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Entry version 130 (25 May 2022)
Sequence version 2 (14 Oct 2015)
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Protein

Cellulase/esterase CelE

Gene

celE

Organism
Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
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

Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan (PubMed:3066698, PubMed:1991028).

Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc) (PubMed:19338387).

3 Publications

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

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

Esterase activity of the CE2 module is inhibited when this domain binds to cellohexaose or beta-glucan.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 7032 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan.1 Publication
  1. KM=165 µM for 4-nitrophenyl acetate1 Publication
  2. KM=2.7 mM for acetylated birchwood xylan1 Publication
  3. KM=0.019 mM for acetylated glucomannan1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.1 Publication
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei193Proton donor; for cellulase activityBy similarity1
Active sitei316Nucleophile; for cellulase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi415Calcium 1PROSITE-ProRule annotation1
Metal bindingi417Calcium 1PROSITE-ProRule annotation1
Metal bindingi419Calcium 1PROSITE-ProRule annotation1
Metal bindingi420Calcium 1; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi421Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi426Calcium 1PROSITE-ProRule annotation1
Metal bindingi451Calcium 2PROSITE-ProRule annotation1
Metal bindingi451Calcium 3PROSITE-ProRule annotation1
Metal bindingi452Calcium 2; via amide nitrogenPROSITE-ProRule annotation1
Metal bindingi453Calcium 3PROSITE-ProRule annotation1
Metal bindingi455Calcium 3PROSITE-ProRule annotation1
Metal bindingi457Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi457Calcium 3; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi462Calcium 2PROSITE-ProRule annotation1
Metal bindingi462Calcium 3PROSITE-ProRule annotation1
Active sitei612Nucleophile; for esterase activity1 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>Sitei658Transition state stabilizerBy similarity1
Sitei705Transition state stabilizerBy similarity1
Sitei791Increases nucleophilicity of active site Ser1 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, Multifunctional enzyme
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
CTHE203119:G1G86-831-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.4, 1530

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

More...
UniPathwayi
UPA00114
UPA00696

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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cellulase/esterase CelECurated
Alternative name(s):
CtCel5C-CE21 Publication
Including the following 2 domains:
Cellulase E1 Publication (EC:3.2.1.42 Publications)
Alternative name(s):
CtCel5C1 Publication
Endo-1,4-beta-glucanase E1 Publication
Short name:
EGE1 Publication
Short name:
Endoglucanase E1 Publication
Acetylxylan esterase / glucomannan deacetylase1 Publication (EC:3.1.1.-1 Publication, EC:3.1.1.721 Publication)
Alternative name(s):
CtCE21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:celE1 Publication
Ordered Locus Names:Cthe_0797Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAcetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri203119 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesClostridiaEubacterialesOscillospiraceaeAcetivibrio
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002145 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi612S → A: Loss of esterase activity. 8-fold increase in the binding affinity to cellohexaose. 1 Publication1
Mutagenesisi789D → A or N: Retains significant esterase activity against 4-NPAc and the polymeric substrates. 1 Publication1
Mutagenesisi791H → A: Loss of esterase activity. 20-fold decrease in the binding affinity to cellohexaose. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 341 PublicationAdd BLAST34
<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_000000785235 – 814Cellulase/esterase CelEAdd BLAST780

<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
203119.Cthe_0797

<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

1814
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P10477

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

More...
SMRi
P10477

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
P10477

<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%5Fand%5Fdomains%5Fsection">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>Domaini409 – 479DockerinPROSITE-ProRule annotationAdd BLAST71

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>Regioni35 – 354CellulaseCuratedAdd BLAST320
Regioni490 – 814EsteraseCuratedAdd BLAST325

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains an N-terminal module that displays cellulase activity (CtCel5C), a central type I dockerin module (Doc) that facilitates the integration of the enzyme into the cellulosome, and a C-terminal module, CtCE2, which displays dual activities: it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its non-catalytic cellulose binding function.2 Publications

<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

In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
In the C-terminal section; belongs to the carbohydrate esterase 2 (CE2) family.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2730, Bacteria
COG2755, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_346724_0_0_9

Identification of Orthologs from Complete Genome Data

More...
OMAi
CAYGNEG

Database of Orthologous Groups

More...
OrthoDBi
1395441at2

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01831, Endoglucanase_E_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1330.10, 1 hit
3.40.50.1110, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR040794, CE2_N
IPR037461, CtCE2-like_dom
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR001087, GDSL
IPR001547, Glyco_hydro_5
IPR018087, Glyco_hydro_5_CS
IPR017853, Glycoside_hydrolase_SF
IPR036514, SGNH_hydro_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17996, CE2_N, 1 hit
PF00150, Cellulase, 1 hit
PF00404, Dockerin_1, 1 hit
PF00657, Lipase_GDSL, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 1 hit
SSF63446, SSF63446, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00448, CLOS_CELLULOSOME_RPT, 2 hits
PS51766, DOCKERIN, 1 hit
PS00659, GLYCOSYL_HYDROL_F5, 1 hit

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

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

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

P10477-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKIVSLVCV LVMLVSILGS FSVVAASPVK GFQVSGTKLL DASGNELVMR
60 70 80 90 100
GMRDISAIDL VKEIKIGWNL GNTLDAPTET AWGNPRTTKA MIEKVREMGF
110 120 130 140 150
NAVRVPVTWD THIGPAPDYK IDEAWLNRVE EVVNYVLDCG MYAIINVHHD
160 170 180 190 200
NTWIIPTYAN EQRSKEKLVK VWEQIATRFK DYDDHLLFET MNEPREVGSP
210 220 230 240 250
MEWMGGTYEN RDVINRFNLA VVNTIRASGG NNDKRFILVP TNAATGLDVA
260 270 280 290 300
LNDLVIPNND SRVIVSIHAY SPYFFAMDVN GTSYWGSDYD KASLTSELDA
310 320 330 340 350
IYNRFVKNGR AVIIGEFGTI DKNNLSSRVA HAEHYAREAV SRGIAVFWWD
360 370 380 390 400
NGYYNPGDAE TYALLNRKTL SWYYPEIVQA LMRGAGVEPL VSPTPTPTLM
410 420 430 440 450
PTPSPTVTAN ILYGDVNGDG KINSTDCTML KRYILRGIEE FPSPSGIIAA
460 470 480 490 500
DVNADLKINS TDLVLMKKYL LRSIDKFPAE DSQTPDEDNP GILYNGRFDF
510 520 530 540 550
SDPNGPKCAW SGSNVELNFY GTEASVTIKS GGENWFQAIV DGNPLPPFSV
560 570 580 590 600
NATTSTVKLV SGLAEGAHHL VLWKRTEASL GEVQFLGFDF GSGKLLAAPK
610 620 630 640 650
PLERKIEFIG DSITCAYGNE GTSKEQSFTP KNENSYMSYA AITARNLNAS
660 670 680 690 700
ANMIAWSGIG LTMNYGGAPG PLIMDRYPYT LPYSGVRWDF SKYVPQVVVI
710 720 730 740 750
NLGTNDFSTS FADKTKFVTA YKNLISEVRR NYPDAHIFCC VGPMLWGTGL
760 770 780 790 800
DLCRSYVTEV VNDCNRSGDL KVYFVEFPQQ DGSTGYGEDW HPSIATHQLM
810
AERLTAEIKN KLGW
Length:814
Mass (Da):90,230
Last modified:October 14, 2015 - 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:i9913A8E252CBBF8D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti147V → L in AAA23224 (PubMed:3066698).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
M22759 Genomic DNA Translation: AAA23224.1
CP000568 Genomic DNA Translation: ABN52032.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JT0347, CZCLEM

NCBI Reference Sequences

More...
RefSeqi
WP_011837903.1, NC_009012.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABN52032; ABN52032; Cthe_0797

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cth:Cthe_0797

<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
M22759 Genomic DNA Translation: AAA23224.1
CP000568 Genomic DNA Translation: ABN52032.1
PIRiJT0347, CZCLEM
RefSeqiWP_011837903.1, NC_009012.1

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
2WABX-ray1.90A485-814[»]
2WAOX-ray1.80A485-814[»]
4IM4X-ray2.42A/B/C/D/E/F51-386[»]
AlphaFoldDBiP10477
SMRiP10477
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi203119.Cthe_0797

Protein family/group databases

CAZyiGH5, Glycoside Hydrolase Family 5

Genome annotation databases

EnsemblBacteriaiABN52032; ABN52032; Cthe_0797
KEGGicth:Cthe_0797

Phylogenomic databases

eggNOGiCOG2730, Bacteria
COG2755, Bacteria
HOGENOMiCLU_346724_0_0_9
OMAiCAYGNEG
OrthoDBi1395441at2

Enzyme and pathway databases

UniPathwayiUPA00114
UPA00696
BioCyciCTHE203119:G1G86-831-MONOMER
BRENDAi3.2.1.4, 1530

Miscellaneous databases

EvolutionaryTraceiP10477

Family and domain databases

CDDicd01831, Endoglucanase_E_like, 1 hit
Gene3Di1.10.1330.10, 1 hit
3.40.50.1110, 1 hit
InterProiView protein in InterPro
IPR040794, CE2_N
IPR037461, CtCE2-like_dom
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR001087, GDSL
IPR001547, Glyco_hydro_5
IPR018087, Glyco_hydro_5_CS
IPR017853, Glycoside_hydrolase_SF
IPR036514, SGNH_hydro_sf
PfamiView protein in Pfam
PF17996, CE2_N, 1 hit
PF00150, Cellulase, 1 hit
PF00404, Dockerin_1, 1 hit
PF00657, Lipase_GDSL, 1 hit
SUPFAMiSSF51445, SSF51445, 1 hit
SSF63446, SSF63446, 1 hit
PROSITEiView protein in PROSITE
PS00448, CLOS_CELLULOSOME_RPT, 2 hits
PS51766, DOCKERIN, 1 hit
PS00659, GLYCOSYL_HYDROL_F5, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<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 nameiCELE_ACET2
<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: P10477
Secondary accession number(s): A3DDK3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 14, 2015
Last modified: May 25, 2022
This is version 130 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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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