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Entry version 114 (07 Oct 2020)
Sequence version 1 (01 May 1992)
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Protein

Endoglucanase B

Gene

cenB

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

<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

  • Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EC:3.2.1.4

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 sitei91NucleophilePROSITE-ProRule annotation1
Active sitei410PROSITE-ProRule annotation1
Active sitei449PROSITE-ProRule annotation1
Active sitei458PROSITE-ProRule annotation1

<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, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM2, Carbohydrate-Binding Module Family 2
CBM3, Carbohydrate-Binding Module Family 3
GH9, Glycoside Hydrolase Family 9

<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:
Endoglucanase B (EC:3.2.1.4)
Alternative name(s):
Cellulase B
Endo-1,4-beta-glucanase B
<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:cenB
<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>OrganismiCellulomonas fimi
<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 identifieri1708 [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 lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

<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 – 33Sequence analysisAdd BLAST33
<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_000000794534 – 1045Endoglucanase BAdd BLAST1012

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 bondi946 ↔ 1044By similarity

Keywords - PTMi

Disulfide bond

<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

More...
SMRi
P26225

Database of comparative protein structure models

More...
ModBasei
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

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>Domaini493 – 642CBM3PROSITE-ProRule annotationAdd BLAST150
Domaini653 – 743Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST91
Domaini751 – 840Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST90
Domaini849 – 940Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST92
Domaini939 – 1045CBM2PROSITE-ProRule annotationAdd BLAST107

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>Regioni34 – 492CatalyticAdd BLAST459
Regioni644 – 650Linker ('hinge') (Pro-Thr box)7
Regioni734 – 748Linker ('hinge') (Pro-Thr box)Add BLAST15
Regioni831 – 846Linker ('hinge') (Pro-Thr box)Add BLAST16
Regioni931 – 944Linker ('hinge') (Pro-Thr box)Add BLAST14

<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

The linker region (also termed 'hinge') may be a potential site for proteolysis.1 Publication

<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 9 (cellulase E) family.PROSITE-ProRule annotationCurated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063, FN3, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.10, 1 hit
2.60.40.10, 3 hits
2.60.40.290, 1 hit
2.60.40.710, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR001919, CBD2
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR012291, CBM2_carb-bd_dom_sf
IPR018366, CBM2_CS
IPR001956, CBM3
IPR036966, CBM3_sf
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR001701, Glyco_hydro_9
IPR033126, Glyco_hydro_9_Asp/Glu_AS
IPR018221, Glyco_hydro_9_His_AS
IPR013783, Ig-like_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00553, CBM_2, 1 hit
PF00942, CBM_3, 1 hit
PF00041, fn3, 3 hits
PF00759, Glyco_hydro_9, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00637, CBD_II, 1 hit
SM01067, CBM_3, 1 hit
SM00060, FN3, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48208, SSF48208, 1 hit
SSF49265, SSF49265, 2 hits
SSF49384, SSF49384, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51173, CBM2, 1 hit
PS00561, CBM2_A, 1 hit
PS51172, CBM3, 1 hit
PS50853, FN3, 3 hits
PS60032, GH9_1, 1 hit
PS00592, GH9_2, 1 hit
PS00698, GH9_3, 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.

P26225-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRQVPRTLV AGGSALAVAV GVLVAPLATG AAAAPTYNYA EALQKSMFFY
60 70 80 90 100
QAQRSGDLPA DFPVSWRGDS GLTDGADVGK DLTGGWYDAG DHVKFGFPMA
110 120 130 140 150
FSATMLAWGA IESPTGYSKA GSLDELKDNL RFVSDYFVKA HTAPNELYVQ
160 170 180 190 200
VGDGEADHKW WGPAEVMTMA RPSHKISASC PGSDVAAETA AALASSAIVL
210 220 230 240 250
KGDDPAYAAT LVSHAKQLYT FADTYRGAYS DCVTAASAYY KSWSGYQDEL
260 270 280 290 300
VWGAYWLYKA TGDATYLAKA EAEYDKLGTE NQSTTRSYKW TIAWDNKQFG
310 320 330 340 350
TYALLAMETG KQKYVDDANR WLDYWTVGVN GQKVPYSPGG QAVLDSWGAL
360 370 380 390 400
RYAANTSFVA LVYSDWMTDA TRKARYHDFG VRQINYALGD NPRSSSYVVG
410 420 430 440 450
FGANPPTAPH HRTAHGSWLD SITTPAQSRH VLYGALVGGP GSPNDAYTDS
460 470 480 490 500
RQDYVANEVA TDYNAGFTSA LARLVEEYGG TPLASFPTPE QPDGDQLFVE
510 520 530 540 550
AMLNQPPSGT FTEVKAMIRN QSAFPARSLK NAKVRYWFTT DGFAASDVTL
560 570 580 590 600
SANYSECGAQ SGKGVSAGGT LGYVELSCVG QDIHPGGQSQ HRREIQFRLT
610 620 630 640 650
GPAGWNPAND PSYTGLTQTA LAKASAITLY DGSTLVWGKE PTGTTTDTTP
660 670 680 690 700
PTTPGTPVAT GVTTVGASLS WAASTDAGSG VAGYELYRVQ GTTQTLVGTT
710 720 730 740 750
TAAAYILRDL TPGTAYSYVV KAKDVAGNVS AASAAVTFTT DTTGETEPPT
760 770 780 790 800
TPGTPVASAV TSTGATLAWA PSTGDPAVSG YDVLRVQGTT TTVVAQTTVP
810 820 830 840 850
TVTLSGLTPS TAYTYAVRAK NVAGDVSALS APVTFTTAAP PVDTVAPTVP
860 870 880 890 900
GTPVASNVAT TGATLTWTAS TDSGGSGLAG YEVLRVSGTT QTLVASPTTA
910 920 930 940 950
TVALAGLTPA TAYSYVVRAK DGAGNVSAVS SPVTFTTLPV TSTPSCTVVY
960 970 980 990 1000
STNSWNVGFT GSVKITNTGT TPLTWTLGFA FPSGQQVTQG WSATWSQTGT
1010 1020 1030 1040
TVTATGLSWN ATLQPGQSTD IGFNGSHPGT NTNPASFTVN GEVCG
Length:1,045
Mass (Da):108,991
Last modified:May 1, 1992 - 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:iAC2F7B84E4E3C4F0
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
M64644 Genomic DNA Translation: AAA23086.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39199

NCBI Reference Sequences

More...
RefSeqi
WP_013769201.1, NZ_LR134387.1

<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
M64644 Genomic DNA Translation: AAA23086.1
PIRiA39199
RefSeqiWP_013769201.1, NZ_LR134387.1

3D structure databases

SMRiP26225
ModBaseiSearch...

Protein family/group databases

CAZyiCBM2, Carbohydrate-Binding Module Family 2
CBM3, Carbohydrate-Binding Module Family 3
GH9, Glycoside Hydrolase Family 9

Family and domain databases

CDDicd00063, FN3, 3 hits
Gene3Di1.50.10.10, 1 hit
2.60.40.10, 3 hits
2.60.40.290, 1 hit
2.60.40.710, 1 hit
InterProiView protein in InterPro
IPR008928, 6-hairpin_glycosidase_sf
IPR012341, 6hp_glycosidase-like_sf
IPR001919, CBD2
IPR008965, CBM2/CBM3_carb-bd_dom_sf
IPR012291, CBM2_carb-bd_dom_sf
IPR018366, CBM2_CS
IPR001956, CBM3
IPR036966, CBM3_sf
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR001701, Glyco_hydro_9
IPR033126, Glyco_hydro_9_Asp/Glu_AS
IPR018221, Glyco_hydro_9_His_AS
IPR013783, Ig-like_fold
PfamiView protein in Pfam
PF00553, CBM_2, 1 hit
PF00942, CBM_3, 1 hit
PF00041, fn3, 3 hits
PF00759, Glyco_hydro_9, 1 hit
SMARTiView protein in SMART
SM00637, CBD_II, 1 hit
SM01067, CBM_3, 1 hit
SM00060, FN3, 3 hits
SUPFAMiSSF48208, SSF48208, 1 hit
SSF49265, SSF49265, 2 hits
SSF49384, SSF49384, 2 hits
PROSITEiView protein in PROSITE
PS51173, CBM2, 1 hit
PS00561, CBM2_A, 1 hit
PS51172, CBM3, 1 hit
PS50853, FN3, 3 hits
PS60032, GH9_1, 1 hit
PS00592, GH9_2, 1 hit
PS00698, GH9_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGUNB_CELFI
<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: P26225
<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: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 7, 2020
This is version 114 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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