Active site	189	1	Proton donor By similarity
	Active site	383	1	Proton acceptor By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	298	1	Substrate By similarity
	Binding site	303	1	Substrate By similarity
	Binding site	345	1	Substrate By similarity
	Binding site	423	1	Substrate By similarity
Natural variations
	Alternative sequence	411 – 420	10	KPKLRMYGFT → LLWRRSEVRA in isoform 2.		VSP_038978
	Alternative sequence	421 – 498	78	Missing in isoform 2.		VSP_038979
Experimental info
	Sequence conflict	155	1	Q → QV in CAB10300. Ref.3
	Sequence conflict	155	1	Q → QV in CAB78563. Ref.4
	Sequence conflict	486	1	F → L in BAA07842. Ref.2
	Sequence conflict	486	1	F → L in AAB34026. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 0589DE69CD825C64	FASTA	498	56,063
	10 20 30 40 50 60 MATNYNEKLL LNYVPVYVML PLGVVNVENV FADPETLETQ LKRLKEEAGV DGVMVDVWWG 70 80 90 100 110 120 IIESKGPKQY DWTAYKTLFQ LIARLGLKIQ AIMSFHQCGG NVGDIVTIPI PQWVRDVGDN 130 140 150 160 170 180 DPDIYYTNRK GTRDIEYLSI GVDNLPLFAG RTAVQLYSDY MSSFKENMAD LIEAGVIVDI 190 200 210 220 230 240 EVGLGPAGEL RYPSYPQSQG WVFPGIGEFQ CYDKYLKKDF KEAAAKAGHP EWDLPEDAGE 250 260 270 280 290 300 YNDKPEETGF FKKDGTYVSE KGKFFMTWYS NKLIFHGDQI LGEANKIFAG LKVNLAAKVS 310 320 330 340 350 360 GIHWLYNHHS HAAELTAGYY NLFKRDGYRP IARMLSKHYG ILNFTCLEMK DTDNTAEALS 370 380 390 400 410 420 APQELVQEVL SKAWKEGIEV AGENALETYG AKGYNQILLN ARPNGVNPNG KPKLRMYGFT 430 440 450 460 470 480 YLRLSDTVFQ ENNFELFKKL VRKMHADQDY CGDAAKYGHE IVPLKTSNSQ LTLEDIADAA 490 QPSGAFKWDS ETDLKVDG
	Isoform 2 [UniParc]. Checksum: 96B8932F1556FFE7	FASTA	420	47,301
	10 20 30 40 50 60 MATNYNEKLL LNYVPVYVML PLGVVNVENV FADPETLETQ LKRLKEEAGV DGVMVDVWWG 70 80 90 100 110 120 IIESKGPKQY DWTAYKTLFQ LIARLGLKIQ AIMSFHQCGG NVGDIVTIPI PQWVRDVGDN 130 140 150 160 170 180 DPDIYYTNRK GTRDIEYLSI GVDNLPLFAG RTAVQLYSDY MSSFKENMAD LIEAGVIVDI 190 200 210 220 230 240 EVGLGPAGEL RYPSYPQSQG WVFPGIGEFQ CYDKYLKKDF KEAAAKAGHP EWDLPEDAGE 250 260 270 280 290 300 YNDKPEETGF FKKDGTYVSE KGKFFMTWYS NKLIFHGDQI LGEANKIFAG LKVNLAAKVS 310 320 330 340 350 360 GIHWLYNHHS HAAELTAGYY NLFKRDGYRP IARMLSKHYG ILNFTCLEMK DTDNTAEALS 370 380 390 400 410 420 APQELVQEVL SKAWKEGIEV AGENALETYG AKGYNQILLN ARPNGVNPNG LLWRRSEVRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA clone encoding a beta-amylase from Arabidopsis thaliana." Monroe J.D., Salminen M.D., Preiss J. Plant Physiol. 97:1599-1601(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Sugar-inducible expression of a gene for beta-amylase in Arabidopsis thaliana." Mita S., Suzuki-Fujii K., Nakamura K. Plant Physiol. 107:895-904(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[7]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[8]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[9]	"Identification and characterization of a phloem-specific beta-amylase." Wang Q., Monroe J., Sjoelund R.D. Plant Physiol. 109:743-750(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]	"The ram1 mutant of Arabidopsis exhibits severely decreased beta-amylase activity." Laby R.J., Kim D., Gibson S.I. Plant Physiol. 127:1798-1807(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[11]	"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] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M73467 mRNA. Translation: AAA32737.1. D43783 Genomic DNA. Translation: BAA07842.1. S77076 Genomic DNA. Translation: AAB34026.1. Z97338 Genomic DNA. Translation: CAB10300.1. AL161540 Genomic DNA. Translation: CAB78563.1. CP002687 Genomic DNA. Translation: AEE83568.1. CP002687 Genomic DNA. Translation: AEE83569.1. AF424573 mRNA. Translation: AAL11567.1. AY142024 mRNA. Translation: AAM98288.1. AK316869 mRNA. Translation: BAH19577.1. AK226353 mRNA. Translation: BAE98501.1.
IPI	IPI00517770. IPI00532891.
PIR	S36094. B71416.
RefSeq	NP_567460.1. NM_117609.2. NP_849389.1. NM_179058.1.
UniGene	At.25187.
3D structure databases
ProteinModelPortal	P25853.
SMR	P25853. Positions 9-498.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G15210.1-P.
Protein family/group databases
CAZy	GH14. Glycoside Hydrolase Family 14.
Proteomic databases
PaxDb	P25853.
PRIDE	P25853.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G15210.1; AT4G15210.1; AT4G15210.
GeneID	827185.
KEGG	ath:AT4G15210.
Organism-specific databases
TAIR	At4g15210.
Phylogenomic databases
eggNOG	NOG322510.
HOGENOM	HOG000238755.
InParanoid	P25853.
OMA	RYPSYPQ.
PhylomeDB	P25853.
ProtClustDB	PLN02801.
Gene expression databases
Genevestigator	P25853.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR001371. Glyco_hydro_14B_pln. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BAM5_ARATH

Accession

Primary (citable) accession number: P25853
Secondary accession number(s): O23375, Q0WWJ7, Q3EA19

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program