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Entry version 69 (02 Jun 2021)
Sequence version 1 (01 May 2000)
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Protein

Multidomain esterase

Gene

cesA

Organism
Ruminococcus flavefaciens
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Esterase involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of chemically acetylated xylan and native, steam-extracted xylan (PubMed:10846217).

Seems to act in synergy with the xylanase XynD which produces xylo-oligosaccharides (PubMed:10846217).

Also catalyzes the deesterification of methyl esters of 4-O-methyl-D-glucuronic acid (MeGlcA) side residues in synthetic glucuronoxylan methyl ester, suggesting that it may be able to cleave ester linkages between MeGlcA carboxyl and more complex alcohols, including linkages between hemicellulose and lignin alcohols in plant cell walls (PubMed:26216754).

2 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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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 sitei68Nucleophile; for acetylxylan esterase activityBy similarity1
Active sitei240For acetylxylan esterase activityBy similarity1
Active sitei243For acetylxylan esterase activityBy similarity1
Active sitei565Nucleophile; for glucuronoyl esterase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei569SubstrateBy similarity1
Binding sitei633SubstrateBy similarity1
Binding sitei679SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Multifunctional enzyme, Serine esterase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.B11, 5478

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

More...
UniPathwayi
UPA00114

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
rumfl-CESA, Glucuronoyl_esterase

<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:
Multidomain esterase1 Publication
Including the following 2 domains:
Acetylxylan esterase1 Publication (EC:3.1.1.721 Publication)
4-O-methyl-glucuronoyl methylesterase1 Publication (EC:3.1.1.-1 Publication)
Alternative name(s):
Glucuronoyl esterase1 Publication
Short name:
GE1 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:cesA1 Publication
<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>OrganismiRuminococcus flavefaciens
<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 identifieri1265 [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 lineageiBacteriaFirmicutesClostridiaEubacterialesOscillospiraceaeRuminococcus

<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 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 – 40Sequence analysisAdd BLAST40
<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_500433152141 – 768Multidomain esteraseAdd BLAST728

<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

<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>Domaini285 – 352DockerinPROSITE-ProRule annotationAdd BLAST68

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>Regioni41 – 264Acetylxylan esteraseCuratedAdd BLAST224
Regioni267 – 289DisorderedSequence analysisAdd BLAST23
Regioni353 – 768Glucuronoyl esterase1 PublicationAdd BLAST416

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi563 – 568GXSYXG catalytic site motifBy similarity6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi267 – 283Polar residuesSequence analysisAdd BLAST17

<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 a dockerin-like region in addition to its catalytic domains, suggesting that this enzyme forms part of a cellulosome-like multienzyme complex.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

In the N-terminal section; belongs to the carbohydrate esterase 3 (CE3) family.Curated
In the C-terminal section; belongs to the carbohydrate esterase 15 (CE15) family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1330.10, 1 hit
3.40.50.1110, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR001087, GDSL
IPR036514, SGNH_hydro_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00404, Dockerin_1, 1 hit
PF00657, Lipase_GDSL, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63446, SSF63446, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51766, DOCKERIN, 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.

Q9RLB8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKHFVVGET IKRFLRIGTS LALSISTLSL LPSAPRLSSA AGTIKIMPLG
60 70 80 90 100
DSITYGMADE GGYRKYLSYF LQQKGYTNVD LVGPEGKDSA SFNYNGQSVK
110 120 130 140 150
YDDNHAGYSG YTITNLPGGW FGQLNGILET MQGGDYIKKY SPDIILLQIG
160 170 180 190 200
TNDVSNGHLD GSEERLHKLL DYLRENMPSN GKVFLTTIPD LGNSGWGGNS
210 220 230 240 250
NGDIAKYNEL IKKVANDYSS KNVIYADIHS VIDASKDLAD GVHPNAGGYE
260 270 280 290 300
KMGKYWLEQI EGYLKASDGP QQTQPTQPSQ GDSGPELIYG DLDGDKTITS
310 320 330 340 350
FDAVIMRKGL INDFKDNNVK KAADIDQNGK AEVADLVQLQ SFIIGKIKEF
360 370 380 390 400
TVAEKTVTEK PVFEKSYNFP AVNQLKSSKD IPDPFIFMDG SKVESTDDWW
410 420 430 440 450
KRQSEISCMY EYYMYGKWID GSDDETTYSI SGNSMTINVK RKSTGKTASF
460 470 480 490 500
KAVINLPKNV RHEGGAPVIL GMHKGISEST ATSNGYAVIT YDSDGMFSAP
510 520 530 540 550
GTAQDNNQHK GAFYDLYPYG RNWDEQTGDL MAWSWGISRI LDALYNGAAK
560 570 580 590 600
ELNINPDSSI VTGVSRYGKA ASVCGAFDTR IKMCAPSCSG AGGLALYRYS
610 620 630 640 650
SVGKTYDFSS KGGSSSYTYK ENEPLGSLQA SGEQGWFNGR FMEFRNAEQF
660 670 680 690 700
PMDQHMLGAL CCDPDRYLFI IGSCESEDWV NAPSVWMAYL GMKHVWDYVG
710 720 730 740 750
ISDHLAINIH KSGHAVIAED IEKMVQYFDY HVYGIQPKMN LEELQTSVFA
760
LPKNKDSFAD TFASKWLY
Length:768
Mass (Da):84,835
Last modified:May 1, 2000 - 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:i420883356109417E
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
AJ238716 Genomic DNA Translation: CAB55348.1

<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
AJ238716 Genomic DNA Translation: CAB55348.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein family/group databases

ESTHERirumfl-CESA, Glucuronoyl_esterase

Enzyme and pathway databases

UniPathwayiUPA00114
BRENDAi3.1.1.B11, 5478

Family and domain databases

Gene3Di1.10.1330.10, 1 hit
3.40.50.1110, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR002105, Dockerin_1_rpt
IPR016134, Dockerin_dom
IPR036439, Dockerin_dom_sf
IPR001087, GDSL
IPR036514, SGNH_hydro_sf
PfamiView protein in Pfam
PF00404, Dockerin_1, 1 hit
PF00657, Lipase_GDSL, 1 hit
SUPFAMiSSF63446, SSF63446, 1 hit
PROSITEiView protein in PROSITE
PS51766, DOCKERIN, 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 nameiCESA_RUMFL
<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: Q9RLB8
<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: April 13, 2016
Last sequence update: May 1, 2000
Last modified: June 2, 2021
This is version 69 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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