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Entry version 65 (02 Dec 2020)
Sequence version 1 (01 Mar 2003)
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Protein

Oligoxyloglucan reducing end-specific cellobiohydrolase

Gene
N/A
Organism
Geotrichum sp. (strain M128)
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>
-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

<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

  • Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.1 Publication EC:3.2.1.150

<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>pH dependencei

Optimum pH is 3.5-5.0 with the oligoxyloglucan heptasaccharide XXXG as a substrate. Over 90% activity is retained between pH 4.8 and 8.0.1 Publication

Temperature dependencei

Optimum temperature is 50-60 degrees Celsius with the oligoxyloglucan heptasaccharide XXXG as a substrate.1 Publication

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 sitei58Nucleophile1 Publication1
Active sitei488Proton donor1 Publication1

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

GO - Biological processi

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

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-16634

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.150, 2419
3.2.1.91, 2419

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH74, Glycoside Hydrolase Family 74

CLAE, a database of fungal genes encoding lignocellulose-active proteins

More...
CLAEi
XBH74A_GEOSP

<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:
Oligoxyloglucan reducing end-specific cellobiohydrolase1 PublicationImported (EC:3.2.1.150)
Short name:
OXG-RCBH1 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>OrganismiGeotrichum sp. (strain M128)
<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 identifieri203496 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeGeotrichumunclassified Geotrichum

<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>Mutagenesisi58D → N: No catalytic activity. 1 Publication1
Mutagenesisi467E → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi488D → N: No catalytic activity. 1 Publication1
Mutagenesisi513D → N: No effect on catalytic activity. 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 – 231 PublicationAdd BLAST23
<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_000039542924 – 812Oligoxyloglucan reducing end-specific cellobiohydrolase1 PublicationAdd BLAST789

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi180N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi289N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi312N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi563N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi697N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi741N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi754N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

<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

1812
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
Q8J0D2

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
Q8J0D2

<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 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati118 – 128BNR 1Sequence analysisAdd BLAST11
Repeati218 – 228BNR 2Sequence analysisAdd BLAST11
Repeati350 – 360BNR 3Sequence analysisAdd BLAST11
Repeati595 – 605BNR 4Sequence analysisAdd BLAST11
Repeati637 – 646BNR 5Sequence analysis10
Repeati681 – 691BNR 6Sequence analysisAdd BLAST11
Repeati736 – 746BNR 7Sequence analysisAdd BLAST11

<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 74 family.1 Publication

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.130.10.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002860, BNR_rpt
IPR015943, WD40/YVTN_repeat-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15899, BNR_6, 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.

Q8J0D2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAVTSLGKA LTALSILASL AVAKEHYEFK NVAIGGGGYI TGIVAHPKTK
60 70 80 90 100
DLLYARTDIG GAYRWDAGTS KWIPLNDFIE AQDMNIMGTE SIALDPNNPD
110 120 130 140 150
RLYLAQGRYV GDEWAAFYVS EDRGQSFTIY ESPFPMGAND MGRNNGERLA
160 170 180 190 200
VNPFNSNEVW MGTRTEGIWK SSDRAKTWTN VTSIPDAFTN GIGYTSVIFD
210 220 230 240 250
PERNGTIYAS ATAPQGMYVT HDGGVSWEPV AGQPSSWLNR TTGAFPDKKP
260 270 280 290 300
ASIAPQPMKV ALTPNFLYVT YADYPGPWGV TFGEVWRQNR TSGAWDDITP
310 320 330 340 350
RVGNSSPAPY NNQTFPAGGF CGLSVDATNP NRLVVITLDR DPGPALDSIY
360 370 380 390 400
LSTDAGATWK DVTQLSSPSN LEGNWGHPTN AARYKDGTPV PWLDFNNGPQ
410 420 430 440 450
WGGYGAPHGT PGLTKFGWWM SAVLIDPFNP EHLMYGTGAT IWATDTLSRV
460 470 480 490 500
EKDWAPSWYL QIDGIEENAI LSLRSPKSGA ALLSGIGDIS GMKHDDLTKP
510 520 530 540 550
QKMFGAPQFS NLDSIDAAGN FPNVVVRAGS SGHEYDSACA RGAYATDGGD
560 570 580 590 600
AWTIFPTCPP GMNASHYQGS TIAVDASGSQ IVWSTKLDEQ ASGPWYSHDY
610 620 630 640 650
GKTWSVPAGD LKAQTANVLS DKVQDGTFYA TDGGKFFVST DGGKSYAAKG
660 670 680 690 700
AGLVTGTSLM PAVNPWVAGD VWVPVPEGGL FHSTDFGASF TRVGTANATL
710 720 730 740 750
VSVGAPKSKS DGKKASAPSA VFIWGTDKPG SDIGLYRSDD NGSTWTRVND
760 770 780 790 800
QEHNYSGPTM IEADPKVYGR VYLGTNGRGI VYADLTNKKS NEEKSTAKCA
810
NGQKGTHCYV KK
Length:812
Mass (Da):87,081
Last modified:March 1, 2003 - 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:iF5C740F32D8B17E5
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
AB089343 mRNA Translation: BAC22065.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:BAC22065

<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
AB089343 mRNA Translation: BAC22065.1

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
1SQJX-ray2.20A/B24-812[»]
2EBSX-ray2.40A/B24-812[»]
SMRiQ8J0D2
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiGH74, Glycoside Hydrolase Family 74
CLAEiXBH74A_GEOSP

Genome annotation databases

KEGGiag:BAC22065

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16634
BRENDAi3.2.1.150, 2419
3.2.1.91, 2419

Miscellaneous databases

EvolutionaryTraceiQ8J0D2

Family and domain databases

Gene3Di2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR002860, BNR_rpt
IPR015943, WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF15899, BNR_6, 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 nameiCBHRE_GEOS1
<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: Q8J0D2
<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 13, 2010
Last sequence update: March 1, 2003
Last modified: December 2, 2020
This is version 65 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 programFungal 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

Documents

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