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Q9LIR6

- BAM1_ARATH

UniProt

Q9LIR6 - BAM1_ARATH

Protein

Beta-amylase 1, chloroplastic

Gene

BAM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    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.3 Publications

    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.

    Enzyme regulationi

    Redox regulation; active in reducing conditions, inactive in oxidizing conditions. Thioredoxins f1, m1, and y1 mediate the reversible reductive activation of oxidized BAM1.1 Publication

    pH dependencei

    Optimum pH is 6-8.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471SubstrateBy similarity
    Binding sitei187 – 1871SubstrateBy similarity
    Binding sitei195 – 1951SubstrateBy similarity
    Active sitei279 – 2791Proton donorPROSITE-ProRule annotation
    Binding sitei392 – 3921SubstrateBy similarity
    Binding sitei397 – 3971SubstrateBy similarity
    Binding sitei439 – 4391SubstrateBy similarity
    Active sitei477 – 4771Proton acceptorPROSITE-ProRule annotation
    Binding sitei517 – 5171SubstrateBy similarity

    GO - Molecular functioni

    1. beta-amylase activity Source: TAIR

    GO - Biological processi

    1. response to water deprivation Source: TAIR
    2. starch catabolic process Source: TAIR

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:AT3G23920-MONOMER.
    BRENDAi3.2.1.2. 399.

    Protein family/group databases

    CAZyiGH14. Glycoside Hydrolase Family 14.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:BAM1
    Synonyms:BMY7, TRBAMY
    Ordered Locus Names:At3g23920
    ORF Names:F14O13.12
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G23920.

    Subcellular locationi

    Plastidchloroplast 2 Publications

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell
    2. cytosol Source: TAIR
    3. nucleus Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    Normal growth rate and starch breakdown in leaves during the night.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731C → S: Impaired redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi189 – 1891C → S: Normal redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi247 – 2471C → S: Normal redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi302 – 3021C → S: Normal redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi440 – 4401C → S: Normal redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi454 – 4541C → S: Normal redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi511 – 5111C → S: Impaired redox inactivation under oxidizing conditions. 1 Publication
    Mutagenesisi547 – 5471C → S: Normal redox enzyme activation under oxidizing conditions. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4141Chloroplast1 PublicationAdd
    BLAST
    Chaini42 – 575534Beta-amylase 1, chloroplasticPRO_0000393416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551Phosphoserine1 Publication
    Modified residuei59 – 591Phosphoserine1 Publication
    Disulfide bondi73 ↔ 511Inhibitory under oxidizing conditions1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    PaxDbiQ9LIR6.
    PRIDEiQ9LIR6.

    Expressioni

    Tissue specificityi

    Expressed in leaves, roots, flowers, pollen, and seeds.1 Publication

    Gene expression databases

    GenevestigatoriQ9LIR6.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G23920.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LIR6.
    SMRiQ9LIR6. Positions 103-538.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni478 – 4792Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 14 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG77898.
    HOGENOMiHOG000238755.
    InParanoidiQ9LIR6.
    KOiK01177.
    OMAiFMSWYSQ.
    PhylomeDBiQ9LIR6.

    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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9LIR6-1 [UniParc]FASTAAdd to Basket

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    MALNLSHQLG VLAGTPIKSG EMTDSSLLSI SPPSARMMTP KAMNRNYKAH    50
    GTDPSPPMSP ILGATRADLS VACKAFAVEN GIGTIEEQRT YREGGIGGKK 100
    EGGGGVPVFV MMPLDSVTMG NTVNRRKAMK ASLQALKSAG VEGIMIDVWW 150
    GLVEKESPGT YNWGGYNELL ELAKKLGLKV QAVMSFHQCG GNVGDSVTIP 200
    LPQWVVEEVD KDPDLAYTDQ WGRRNHEYIS LGADTLPVLK GRTPVQCYAD 250
    FMRAFRDNFK HLLGETIVEI QVGMGPAGEL RYPSYPEQEG TWKFPGIGAF 300
    QCYDKYSLSS LKAAAETYGK PEWGSTGPTD AGHYNNWPED TQFFKKEGGG 350
    WNSEYGDFFL SWYSQMLLDH GERILSSAKS IFENMGVKIS VKIAGIHWHY 400
    GTRSHAPELT AGYYNTRFRD GYLPIAQMLA RHNAIFNFTC IEMRDHEQPQ 450
    DALCAPEKLV NQVALATLAA EVPLAGENAL PRYDDYAHEQ ILKASALNLD 500
    QNNEGEPREM CAFTYLRMNP ELFQADNWGK FVAFVKKMGE GRDSHRCREE 550
    VEREAEHFVH VTQPLVQEAA VALTH 575
    Length:575
    Mass (Da):63,762
    Last modified:October 1, 2000 - v1
    Checksum:iCDCF1007217789A0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti405 – 4051H → N in BAE98433. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_189034.1. NM_113297.2.
    UniGeneiAt.8278.

    Genome annotation databases

    EnsemblPlantsiAT3G23920.1; AT3G23920.1; AT3G23920.
    GeneIDi821975.
    KEGGiath:AT3G23920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_189034.1. NM_113297.2.
    UniGenei At.8278.

    3D structure databases

    ProteinModelPortali Q9LIR6.
    SMRi Q9LIR6. Positions 103-538.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G23920.1-P.

    Protein family/group databases

    CAZyi GH14. Glycoside Hydrolase Family 14.

    Proteomic databases

    PaxDbi Q9LIR6.
    PRIDEi Q9LIR6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G23920.1 ; AT3G23920.1 ; AT3G23920 .
    GeneIDi 821975.
    KEGGi ath:AT3G23920.

    Organism-specific databases

    TAIRi AT3G23920.

    Phylogenomic databases

    eggNOGi NOG77898.
    HOGENOMi HOG000238755.
    InParanoidi Q9LIR6.
    KOi K01177.
    OMAi FMSWYSQ.
    PhylomeDBi Q9LIR6.

    Enzyme and pathway databases

    BioCyci MetaCyc:AT3G23920-MONOMER.
    BRENDAi 3.2.1.2. 399.

    Gene expression databases

    Genevestigatori Q9LIR6.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001554. Glyco_hydro_14.
    IPR018238. Glyco_hydro_14_CS.
    IPR001371. Glyco_hydro_14B_pln.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01373. Glyco_hydro_14. 1 hit.
    [Graphical view ]
    PRINTSi PR00750. BETAAMYLASE.
    PR00842. GLHYDLASE14B.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
    PS00679. BETA_AMYLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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].

    Entry informationi

    Entry nameiBAM1_ARATH
    AccessioniPrimary (citable) accession number: Q9LIR6
    Secondary accession number(s): Q0WWR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 20, 2010
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 96 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

    External Data

    Dasty 3