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Q01738 (CDH_PHACH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellobiose dehydrogenase

Short name=CDH
EC=1.1.99.18
Alternative name(s):
Cellobiose-quinone oxidoreductase
Gene names
Name:CDH-1
AND
Name:CDH-2
OrganismPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifier5306 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

Protein attributes

Sequence length773 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone.

Catalytic activity

Cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor.

Cofactor

Binds 1 FAD per subunit.

Binds 1 heme group per subunit.

Subcellular location

Secreted.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 773755Cellobiose dehydrogenase
PRO_0000012331

Regions

Nucleotide binding236 – 26530FAD Potential
Region19 – 208190Heme domain
Region235 – 773539Oxidoreductase

Sites

Active site7071 By similarity
Metal binding831Iron (heme axial ligand)
Metal binding1811Iron (heme axial ligand)

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid

Secondary structure

................................................................................................................................. 773
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01738 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 54F721E779AA4D7B

FASTA77382,007
        10         20         30         40         50         60 
MLGRSLLALL PFVGLAFSQS ASQFTDPTTG FQFTGITDPV HDVTYGFVFP PLATSGAQST 

        70         80         90        100        110        120 
EFIGEVVAPI ASKWIGIALG GAMNNDLLLV AWANGNQIVS STRWATGYVQ PTAYTGTATL 

       130        140        150        160        170        180 
TTLPETTINS THWKWVFRCQ GCTEWNNGGG IDVTSQGVLA WAFSNVAVDD PSDPQSTFSE 

       190        200        210        220        230        240 
HTDFGFFGID YSTAHSANYQ NYLNGDSGNP TTTSTKPTST SSSVTTGPTV SATPYDYIIV 

       250        260        270        280        290        300 
GAGPGGIIAA DRLSEAGKKV LLLERGGPST KQTGGTYVAP WATSSGLTKF DIPGLFESLF 

       310        320        330        340        350        360 
TDSNPFWWCK DITVFAGCLV GGGTSVNGAL YWYPNDGDFS SSVGWPSSWT NHAPYTSKLS 

       370        380        390        400        410        420 
SRLPSTDHPS TDGQRYLEQS FNVVSQLLKG QGYNQATIND NPNYKDHVFG YSAFDFLNGK 

       430        440        450        460        470        480 
RAGPVATYLQ TALARPNFTF KTNVMVSNVV RNGSQILGVQ TNDPTLGPNG FIPVTPKGRV 

       490        500        510        520        530        540 
ILSAGAFGTS RILFQSGIGP TDMIQTVQSN PTAAAALPPQ NQWINLPVGM NAQDNPSINL 

       550        560        570        580        590        600 
VFTHPSIDAY ENWADVWSNP RPADAAQYLA NQSGVFAGAS PKLNFWRAYS GSDGFTRYAQ 

       610        620        630        640        650        660 
GTVRPGAASV NSSLPYNASQ IFTITVYLST GIQSRGRIGI DAALRGTVLT PPWLVNPVDK 

       670        680        690        700        710        720 
TVLLQALHDV VSNIGSIPGL TMITPDVTQT LEEYVDAYDP ATMNSNHWVS STTIGSSPQS 

       730        740        750        760        770 
AVVDSNVKVF GTNNLFIVDA GIIPHLPTGN PQGTLMSAAE QAAAKILALA GGP 

« Hide

References

[1]"Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium."
Li B., Nagalla S.R., Renganathan V.
Appl. Environ. Microbiol. 62:1329-1335(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 201542 / OGC101.
[2]"Cellobiose dehydrogenase from Phanerochaete chrysosporium is encoded by two allelic variants."
Li B., Nagalla S.R., Renganathan V.
Appl. Environ. Microbiol. 63:796-799(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 201542 / OGC101.
[3]"A new scaffold for binding haem in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase."
Hallberg B.M., Bergfors T., Boeckbro K., Pettersson G., Henriksson G., Divne C.
Structure 8:79-88(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-208, PYROGLUTAMATE FORMATION AT GLN-19.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46081 mRNA. Translation: AAC49277.1.
U65888 Genomic DNA. Translation: AAB61455.1.
U50409 Genomic DNA. Translation: AAB92262.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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/B20-204[»]
ProteinModelPortalQ01738.
SMRQ01738. Positions 19-208, 228-773.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2303.
OMATPRILFQ.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17578.
BRENDA1.1.99.18. 4722.

Family and domain databases

Gene3D2.60.40.1210. 1 hit.
InterProIPR015920. Cellobiose_DH_cyt.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01738.

Entry information

Entry nameCDH_PHACH
AccessionPrimary (citable) accession number: Q01738
Secondary accession number(s): O00047
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references