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Entry version 57 (08 May 2019)
Sequence version 1 (01 Jun 2003)
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Protein

Intracellular exo-alpha-(1->5)-L-arabinofuranosidase

Gene

abfB

Organism
Bifidobacterium longum
Status
Reviewed-Annotation score:

Annotation score:4 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 cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It is active with sugar beet arabinan and wheat arabinoxylan. It also exhibited activity against alpha-(1->5)-linked arabinobiose, arabinotriose, arabinotetraose, and arabinopentaose.1 Publication

<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

  • Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.1 Publication EC:3.2.1.55

<p>This subsection of the ‘Function’ 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

Completely inhibited by Hg2+ and Cu2+ ions, whereas 1 mM Zn2+ inhibited activity by 51%.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>Kineticsi

  1. KM=0.295 mM for p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf)(at pH 6 and 45 degrees Celsius)1 Publication
  1. Vmax=0.83 µmol/min/mg enzyme with arabinan as substrate (at pH 6 and 45 degrees Celsius)1 Publication
  2. Vmax=1.22 µmol/min/mg enzyme with arabinoxylan as substrate (at pH 6 and 45 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6. The enzyme retains full activity at pH values from 5.5 to 7.5. After exposure to pH 4.5, the activity is reduced by 40%, and no residual activity is detected at pH values below 4.5 or above 7.5.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. The enzymatic activity decreases significantly at temperatures below 35 degrees Celsius and above 60 degrees Celsius, although considerable levels of activity are still detected at 20 and 70 degrees Celsius.1 Publication

<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 ‘Function’ 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 sitei69SubstrateBy similarity1
Binding sitei114Substrate; via amide nitrogenBy similarity1
<p>This subsection of the ‘Function’ 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 sitei215Proton donor/acceptorBy similarity1
Binding sitei286SubstrateBy similarity1
Active sitei340NucleophileBy similarity1
Binding sitei340SubstrateBy 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>Sitei344Important for substrate recognitionBy similarity1
Binding sitei409SubstrateBy similarity1
Sitei409Important for substrate recognitionBy 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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.55 851

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q841V6

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

More...
UniPathwayi
UPA00667

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH51 Glycoside Hydrolase Family 51

<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:
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
ABF
Alternative name(s):
Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase
Short name:
Arabinosidase
<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:abfB
<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>OrganismiBifidobacterium longum
<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 identifieri216816 [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 lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium

<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

  • Cytoplasm 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004221271 – 566Intracellular exo-alpha-(1->5)-L-arabinofuranosidaseAdd BLAST566

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q841V6

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer; trimer of dimers.1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
216816.GS08_02725

<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

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SMRi
Q841V6

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Regioni214 – 215Substrate 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 51 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CZZ Bacteria
COG3534 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010720 Alpha-L-AF_C
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06964 Alpha-L-AF_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00813 Alpha-L-AF_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 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>.<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.

Q841V6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTHNSQYSA ETTHPDKQES SPAPTAAGTT ASNVSTTGNA TTPDASIALN
60 70 80 90 100
ADATPVADVP PRLFGSFVEH LGRCVYGGIY EPSHPTADEN GFRQDVLDLV
110 120 130 140 150
KELGVTCVRY PGGNFVSNYN WEDGIGPREN RPMRRDLAWH CTETNEMGID
160 170 180 190 200
DFYRWSQKAG TEIMLAVNMG TRGLKAALDE LEYVNGAPGT AWADQRVANG
210 220 230 240 250
IEEPMDIKMW CIGNEMDGPW QVGHMSPEEY AGAVDKVAHA MKLAESGLEL
260 270 280 290 300
VACGSSGAYM PTFGTWEKTV LTKAYENLDF VSCHAYYFDR GHKTRAAASM
310 320 330 340 350
QDFLASSEDM TKFIATVSDA ADQAREANNG TKDIALSFDE WGVWYSDKWN
360 370 380 390 400
EQEDQWKAEA AQGLHHEPWP KSPHLLEDIY TAADAVVEGS LMITLLKHCD
410 420 430 440 450
RVRSASRAQL VNVIAPIMAE EHGPAWRQTT FYPFAEAALH ARGQAYAPAI
460 470 480 490 500
SSPTIHTEAY GDVPAIDAVV TWDEQARTGL LLAVNRDANT PHTLTIDLSG
510 520 530 540 550
LPGLPGLGTL ALGKAQLLHE DDPYRTNTAE APEAVTPQPL DIAMNATGTC
560
TATLPAISWI SVEFHG
Length:566
Mass (Da):61,548
Last modified:June 1, 2003 - 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:iACF964B9B6C0DFBC
GO

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
AY259087 Genomic DNA Translation: AAO84266.1

NCBI Reference Sequences

More...
RefSeqi
WP_013410312.1, NZ_QSPR01000001.1

<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
AY259087 Genomic DNA Translation: AAO84266.1
RefSeqiWP_013410312.1, NZ_QSPR01000001.1

3D structure databases

SMRiQ841V6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216816.GS08_02725

Protein family/group databases

CAZyiGH51 Glycoside Hydrolase Family 51

Proteomic databases

PRIDEiQ841V6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CZZ Bacteria
COG3534 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00667

BRENDAi3.2.1.55 851
SABIO-RKiQ841V6

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR010720 Alpha-L-AF_C
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF06964 Alpha-L-AF_C, 1 hit
SMARTiView protein in SMART
SM00813 Alpha-L-AF_C, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiIABF_BIFLN
<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: Q841V6
<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: May 1, 2013
Last sequence update: June 1, 2003
Last modified: May 8, 2019
This is version 57 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 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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