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Q9LIR6 (BAM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Plastidchloroplast 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4141Chloroplast
Chain42 – 575534Beta-amylase 1, chloroplastic
PRO_0000393416

Regions

Region478 – 4792Substrate binding By similarity

Sites

Active site2791Proton donor By similarity
Active site4771Proton acceptor By similarity
Binding site1471Substrate By similarity
Binding site1871Substrate By similarity
Binding site1951Substrate By similarity
Binding site3921Substrate By similarity
Binding site3971Substrate By similarity
Binding site4391Substrate By similarity
Binding site5171Substrate By similarity

Amino acid modifications

Modified residue551Phosphoserine Ref.7
Modified residue591Phosphoserine Ref.7
Disulfide bond73 ↔ 511Inhibitory under oxidizing conditions Ref.5

Experimental info

Mutagenesis731C → S: Impaired redox inactivation under oxidizing conditions. Ref.5
Mutagenesis1891C → S: Normal redox inactivation under oxidizing conditions. Ref.5
Mutagenesis2471C → S: Normal redox inactivation under oxidizing conditions. Ref.5
Mutagenesis3021C → S: Normal redox inactivation under oxidizing conditions. Ref.5
Mutagenesis4401C → S: Normal redox inactivation under oxidizing conditions. Ref.5
Mutagenesis4541C → S: Normal redox inactivation under oxidizing conditions. Ref.5
Mutagenesis5111C → S: Impaired redox inactivation under oxidizing conditions. Ref.5
Mutagenesis5471C → S: Normal redox enzyme activation under oxidizing conditions. Ref.5
Sequence conflict4051H → N in BAE98433. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9LIR6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: CDCF1007217789A0

FASTA57563,762
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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].
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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISULFIDE BOND, TRANSIT PEPTIDE CLEAVAGE SITE, 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: cv. Columbia.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_189034.1. NM_113297.2.
UniGeneAt.8278.

3D structure databases

ProteinModelPortalQ9LIR6.
SMRQ9LIR6. Positions 103-538.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G23920.1-P.

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PaxDbQ9LIR6.
PRIDEQ9LIR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G23920.1; AT3G23920.1; AT3G23920.
GeneID821975.
KEGGath:AT3G23920.

Organism-specific databases

TAIRAT3G23920.

Phylogenomic databases

eggNOGNOG77898.
HOGENOMHOG000238755.
InParanoidQ9LIR6.
KOK01177.
OMAFMSWYSQ.
PhylomeDBQ9LIR6.

Enzyme and pathway databases

BioCycMetaCyc:AT3G23920-MONOMER.
BRENDA3.2.1.2. 399.

Gene expression databases

GenevestigatorQ9LIR6.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAM1_ARATH
AccessionPrimary (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: June 11, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names