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Entry version 112 (02 Jun 2021)
Sequence version 2 (05 Jul 2005)
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Protein

Mannan endo-1,4-beta-mannosidase

Gene

manA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
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

Catalyzes the endo hydrolysis of beta-1,4-linked mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall (PubMed:11382747).

Preferentially hydrolyzes the larger oligosaccharides and has greater activity against non-substituted polysaccharides (PubMed:7848261) (PubMed:8973192).

It displays tight specificity for mannose at both the -2 and the -1 subsites (PubMed:19441796).

Appears to act in synergy with alpha-galactosidase (AgaA) to elicit hydrolysis of galactomannan (PubMed:11064195).

5 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 '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 14.7 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:8973192). Kcat is 20 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:11382747). Kcat is 1759 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:8973192). Kcat is 2904 sec(-1) for mannanase activity with carob galactomannan as substrate (PubMed:11382747). Kcat is 3861 sec(-1) for mannanase activity with mannotetraose as substrate (PubMed:8973192). Kcat is 280000 min(-1) for mannanase activity with galactomannan as substrate (PubMed:19441796). Kcat is 400000 min(-1) for mannanase activity with glucomannan as substrate (PubMed:19441796).3 Publications
  1. KM=0.9 mg/ml for carob galactomannan1 Publication
  2. KM=2.8 mg/ml for glucomannan1 Publication
  3. KM=3.2 mg/ml for galactomannan1 Publication
  4. KM=9.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication
  5. KM=12.3 µM for 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM)1 Publication

pH dependencei

Optimum pH is about 7.0.1 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 sitei121Substrate2 Publications1
Binding sitei143Substrate3 Publications1
Binding sitei162Substrate1 Publication1 Publication1
<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>Sitei211Plays an important role in maintaining the position of the catalytic nucleophile1 Publication1 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 sitei212Proton donor4 Publications1
Binding sitei217Substrate1 Publication1
Binding sitei285Substrate2 Publications1
Active sitei320Nucleophile2 Publications1
Binding sitei377Substrate3 Publications1

<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
CJAP498211:G1GB3-2766-MONOMER

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH26, Glycoside Hydrolase Family 26

<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-mannosidase1 Publication (EC:3.2.1.784 Publications)
Alternative name(s):
Mannanase 26A1 Publication
Short name:
Man26A1 Publication
Mannanase A1 Publication
Short name:
ManA1 Publication
<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:manA1 Publication
Synonyms:man26A
Ordered Locus Names:CJA_2770
<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>OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
<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 identifieri498211 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
<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
  • UP000001036 <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 disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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>Mutagenesisi121E → A: Strong decrease of mannanase activity against both oligosaccharides and polysaccharides. 1 Publication1
Mutagenesisi143H → A: Very low mannanase activity against both mannans and mannooligosaccharides. 1 Publication1
Mutagenesisi156W → A: Similar to the wild-type. 1 Publication1
Mutagenesisi162W → A: The mannanase activity is 95, 70, and 30-fold less active than the wild-type against mannotriose, mannotetraose and mannohexaose, respectively. 1 Publication1
Mutagenesisi211H → A: Causes a 100- and 700-fold decrease in mannanase activity against carob galactomannans and mannotetraose, respectively, but only a 6-fold reduction in mannanase activity against 2,4-DNPM. 1 Publication1
Mutagenesisi212E → A: Causes a dramatic decrease in the catalytic efficiency against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. 2 Publications1
Mutagenesisi212E → D: 10-fold decrease of the catalytic efficiency against 2,4-DNPM. 1 Publication1
Mutagenesisi217W → A: Lack of mannanase activity against both mannotriose and mannotetraose. 1 Publication1
Mutagenesisi278D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
Mutagenesisi278D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
Mutagenesisi283D → A: Retains significant activity against mannotetraose and azo-carob galactomannan. Lack of activity against all substrates; when associated with A-320. 2 Publications1
Mutagenesisi283D → E: Retains significant activity against mannotetraose and azo-carob galactomannan. 1 Publication1
Mutagenesisi285Y → A: Reduction of the catalytic efficiency with carob galactomannan and 2,4-DNPM. 1 Publication1
Mutagenesisi320E → A: Does not alter the affinity against carob galactomannan, azo-carob galactomannan, mannotetraose and 2,4-DNPM. Lack of activity against all substrates; when associated with A-283. 2 Publications1
Mutagenesisi320E → D: Causes a dramatic decrease in the catalytic efficiency against mannotetraose. 1 Publication1
Mutagenesisi320E → G: Lack of activity against all substrates. 2 Publications1
Mutagenesisi360W → A: Lack of activity against all substrates. 1 Publication1
Mutagenesisi361R → A: Strong decrease of mannanase activity against oligosaccharides, while the reduction in the rate of polysaccharide hydrolysis is more modest. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-377. 1 Publication1
Mutagenesisi377H → A: 100-fold decrease in the activity of the mannanase against mannotetraose and 4-nitrophenyl-beta-D-Man2. It hydrolyzes polysaccharides only 10-20-fold less efficiently than the wild-type. Strong decrease of mannanase activity and not able to distinguish between mannose and glucose units; when associated with A-361. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02680, 1,3-Dinitrobenzene
DB03814, 2-(N-morpholino)ethanesulfonic acid
DB04084, 2-deoxy-2-fluoro-Alpha-D-mannose
DB04483, 2-deoxy-2-fluoro-Beta-D-mannose

<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 – 27PROSITE-ProRule annotation1 PublicationAdd BLAST27
<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_000001217328 – 423Mannan endo-1,4-beta-mannosidaseAdd BLAST396

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P49424

<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

Homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
498211.CJA_2770

<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

1423
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
P49424

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
P49424

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini56 – 409GH26PROSITE-ProRule annotationAdd BLAST354

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>Regioni360 – 361Substrate binding3 Publications2

<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 26 family.PROSITE-ProRule annotationCurated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4124, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016930_0_1_6

Identification of Orthologs from Complete Genome Data

More...
OMAi
FGHQDDL

Database of Orthologous Groups

More...
OrthoDBi
669354at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022790, GH26_dom
IPR000805, Glyco_hydro_26
IPR017853, Glycoside_hydrolase_SF

The PANTHER Classification System

More...
PANTHERi
PTHR40079, PTHR40079, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02156, Glyco_hydro_26, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00739, GLHYDRLASE26

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
PS51764, GH26, 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.

P49424-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV
60 70 80 90 100
DSQATMETRS LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA
110 120 130 140 150
VGDFAAVYGW DTLSIVAPKA EGDIVAQVKK AYARGGIITV SSHFDNPKTD
160 170 180 190 200
TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV LNGYLDQVAE WANNLKDEQG
210 220 230 240 250
RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY LRDVKGVRNF
260 270 280 290 300
LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA
310 320 330 340 350
NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD
360 370 380 390 400
AREIAFLLVW RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY
410 420
ADEFTAFNRD IEQVYQRPTL IVK
Length:423
Mass (Da):47,487
Last modified:July 5, 2005 - v2
<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:iEFDAB597F10BA3DD
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
X82179 Genomic DNA Translation: CAA57670.2
CP000934 Genomic DNA Translation: ACE82849.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S53374

NCBI Reference Sequences

More...
RefSeqi
WP_012488364.1, NC_010995.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ACE82849; ACE82849; CJA_2770

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cja:CJA_2770

<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
X82179 Genomic DNA Translation: CAA57670.2
CP000934 Genomic DNA Translation: ACE82849.1
PIRiS53374
RefSeqiWP_012488364.1, NC_010995.1

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
1GVYX-ray1.70A39-422[»]
1GW1X-ray1.65A43-421[»]
1J9YX-ray1.85A39-423[»]
1ODZX-ray1.40A/B39-423[»]
1R7OX-ray1.85A29-423[»]
2WHMX-ray1.50A39-423[»]
SMRiP49424
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_2770

Chemistry databases

DrugBankiDB02680, 1,3-Dinitrobenzene
DB03814, 2-(N-morpholino)ethanesulfonic acid
DB04084, 2-deoxy-2-fluoro-Alpha-D-mannose
DB04483, 2-deoxy-2-fluoro-Beta-D-mannose

Protein family/group databases

CAZyiGH26, Glycoside Hydrolase Family 26

Proteomic databases

PRIDEiP49424

Genome annotation databases

EnsemblBacteriaiACE82849; ACE82849; CJA_2770
KEGGicja:CJA_2770

Phylogenomic databases

eggNOGiCOG4124, Bacteria
HOGENOMiCLU_016930_0_1_6
OMAiFGHQDDL
OrthoDBi669354at2

Enzyme and pathway databases

BioCyciCJAP498211:G1GB3-2766-MONOMER

Miscellaneous databases

EvolutionaryTraceiP49424

Family and domain databases

InterProiView protein in InterPro
IPR022790, GH26_dom
IPR000805, Glyco_hydro_26
IPR017853, Glycoside_hydrolase_SF
PANTHERiPTHR40079, PTHR40079, 1 hit
PfamiView protein in Pfam
PF02156, Glyco_hydro_26, 1 hit
PRINTSiPR00739, GLHYDRLASE26
SUPFAMiSSF51445, SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51764, GH26, 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_CELJU
<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: P49424
Secondary accession number(s): B3PBK3
<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: February 1, 1996
Last sequence update: July 5, 2005
Last modified: June 2, 2021
This is version 112 of the entry and version 2 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, Direct protein sequencing, Reference proteome

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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