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Entry version 55 (02 Jun 2021)
Sequence version 1 (23 Sep 2008)
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Protein

Mannan endo-1,4-beta-mannosidase

Gene
N/A
Organism
Cryptopygus antarcticus (Antarctic springtail)
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

Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Has high activity toward locust bean gum (PubMed:18579426, PubMed:25082572).

Also active toward konjac and beta-1,4-mannan. Hydrolyzes mannotetraose (M4) and mannopentaose (M5) to mannobiose (M2) and mannotriose (M3) with a little production of mannose (M1). Hydrolyzes beta-1,4-mannan to M2, M3 and M4. Hardly hydrolyzes M2 and M3. Does not hydrolyze p-nitrophenyl-beta-D-mannopyranoside, gua-gum, carboxymethyl cellulose, soluble starch or laminarin (PubMed:18579426).

2 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

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

Activated particularly by Ca2+ and Zn2+, and to a lesser extent by Na+, K+, Mg2+ and Cu2+. Activation effect of the divalent metal ions Ca2+, Zn2+, Mg2+ and Cu2+ is reduced significantly by the addition of EDTA. Strongly inhibited by Mn2+, Hg2+ and Ag+.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

kcat is 1659.90 sec(-1) for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate).1 Publication
  1. KM=5.61 mg/ml for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate)1 Publication
  1. Vmax=2477.22 mol/min/mg enzyme with 0.5% locust bean gum as substrate (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate)1 Publication

pH dependencei

Optimum pH is 3.5. Maintains more than 50% of the maximum activity at pH 2.5-6.0. Not active at a pH above 7.0.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius. Retains approximately 20-40% of its maximum activity even at 0-5 degrees Celsius. Drastic loss of activity at temperatures above 45 degrees Celsius, at which the half-life of the enzyme activity is less than 10 min.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei83SubstrateCombined sources1 Publication1
Binding sitei144SubstrateCombined sources1 Publication1
Binding sitei180SubstrateCombined sources1 Publication1
<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 sitei181Proton donor/acceptorBy similarity1
Binding sitei187SubstrateCombined sources1 Publication1
Binding sitei204SubstrateCombined sources1 Publication1
Binding sitei208SubstrateCombined sources1 Publication1
Binding sitei243SubstrateCombined sources1 Publication1
Binding sitei282SubstrateCombined sources1 Publication1
Binding sitei284SubstrateCombined sources1 Publication1
Active sitei312NucleophileBy similarity1
Binding sitei341SubstrateCombined sources1 Publication1
Binding sitei348Substrate; via carbonyl oxygenCombined sources1 Publication1

<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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.78, 11159

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH5, Glycoside Hydrolase Family 5

<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:
Mannan endo-1,4-beta-mannosidaseCurated (EC:3.2.1.783 PublicationsImported)
Alternative name(s):
Beta-mannanase1 Publication
CaMan4 Publications
Endo-beta-1,4-D-mannanase2 Publications
<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>OrganismiCryptopygus antarcticus (Antarctic springtail)Imported
<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 identifieri187623 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaCollembolaEntomobryomorphaIsotomoideaIsotomidaeAnurophorinaeCryptopygusCryptopygus antarcticus complex

<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

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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Potential use in mannan-hydrolysis industries which need especially low temperature and an acidic condition such as the food and the animal feed industries.1 Publication

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>Mutagenesisi243W → F: 2.5-fold reduction in substrate affinity and minor reduction in substrate turnover compared to the wild-type. 1 Publication1
Mutagenesisi284H → A: Slight reduction in substrate affinity and minor reduction in substrate turnover compared to the wild-type. 1 Publication1
Mutagenesisi284H → W: About 1.4-fold increase in substrate affinity, but 1.5-fold reduction in substrate turnover compared to the wild-type. 1 Publication1
Mutagenesisi341W → F: 2-fold reduction in substrate affinity and 10-fold reduction in substrate turnover compared to the wild-type. 1 Publication1
Mutagenesisi346 – 350Missing : Optimum temperature is increased by 5 degrees Celsius compared to the wild-type. Exhibits approximately half of its Vmax at 0-30 degrees Celsius. No significant difference in substrate affinity, but nearly 2-fold reduction in substrate turnover compared to the wild-type. Requires 1.8 kcalmol(-1) higher activation enthalpy than the wild-type. 1 Publication5

<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 – 19Sequence analysisAdd BLAST19
<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_500282836320 – 382Mannan endo-1,4-beta-mannosidaseSequence analysisAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi195 ↔ 262Combined sources1 Publication
Disulfide bondi317 ↔ 349Combined sources1 Publication

Keywords - PTMi

Disulfide bond

<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

Monomer.

2 Publications

<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

1382
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
B4XC07

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Regioni147 – 151Substrate bindingCombined sources1 Publication5
Regioni346 – 350Involved in stabilization of the transition state1 Publication5

<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

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017853, Glycoside_hydrolase_SF

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>. 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.

B4XC07-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVKLFSFLLL VWVASPAFSS EFLKASGSNF YYGGQKVFLS GVNFAWRSYG
60 70 80 90 100
SDFGNGQYAS NGPALKDWIN KVKASGGNTA RVWVHVEGQV SPAFDSHGFV
110 120 130 140 150
TSTDSKKTLI NDLSDLLDYA NGQNVFLILV LFNGALQNNS NVQNLFWDES
160 170 180 190 200
KLNSYINNAL TPMVNALKSK PSLAAWEVLN EPEGTLQPGS DQNSCYDTST
210 220 230 240 250
LAAQGAGWGG KKFPMKQILK TINWISSAIH NADSKALVTV GSWSELTQTD
260 270 280 290 300
SFGYRNHYKD SCLTGAGGKS NGIINFYQMH TYSHSGKWNQ NAPFKVNRWA
310 320 330 340 350
YNVNDKPLLI GEFASVCSQN EGIQNLYKYA YNNGYNGALT WQFNSGGDCS
360 370 380
DTYSNQMYGM QALKGQNDQS GGKGGMVSVN IN
Length:382
Mass (Da):41,833
Last modified:September 23, 2008 - 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:i9521BA15DED63968
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EU021047 mRNA Translation: ABV68808.1

<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
EU021047 mRNA Translation: ABV68808.1

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
4OOUX-ray2.36A/B1-382[»]
4OOZX-ray2.60A/B1-382[»]
SMRiB4XC07
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGH5, Glycoside Hydrolase Family 5

Enzyme and pathway databases

BRENDAi3.2.1.78, 11159

Family and domain databases

InterProiView protein in InterPro
IPR017853, Glycoside_hydrolase_SF
SUPFAMiSSF51445, SSF51445, 1 hit

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 nameiMANA_CRYAT
<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: B4XC07
<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: August 12, 2020
Last sequence update: September 23, 2008
Last modified: June 2, 2021
This is version 55 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)

<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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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