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O65258 (BAM2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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
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 2, chloroplastic
EC=3.2.1.2
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Beta-amylase 9
Gene names
Name:BAM2
Synonyms:BMY9
Ordered Locus Names:At4g00490
ORF Names:F6N23.1
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Low beta-amylase activity. Interacts poorly with starch or other alpha-1,4-glucan. Ref.4 Ref.6

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.4 Ref.5.

Induction

Slightly by cold stress. Ref.3

Disruption phenotype

Normal growth rate and starch breakdown in leaves during the night. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6. Ref.4 Ref.6

Sequence caution

The sequence AAC13634.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80858.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast stroma

Inferred from direct assay. Source: TAIR

   Molecular functionbeta-amylase activity

Inferred from direct assay Ref.4. Source: TAIR

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast Potential
Chain56 – 542487Beta-amylase 2, chloroplastic
PRO_0000393417

Regions

Region466 – 4672Substrate binding By similarity

Sites

Active site2691Proton donor By similarity
Active site4651Proton acceptor By similarity
Binding site1361Substrate By similarity
Binding site1761Substrate By similarity
Binding site1841Substrate By similarity
Binding site3771Substrate By similarity
Binding site3821Substrate By similarity
Binding site4241Substrate By similarity
Binding site5011Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O65258 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 892C9202CD34E1A9

FASTA54261,398
        10         20         30         40         50         60 
MAIRLNHSVI PVSVKLGAPT RVSARSSLPF SVGDWRGVST FSGARPLVLA KVKLRAESTE 

        70         80         90        100        110        120 
EDRVPIDDDD DSTDQLVDEE IVHFEERDFA GTACVPVYVM LPLGVIDMNS EVVEPEELLD 

       130        140        150        160        170        180 
QLRTLKSVNV DGVMVDCWWG IVESHTPQVY NWSGYKKLFQ MIRELGLKIQ VVMSFHECGG 

       190        200        210        220        230        240 
NVGDDVHIQI PEWVREIGQS NPDIYFTDSA GRRNTECLTW GIDKQRVLRG RTALEVYFDY 

       250        260        270        280        290        300 
MRSFRVEFDE FFEEKIIPEI EVGLGPCGEL RYPSYPAQFG WKYPGIGEFQ CYDKYLMNSL 

       310        320        330        340        350        360 
KEAAEVRGHS FWGRGPDNTE TYNSTPHGTG FFRDGGDYDS YYGRFFLNWY SRVLIDHGDR 

       370        380        390        400        410        420 
VLAMANLAFE GTCIAAKLSG IHWWYKTASH AAELTAGFYN SSNRDGYGPI AAMFKKHDAA 

       430        440        450        460        470        480 
LNFTCVELRT LDQHEDFPEA LADPEGLVWQ VLNAAWDASI PVASENALPC YDREGYNKIL 

       490        500        510        520        530        540 
ENAKPLTDPD GRHLSCFTYL RLNPTLMESQ NFKEFERFLK RMHGEAVPDL GLAPGTQETN 


PE

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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: INDUCTION BY COLD.
[4]"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.
[5]"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
PLoS ONE 3:E1994-E1994(2008) [PubMed: 18431481] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF058919 Genomic DNA. Translation: AAC13634.1. Sequence problems.
AL161472 Genomic DNA. Translation: CAB80858.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE81889.1.
IPIIPI00525144.
PIRT01213.
RefSeqNP_191958.3. NM_116273.4.
UniGeneAt.27432.
At.68473.

3D structure databases

HSSPHSSP built from PDB template 1B1Y based on UniProtKB P16098.
ProteinModelPortalO65258.
SMRO65258. Positions 92-542.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PRIDEO65258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G00490.1; AT4G00490.1; AT4G00490.
GeneID827959.
GenomeReviewsGene locus AT4G00490 in contig CT486007_GR.
KEGGath:AT4G00490.

Organism-specific databases

TAIRAt4g00490.

Phylogenomic databases

eggNOGNOG77898.
GeneTreeEPGT00070000029015.
HOGENOMHBG747772.
InParanoidO65258.
ProtClustDBCLSN2920283.

Gene expression databases

ArrayExpressO65258.
GenevestigatorO65258.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAM2_ARATH
AccessionPrimary (citable) accession number: O65258
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 20, 2010
Last modified: January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents