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Entry version 134 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Cellobiose dehydrogenase

Gene

CDH-1

more
Organism
Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
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

Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone.

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi83Iron (heme axial ligand)1
Metal bindingi181Iron (heme axial ligand)1
<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 sitei707Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi236 – 265FADSequence analysisAdd BLAST30

<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 functionOxidoreductase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation
LigandFAD, Flavoprotein, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17578

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.99.18, 1380

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
AA3, Auxiliary Activities 3
AA8, Auxiliary Activities 8

<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:
Cellobiose dehydrogenase (EC:1.1.99.18)
Short name:
CDH
Alternative name(s):
Cellobiose-quinone oxidoreductase
<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:CDH-1
AND
Name:CDH-2
<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>OrganismiPhanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
<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 identifieri2822231 [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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerodontia

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:AGR57_11438

<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 – 18Add BLAST18
<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_000001233119 – 773Cellobiose dehydrogenaseAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19Pyrrolidone carboxylic acid1 Publication1

Keywords - PTMi

Pyrrolidone carboxylic acid

<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

1773
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
Q01738

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
Q01738

<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

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>Regioni19 – 208Heme domainAdd BLAST190
Regioni203 – 227DisorderedSequence analysisAdd BLAST25
Regioni235 – 773OxidoreductaseAdd BLAST539

<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 C-terminal section; belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
RSNFKLW

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09630, CDH_like_cytochrome, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015920, Cellobiose_DH_cyt
IPR005018, DOMON_domain
IPR036188, FAD/NAD-bd_sf
IPR000172, GMC_OxRdtase_N
IPR007867, GMC_OxRtase_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16010, CDH-cyt, 1 hit
PF05199, GMC_oxred_C, 1 hit
PF00732, GMC_oxred_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00664, DoH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51905, SSF51905, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00623, GMC_OXRED_1, 1 hit
PS00624, GMC_OXRED_2, 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.

Q01738-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGRSLLALL PFVGLAFSQS ASQFTDPTTG FQFTGITDPV HDVTYGFVFP
60 70 80 90 100
PLATSGAQST EFIGEVVAPI ASKWIGIALG GAMNNDLLLV AWANGNQIVS
110 120 130 140 150
STRWATGYVQ PTAYTGTATL TTLPETTINS THWKWVFRCQ GCTEWNNGGG
160 170 180 190 200
IDVTSQGVLA WAFSNVAVDD PSDPQSTFSE HTDFGFFGID YSTAHSANYQ
210 220 230 240 250
NYLNGDSGNP TTTSTKPTST SSSVTTGPTV SATPYDYIIV GAGPGGIIAA
260 270 280 290 300
DRLSEAGKKV LLLERGGPST KQTGGTYVAP WATSSGLTKF DIPGLFESLF
310 320 330 340 350
TDSNPFWWCK DITVFAGCLV GGGTSVNGAL YWYPNDGDFS SSVGWPSSWT
360 370 380 390 400
NHAPYTSKLS SRLPSTDHPS TDGQRYLEQS FNVVSQLLKG QGYNQATIND
410 420 430 440 450
NPNYKDHVFG YSAFDFLNGK RAGPVATYLQ TALARPNFTF KTNVMVSNVV
460 470 480 490 500
RNGSQILGVQ TNDPTLGPNG FIPVTPKGRV ILSAGAFGTS RILFQSGIGP
510 520 530 540 550
TDMIQTVQSN PTAAAALPPQ NQWINLPVGM NAQDNPSINL VFTHPSIDAY
560 570 580 590 600
ENWADVWSNP RPADAAQYLA NQSGVFAGAS PKLNFWRAYS GSDGFTRYAQ
610 620 630 640 650
GTVRPGAASV NSSLPYNASQ IFTITVYLST GIQSRGRIGI DAALRGTVLT
660 670 680 690 700
PPWLVNPVDK TVLLQALHDV VSNIGSIPGL TMITPDVTQT LEEYVDAYDP
710 720 730 740 750
ATMNSNHWVS STTIGSSPQS AVVDSNVKVF GTNNLFIVDA GIIPHLPTGN
760 770
PQGTLMSAAE QAAAKILALA GGP
Length:773
Mass (Da):82,007
Last modified:November 1, 1996 - 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:i54F721E779AA4D7B
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
U46081 mRNA Translation: AAC49277.1
U65888 Genomic DNA Translation: AAB61455.1
U50409 Genomic DNA Translation: AAB92262.1

<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
U46081 mRNA Translation: AAC49277.1
U65888 Genomic DNA Translation: AAB61455.1
U50409 Genomic DNA Translation: AAB92262.1

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
1D7BX-ray1.90A/B20-204[»]
1D7CX-ray1.90A/B20-208[»]
1D7DX-ray1.90A/B20-204[»]
1KDGX-ray1.50A/B228-773[»]
1NAAX-ray1.80A/B233-773[»]
1PL3X-ray1.90A/B19-204[»]
SMRiQ01738
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiAA3, Auxiliary Activities 3
AA8, Auxiliary Activities 8

Organism-specific databases

VEuPathDBiFungiDB:AGR57_11438

Phylogenomic databases

OMAiRSNFKLW

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17578
BRENDAi1.1.99.18, 1380

Miscellaneous databases

EvolutionaryTraceiQ01738

Family and domain databases

CDDicd09630, CDH_like_cytochrome, 1 hit
Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR015920, Cellobiose_DH_cyt
IPR005018, DOMON_domain
IPR036188, FAD/NAD-bd_sf
IPR000172, GMC_OxRdtase_N
IPR007867, GMC_OxRtase_C
PfamiView protein in Pfam
PF16010, CDH-cyt, 1 hit
PF05199, GMC_oxred_C, 1 hit
PF00732, GMC_oxred_N, 1 hit
SMARTiView protein in SMART
SM00664, DoH, 1 hit
SUPFAMiSSF51905, SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00623, GMC_OXRED_1, 1 hit
PS00624, GMC_OXRED_2, 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 nameiCDH_PHACH
<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: Q01738
Secondary accession number(s): O00047
<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: May 30, 2000
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 134 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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