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Entry version 130 (12 Aug 2020)
Sequence version 1 (01 Oct 2000)
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Protein

Beta-amylase 1, chloroplastic

Gene

BAM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>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. EC:3.2.1.2

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 6-8.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei147SubstrateBy similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei195SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei279Proton donorPROSITE-ProRule annotation1
Binding sitei392SubstrateBy similarity1
Binding sitei397SubstrateBy similarity1
Binding sitei439SubstrateBy similarity1
Active sitei477Proton acceptorPROSITE-ProRule annotation1
Binding sitei517SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:AT3G23920-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.2, 399

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH14, Glycoside Hydrolase Family 14

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:BAM1
Synonyms:BMY7, TRBAMY
Ordered Locus Names:At3g23920
ORF Names:F14O13.12
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT3G23920

The Arabidopsis Information Resource

More...
TAIRi
locus:2076086, AT3G23920

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi73C → S: Impaired redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi189C → S: Normal redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi247C → S: Normal redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi302C → S: Normal redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi440C → S: Normal redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi454C → S: Normal redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi511C → S: Impaired redox inactivation under oxidizing conditions. 1 Publication1
Mutagenesisi547C → S: Normal redox enzyme activation under oxidizing conditions. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 41Chloroplast1 PublicationAdd BLAST41
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000039341642 – 575Beta-amylase 1, chloroplasticAdd BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei55PhosphoserineCombined sources1
Modified residuei59PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi73 ↔ 511Inhibitory under oxidizing conditions1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9LIR6

PRoteomics IDEntifications database

More...
PRIDEi
Q9LIR6

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
240813

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9LIR6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9LIR6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9LIR6, AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3702.AT3G23920.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9LIR6

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni478 – 479Substrate bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QTBX, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016754_1_1_1

KEGG Orthology (KO)

More...
KOi
K01177

Identification of Orthologs from Complete Genome Data

More...
OMAi
GEYNWSA

Database of Orthologous Groups

More...
OrthoDBi
533202at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9LIR6

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001554, Glyco_hydro_14
IPR018238, Glyco_hydro_14_CS
IPR001371, Glyco_hydro_14B_pln
IPR017853, Glycoside_hydrolase_SF

The PANTHER Classification System

More...
PANTHERi
PTHR31352, PTHR31352, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01373, Glyco_hydro_14, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00750, BETAAMYLASE
PR00842, GLHYDLASE14B

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00506, BETA_AMYLASE_1, 1 hit
PS00679, BETA_AMYLASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LIR6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALNLSHQLG VLAGTPIKSG EMTDSSLLSI SPPSARMMTP KAMNRNYKAH
60 70 80 90 100
GTDPSPPMSP ILGATRADLS VACKAFAVEN GIGTIEEQRT YREGGIGGKK
110 120 130 140 150
EGGGGVPVFV MMPLDSVTMG NTVNRRKAMK ASLQALKSAG VEGIMIDVWW
160 170 180 190 200
GLVEKESPGT YNWGGYNELL ELAKKLGLKV QAVMSFHQCG GNVGDSVTIP
210 220 230 240 250
LPQWVVEEVD KDPDLAYTDQ WGRRNHEYIS LGADTLPVLK GRTPVQCYAD
260 270 280 290 300
FMRAFRDNFK HLLGETIVEI QVGMGPAGEL RYPSYPEQEG TWKFPGIGAF
310 320 330 340 350
QCYDKYSLSS LKAAAETYGK PEWGSTGPTD AGHYNNWPED TQFFKKEGGG
360 370 380 390 400
WNSEYGDFFL SWYSQMLLDH GERILSSAKS IFENMGVKIS VKIAGIHWHY
410 420 430 440 450
GTRSHAPELT AGYYNTRFRD GYLPIAQMLA RHNAIFNFTC IEMRDHEQPQ
460 470 480 490 500
DALCAPEKLV NQVALATLAA EVPLAGENAL PRYDDYAHEQ ILKASALNLD
510 520 530 540 550
QNNEGEPREM CAFTYLRMNP ELFQADNWGK FVAFVKKMGE GRDSHRCREE
560 570
VEREAEHFVH VTQPLVQEAA VALTH
Length:575
Mass (Da):63,762
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCDCF1007217789A0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti405H → N in BAE98433 (Ref. 4) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

NCBI Reference Sequences

More...
RefSeqi
NP_189034.1, NM_113297.3

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT3G23920.1; AT3G23920.1; AT3G23920

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
821975

Gramene; a comparative resource for plants

More...
Gramenei
AT3G23920.1; AT3G23920.1; AT3G23920

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT3G23920

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_113297.3

3D structure databases

SMRiQ9LIR6
ModBaseiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G23920.1

Protein family/group databases

CAZyiGH14, Glycoside Hydrolase Family 14

PTM databases

iPTMnetiQ9LIR6

Proteomic databases

PaxDbiQ9LIR6
PRIDEiQ9LIR6
ProteomicsDBi240813

Genome annotation databases

EnsemblPlantsiAT3G23920.1; AT3G23920.1; AT3G23920
GeneIDi821975
GrameneiAT3G23920.1; AT3G23920.1; AT3G23920
KEGGiath:AT3G23920

Organism-specific databases

AraportiAT3G23920
TAIRilocus:2076086, AT3G23920

Phylogenomic databases

eggNOGiENOG502QTBX, Eukaryota
HOGENOMiCLU_016754_1_1_1
KOiK01177
OMAiGEYNWSA
OrthoDBi533202at2759
PhylomeDBiQ9LIR6

Enzyme and pathway databases

BioCyciMetaCyc:AT3G23920-MONOMER
BRENDAi3.2.1.2, 399

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9LIR6

Gene expression databases

ExpressionAtlasiQ9LIR6, baseline and differential
GenevisibleiQ9LIR6, AT

Family and domain databases

InterProiView protein in InterPro
IPR001554, Glyco_hydro_14
IPR018238, Glyco_hydro_14_CS
IPR001371, Glyco_hydro_14B_pln
IPR017853, Glycoside_hydrolase_SF
PANTHERiPTHR31352, PTHR31352, 1 hit
PfamiView protein in Pfam
PF01373, Glyco_hydro_14, 1 hit
PRINTSiPR00750, BETAAMYLASE
PR00842, GLHYDLASE14B
SUPFAMiSSF51445, SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00506, BETA_AMYLASE_1, 1 hit
PS00679, BETA_AMYLASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBAM1_ARATH
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9LIR6
Secondary accession number(s): Q0WWR5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: October 1, 2000
Last modified: August 12, 2020
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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