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Protein

Beta-amylase 5

Gene

BAM5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Beta-amylase activity. Major cytosolic beta-amylase isoform in rosette leaves and inflorescences stems.1 Publication

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561SubstrateBy similarity
Binding sitei96 – 961SubstrateBy similarity
Binding sitei104 – 1041SubstrateBy similarity
Active sitei189 – 1891Proton donorPROSITE-ProRule annotation
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei303 – 3031SubstrateBy similarity
Binding sitei345 – 3451SubstrateBy similarity
Active sitei383 – 3831Proton acceptorPROSITE-ProRule annotation
Binding sitei423 – 4231SubstrateBy similarity

GO - Molecular functioni

  • beta-amylase activity Source: TAIR

GO - Biological processi

  • response to herbivore Source: TAIR
  • starch catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyciARA:GQT-1125-MONOMER.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-amylase 5 (EC:3.2.1.2)
Short name:
AtBeta-Amy
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Protein REDUCED BETA AMYLASE 1
Gene namesi
Name:BAM5
Synonyms:BMY1, RAM1
Ordered Locus Names:At4g15210
ORF Names:dl3650c, FCAALL.97
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G15210.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Present in the continuous phloem cytoplasm.

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Almost complete loss of beta-amylase activity in rosette leaves and inflorescences (stems).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Beta-amylase 5PRO_0000153932Add
BLAST

Proteomic databases

PaxDbiP25853.
PRIDEiP25853.

PTM databases

iPTMnetiP25853.

Expressioni

Tissue specificityi

Detected in phloem sieve elements.1 Publication

Inductioni

Circadian-regulated, with a peak in expression just before the light period in short day conditions.

Gene expression databases

GenevisibleiP25853. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G15210.1.

Structurei

3D structure databases

ProteinModelPortaliP25853.
SMRiP25853. Positions 9-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni384 – 3852Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

Phylogenomic databases

eggNOGiENOG410IJER. Eukaryota.
ENOG410XNXS. LUCA.
HOGENOMiHOG000238755.
InParanoidiP25853.
OMAiYADYMKS.
PhylomeDBiP25853.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25853-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MATNYNEKLL LNYVPVYVML PLGVVNVENV FADPETLETQ LKRLKEEAGV
60 70 80 90 100
DGVMVDVWWG IIESKGPKQY DWTAYKTLFQ LIARLGLKIQ AIMSFHQCGG
110 120 130 140 150
NVGDIVTIPI PQWVRDVGDN DPDIYYTNRK GTRDIEYLSI GVDNLPLFAG
160 170 180 190 200
RTAVQLYSDY MSSFKENMAD LIEAGVIVDI EVGLGPAGEL RYPSYPQSQG
210 220 230 240 250
WVFPGIGEFQ CYDKYLKKDF KEAAAKAGHP EWDLPEDAGE YNDKPEETGF
260 270 280 290 300
FKKDGTYVSE KGKFFMTWYS NKLIFHGDQI LGEANKIFAG LKVNLAAKVS
310 320 330 340 350
GIHWLYNHHS HAAELTAGYY NLFKRDGYRP IARMLSKHYG ILNFTCLEMK
360 370 380 390 400
DTDNTAEALS APQELVQEVL SKAWKEGIEV AGENALETYG AKGYNQILLN
410 420 430 440 450
ARPNGVNPNG KPKLRMYGFT YLRLSDTVFQ ENNFELFKKL VRKMHADQDY
460 470 480 490
CGDAAKYGHE IVPLKTSNSQ LTLEDIADAA QPSGAFKWDS ETDLKVDG
Length:498
Mass (Da):56,063
Last modified:May 1, 1992 - v1
Checksum:i0589DE69CD825C64
GO
Isoform 2 (identifier: P25853-2) [UniParc]FASTAAdd to basket

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

Show »
Length:420
Mass (Da):47,301
Checksum:i96B8932F1556FFE7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551Q → QV in CAB10300 (PubMed:9461215).Curated
Sequence conflicti155 – 1551Q → QV in CAB78563 (PubMed:10617198).Curated
Sequence conflicti486 – 4861F → L in BAA07842 (PubMed:7716246).Curated
Sequence conflicti486 – 4861F → L in AAB34026 (PubMed:7716246).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei411 – 42010KPKLRMYGFT → LLWRRSEVRA in isoform 2. 1 PublicationVSP_038978
Alternative sequencei421 – 49878Missing in isoform 2. 1 PublicationVSP_038979Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB71416. S36094.
RefSeqiNP_567460.1. NM_117609.2. [P25853-1]
NP_849389.1. NM_179058.1. [P25853-2]
UniGeneiAt.25187.

Genome annotation databases

EnsemblPlantsiAT4G15210.1; AT4G15210.1; AT4G15210. [P25853-1]
GeneIDi827185.
KEGGiath:AT4G15210.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB71416. S36094.
RefSeqiNP_567460.1. NM_117609.2. [P25853-1]
NP_849389.1. NM_179058.1. [P25853-2]
UniGeneiAt.25187.

3D structure databases

ProteinModelPortaliP25853.
SMRiP25853. Positions 9-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G15210.1.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

PTM databases

iPTMnetiP25853.

Proteomic databases

PaxDbiP25853.
PRIDEiP25853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G15210.1; AT4G15210.1; AT4G15210. [P25853-1]
GeneIDi827185.
KEGGiath:AT4G15210.

Organism-specific databases

TAIRiAT4G15210.

Phylogenomic databases

eggNOGiENOG410IJER. Eukaryota.
ENOG410XNXS. LUCA.
HOGENOMiHOG000238755.
InParanoidiP25853.
OMAiYADYMKS.
PhylomeDBiP25853.

Enzyme and pathway databases

BioCyciARA:GQT-1125-MONOMER.

Miscellaneous databases

PROiP25853.

Gene expression databases

GenevisibleiP25853. AT.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSiPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiBAM5_ARATH
AccessioniPrimary (citable) accession number: P25853
Secondary accession number(s): O23375, Q0WWJ7, Q3EA19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: January 20, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.