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Entry version 114 (16 Oct 2019)
Sequence version 3 (07 Jul 2009)
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Protein

Extracellular endo-alpha-(1->5)-L-arabinanase 1

Gene

abnA

Organism
Bacillus subtilis (strain 168)
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

Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p-nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substituted.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.1 Publication EC:3.2.1.99

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+CuratedNote: Binds 1 Ca2+ ion per subunit.Curated

<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>Kineticsi

  1. KM=3.5 mM for arabinotetraose (at 27 degrees Celsius and pH 7)2 Publications
  2. KM=5.92 mM for linear 1,5-alpha-L-arabinan (at 37 degrees Celsius and pH 6.6)2 Publications
  1. Vmax=1.31 mmol/min/mg enzyme (at 37 degrees Celsius and pH 6.6)2 Publications

pH dependencei

Optimum pH is 6.0. At pH 4.0 the arabinosidase retains about 8% of activity.2 Publications

Temperature dependencei

Optimum temperature is 60 degrees Celsius. At 80 degrees Celsius retains about 2% of activity.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei44Proton acceptor1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei44SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi107CalciumSequence analysis1
Binding sitei125Substrate; via amide nitrogenBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei163Important for catalytic activity, responsible for pKa modulation of the active site Glu and correct orientation of both the proton donor and substrate1 Publication1
Metal bindingi165CalciumSequence analysis1
Active sitei215Proton donor1 Publication1
Metal bindingi287CalciumSequence analysis1

<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
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU28810-MONOMER
MetaCyc:BSU28810-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P94522

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00667

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH43 Glycoside Hydrolase Family 43

<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_and_taxonomy_section">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:
Extracellular endo-alpha-(1->5)-L-arabinanase 1 (EC:3.2.1.99)
Short name:
ABN
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:abnA
Ordered Locus Names:BSU28810
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<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

Cells lacking this gene retains about 40% of the capacity to hydrolyze linear arabinan compared to the wild-type.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi43H → A: Decrease in binding affinity. 1 Publication1
Mutagenesisi44D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi104W → A: Significantly less active (10000-fold) than the wild-type arabinanase against both linear arabinan and arabinooligosaccharides. 1 Publication1
Mutagenesisi124F → A: Increase in binding affinity. 1 Publication1
Mutagenesisi163D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi181F → A: Significantly less active than the wild-type arabinanase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). 1 Publication1
Mutagenesisi182W → A: Same binding affinity as wild-type. 1 Publication1
Mutagenesisi215E → A: Loss of arabinanase activity. 2 Publications1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 321 PublicationAdd BLAST32
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000036043733 – 323Extracellular endo-alpha-(1->5)-L-arabinanase 1Add BLAST291

Proteomic databases

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

More...
PaxDbi
P94522

PRoteomics IDEntifications database

More...
PRIDEi
P94522

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by arabinose and arabina,n and repressed by glucose.1 Publication

<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
224308.BSU28810

<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

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P94522

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P94522

<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>Regioni160 – 163Substrate bindingBy similarity4
Regioni180 – 182Substrate bindingBy similarity3

<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 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107PMW Bacteria
COG3507 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000292006

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P94522

KEGG Orthology (KO)

More...
KOi
K06113

Identification of Orthologs from Complete Genome Data

More...
OMAi
FYIEDGG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P94522

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.115.10.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006710 Glyco_hydro_43
IPR016840 Glyco_hydro_43_endo_a_Ara-ase
IPR023296 Glyco_hydro_beta-prop_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04616 Glyco_hydro_43, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF026534 Endo_alpha-L-arabinosidase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF75005 SSF75005, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P94522-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE
60 70 80 90 100
GSSWYALGTG LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG
110 120 130 140 150
QNQWAPDIQY YNGKYWLYYS VSSFGSNTSA IGLASSTSIS SGGWKDEGLV
160 170 180 190 200
IRSTSSNNYN AIDPELTFDK DGNPWLAFGS FWSGIKLTKL DKSTMKPTGS
210 220 230 240 250
LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN STYKIAYGRS
260 270 280 290 300
KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD
310 320
ANDNGIPKLL INDLNWSSGW PSY
Length:323
Mass (Da):35,446
Last modified:July 7, 2009 - v3
<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:i0105FB280E83BC69
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA99586 differs from that shown. Reason: Frameshift.Curated

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 conflicti172G → D in CAA99586 (PubMed:8969504).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
Z75208 Genomic DNA Translation: CAA99586.1 Frameshift.
AY669857 Genomic DNA Translation: AAV87172.1
AL009126 Genomic DNA Translation: CAB14841.2

Protein sequence database of the Protein Information Resource

More...
PIRi
E69580

NCBI Reference Sequences

More...
RefSeqi
NP_390759.2, NC_000964.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB14841; CAB14841; BSU28810

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
937430

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU28810

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.3129

<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
Z75208 Genomic DNA Translation: CAA99586.1 Frameshift.
AY669857 Genomic DNA Translation: AAV87172.1
AL009126 Genomic DNA Translation: CAB14841.2
PIRiE69580
RefSeqiNP_390759.2, NC_000964.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UV4X-ray1.50A31-323[»]
SMRiP94522
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU28810

Protein family/group databases

CAZyiGH43 Glycoside Hydrolase Family 43

Proteomic databases

PaxDbiP94522
PRIDEiP94522

Genome annotation databases

EnsemblBacteriaiCAB14841; CAB14841; BSU28810
GeneIDi937430
KEGGibsu:BSU28810
PATRICifig|224308.179.peg.3129

Phylogenomic databases

eggNOGiENOG4107PMW Bacteria
COG3507 LUCA
HOGENOMiHOG000292006
InParanoidiP94522
KOiK06113
OMAiFYIEDGG
PhylomeDBiP94522

Enzyme and pathway databases

UniPathwayiUPA00667
BioCyciBSUB:BSU28810-MONOMER
MetaCyc:BSU28810-MONOMER
SABIO-RKiP94522

Miscellaneous databases

EvolutionaryTraceiP94522

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR006710 Glyco_hydro_43
IPR016840 Glyco_hydro_43_endo_a_Ara-ase
IPR023296 Glyco_hydro_beta-prop_sf
PfamiView protein in Pfam
PF04616 Glyco_hydro_43, 1 hit
PIRSFiPIRSF026534 Endo_alpha-L-arabinosidase, 1 hit
SUPFAMiSSF75005 SSF75005, 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 nameiEABN1_BACSU
<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: P94522
Secondary accession number(s): Q5MPF4, Q795W7
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: October 16, 2019
This is version 114 of the entry and version 3 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 programProkaryotic 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  5. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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