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Reviewed, UniProtKB/Swiss-Prot P25853 (AMYB_ARATH)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-amylase
    EC=3.2.1.2
Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
Gene names
Name: BMY1
Ordered Locus Names: At4g15210
ORF Names: dl3650c
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

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.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Coding sequence diversityAlternative splicing
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processresponse to herbivore

Inferred from expression pattern. Source: TAIR

starch catabolic process Ref.2

Inferred from direct assay. Source: TAIR

   Molecular functionbeta-amylase activity Ref.2

Inferred from direct assay. Source: TAIR

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Beta-amylase
PRO_0000153932

Sites

Active site1891 By similarity
Active site3831 By similarity

Experimental info

Sequence conflict1551Q → QV Ref.3
Sequence conflict1551Q → QV Ref.4
Sequence conflict4861F → L in BAA07842. Ref.2
Sequence conflict4861F → L in AAB34026. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0589DE69CD825C64

FASTA49856,063
        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

« Hide

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References

« Hide '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: 16668593] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 7716246] [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. expand/collapse author list , 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.
[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. 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.
[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. 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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

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Cross-references

Sequence databases

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.
AF424573 mRNA. Translation: AAL11567.1.
AY142024 mRNA. Translation: AAM98288.1.
IPIIPI00532891.
PIRS36094. B71416.
RefSeqNP_567460.1.
UniGeneAt.25187

3D structure databases

HSSPHSSP built from PDB template 1BTC based on UniProtKB P10538.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PRIDEP25853.

Genome annotation databases

GeneID827185.
GenomeReviewsGene locus AT4G15210 in contig CT486007_GR.
KEGGath:AT4G15210.

Organism-specific databases

TAIRAt4g15210.

Phylogenomic databases

OMAP25853. KMHADQD.

Enzyme and pathway databases

BRENDA3.2.1.2. 302.

Gene expression databases

ArrayExpressP25853.

Family and domain databases

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

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Entry information

Entry nameAMYB_ARATH
AccessionPrimary (citable) accession number: P25853
Secondary accession number(s): O23375
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents