Q9LIR6 (BAM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-amylase 1, chloroplastic
EC=3.2.1.2

Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Beta-amylase 7
Thioredoxin-regulated beta-amylase
Short name=TR-BAMY

Gene names

Name:	BAM1
Synonyms:	BMY7, TRBAMY
Ordered Locus Names:	At3g23920
ORF Names:	F14O13.12

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	575 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. Can use p-nitrophenyl maltopentaoside (PNPG5) as substrate only in reduced form. Can play a minor role in the starch degradation and maltose metabolism in chloroplasts during the night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan. Ref.6 Ref.8 Ref.9
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. Thioredoxins f1, m1, and y1 mediate the reversible reductive activation of oxidized BAM1. Ref.5
Subcellular location	Plastid › chloroplast Ref.5 Ref.8.
Tissue specificity	Expressed in leaves, roots, flowers, pollen, and seeds. Ref.5
Disruption phenotype	Normal growth rate and starch breakdown in leaves during the night. Ref.8
Sequence similarities	Belongs to the glycosyl hydrolase 14 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6-8. Ref.5 Ref.8 Ref.9

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to water deprivation Inferred from expression pattern. Source: TAIR starch catabolic process Inferred from mutant phenotype Ref.8. Source: TAIR
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.7. Source: TAIR nucleus Inferred from direct assay Ref.7. Source: TAIR
Molecular function	beta-amylase activity Inferred from direct assay Ref.8. Source: TAIR 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 – 41	41	Chloroplast
	Chain	42 – 575	534	Beta-amylase 1, chloroplastic		PRO_0000393416
Regions
	Region	478 – 479	2	Substrate binding By similarity
Sites
	Active site	279	1	Proton donor By similarity
	Active site	477	1	Proton acceptor By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Binding site	392	1	Substrate By similarity
	Binding site	397	1	Substrate By similarity
	Binding site	439	1	Substrate By similarity
	Binding site	517	1	Substrate By similarity
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.10
	Modified residue	55	1	Phosphoserine Ref.7 Ref.10
	Modified residue	59	1	Phosphoserine Ref.7 Ref.10
	Disulfide bond	73 ↔ 511		Inhibitory under oxidizing conditions Ref.5
Experimental info
	Mutagenesis	73	1	C → S: Impaired redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	189	1	C → S: Normal redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	247	1	C → S: Normal redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	302	1	C → S: Normal redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	440	1	C → S: Normal redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	454	1	C → S: Normal redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	511	1	C → S: Impaired redox inactivation under oxidizing conditions. Ref.5
	Mutagenesis	547	1	C → S: Normal redox enzyme activation under oxidizing conditions. Ref.5
	Sequence conflict	405	1	H → N in BAE98433. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9LIR6 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CDCF1007217789A0	FASTA	575	63,762
	10 20 30 40 50 60 MALNLSHQLG VLAGTPIKSG EMTDSSLLSI SPPSARMMTP KAMNRNYKAH GTDPSPPMSP 70 80 90 100 110 120 ILGATRADLS VACKAFAVEN GIGTIEEQRT YREGGIGGKK EGGGGVPVFV MMPLDSVTMG 130 140 150 160 170 180 NTVNRRKAMK ASLQALKSAG VEGIMIDVWW GLVEKESPGT YNWGGYNELL ELAKKLGLKV 190 200 210 220 230 240 QAVMSFHQCG GNVGDSVTIP LPQWVVEEVD KDPDLAYTDQ WGRRNHEYIS LGADTLPVLK 250 260 270 280 290 300 GRTPVQCYAD FMRAFRDNFK HLLGETIVEI QVGMGPAGEL RYPSYPEQEG TWKFPGIGAF 310 320 330 340 350 360 QCYDKYSLSS LKAAAETYGK PEWGSTGPTD AGHYNNWPED TQFFKKEGGG WNSEYGDFFL 370 380 390 400 410 420 SWYSQMLLDH GERILSSAKS IFENMGVKIS VKIAGIHWHY GTRSHAPELT AGYYNTRFRD 430 440 450 460 470 480 GYLPIAQMLA RHNAIFNFTC IEMRDHEQPQ DALCAPEKLV NQVALATLAA EVPLAGENAL 490 500 510 520 530 540 PRYDDYAHEQ ILKASALNLD QNNEGEPREM CAFTYLRMNP ELFQADNWGK FVAFVKKMGE 550 560 570 GRDSHRCREE VEREAEHFVH VTQPLVQEAA VALTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed: 10907853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"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.
[4]	"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] OF 242-407. Strain: cv. Columbia.
[5]	"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, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISULFIDE BOND, TRANSIT PEPTIDE, MUTAGENESIS OF CYS-73; CYS-189; CYS-247; CYS-302; CYS-440; CYS-454; CYS-511 AND CYS-547.
[6]	"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.
[7]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, MASS SPECTROMETRY. Tissue: Root.
[8]	"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.
[9]	"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.
[10]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-55 AND SER-59, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP001297 Genomic DNA. Translation: BAB03009.1. CP002686 Genomic DNA. Translation: AEE76832.1. AF367293 mRNA. Translation: AAK56281.1. AY074393 mRNA. Translation: AAL67089.1. AY078046 mRNA. Translation: AAL77747.1. AY096517 mRNA. Translation: AAM20167.1. AK226274 mRNA. Translation: BAE98433.1.
IPI	IPI00518242.
RefSeq	NP_189034.1. NM_113297.2.
UniGene	At.8278.
3D structure databases
HSSP	HSSP built from PDB template 1B1Y based on UniProtKB P16098.
ProteinModelPortal	Q9LIR6.
SMR	Q9LIR6. Positions 100-565.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LIR6.
Protein family/group databases
CAZy	GH14. Glycoside Hydrolase Family 14.
Proteomic databases
PRIDE	Q9LIR6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G23920.1; AT3G23920.1; AT3G23920.
GeneID	821975.
GenomeReviews	Gene locus AT3G23920 in contig BA000014_GR.
KEGG	ath:AT3G23920.
NMPDR	fig|3702.1.peg.14650.
Organism-specific databases
TAIR	At3g23920.
Phylogenomic databases
GeneTree	EPGT00070000028196.
InParanoid	Q9LIR6.
OMA	DKDQDLA.
PhylomeDB	Q9LIR6.
ProtClustDB	PLN00197.
Enzyme and pathway databases
BRENDA	3.2.1.2. 399.
Gene expression databases
ArrayExpress	Q9LIR6.
Genevestigator	Q9LIR6.
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.
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

BAM1_ARATH

Accession

Primary (citable) accession number: Q9LIR6
Secondary accession number(s): Q0WWR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program