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Protein

Cellobiose dehydrogenase

Gene

CDH-1

more
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • FADNote: Binds 1 FAD per subunit.
  • hemeNote: Binds 1 heme group per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi83Iron (heme axial ligand)1
Metal bindingi181Iron (heme axial ligand)1
Active sitei707Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi236 – 265FADSequence analysisAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17578.
BRENDAi1.1.99.18. 1380.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.
AA8. Auxiliary Activities 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellobiose dehydrogenase (EC:1.1.99.18)
Short name:
CDH
Alternative name(s):
Cellobiose-quinone oxidoreductase
Gene namesi
Name:CDH-1
AND
Name:CDH-2
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000001233119 – 773Cellobiose dehydrogenaseAdd BLAST755

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Pyrrolidone carboxylic acid1 Publication1

Keywords - PTMi

Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi5306.JGI74422.

Structurei

Secondary structure

1773
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 25Combined sources4
Turni27 – 29Combined sources3
Beta strandi32 – 38Combined sources7
Turni39 – 42Combined sources4
Beta strandi43 – 49Combined sources7
Beta strandi54 – 56Combined sources3
Beta strandi62 – 69Combined sources8
Beta strandi74 – 78Combined sources5
Beta strandi81 – 86Combined sources6
Beta strandi88 – 94Combined sources7
Beta strandi97 – 104Combined sources8
Beta strandi106 – 109Combined sources4
Beta strandi119 – 122Combined sources4
Beta strandi130 – 140Combined sources11
Turni141 – 143Combined sources3
Beta strandi155 – 166Combined sources12
Beta strandi182 – 190Combined sources9
Helixi191 – 193Combined sources3
Helixi199 – 203Combined sources5
Beta strandi235 – 240Combined sources6
Helixi244 – 255Combined sources12
Beta strandi260 – 263Combined sources4
Helixi271 – 273Combined sources3
Helixi280 – 285Combined sources6
Turni289 – 291Combined sources3
Helixi293 – 300Combined sources8
Beta strandi312 – 314Combined sources3
Helixi322 – 325Combined sources4
Helixi336 – 339Combined sources4
Helixi341 – 343Combined sources3
Helixi347 – 349Combined sources3
Helixi353 – 362Combined sources10
Helixi379 – 389Combined sources11
Turni390 – 392Combined sources3
Helixi398 – 400Combined sources3
Beta strandi408 – 411Combined sources4
Helixi423 – 426Combined sources4
Helixi428 – 433Combined sources6
Beta strandi438 – 441Combined sources4
Beta strandi446 – 452Combined sources7
Beta strandi455 – 462Combined sources8
Helixi468 – 470Combined sources3
Beta strandi471 – 482Combined sources12
Helixi485 – 495Combined sources11
Helixi501 – 508Combined sources8
Helixi511 – 516Combined sources6
Helixi520 – 522Combined sources3
Turni528 – 531Combined sources4
Beta strandi538 – 543Combined sources6
Helixi550 – 553Combined sources4
Turni554 – 558Combined sources5
Helixi562 – 571Combined sources10
Helixi575 – 577Combined sources3
Beta strandi583 – 590Combined sources8
Beta strandi596 – 606Combined sources11
Helixi618 – 620Combined sources3
Beta strandi621 – 628Combined sources8
Beta strandi636 – 640Combined sources5
Beta strandi646 – 650Combined sources5
Helixi657 – 670Combined sources14
Turni671 – 673Combined sources3
Helixi674 – 676Combined sources3
Beta strandi681 – 685Combined sources5
Helixi691 – 697Combined sources7
Helixi700 – 703Combined sources4
Turni718 – 720Combined sources3
Beta strandi733 – 737Combined sources5
Helixi740 – 742Combined sources3
Helixi752 – 768Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ01738.
SMRiQ01738.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01738.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 208Heme domainAdd BLAST190
Regioni235 – 773OxidoreductaseAdd BLAST539

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IUIF. Eukaryota.
COG2303. LUCA.
OMAiSGRWGGT.

Family and domain databases

CDDicd09630. CDH_like_cytochrome. 1 hit.
Gene3Di2.60.40.1210. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR015920. Cellobiose_DH_cyt.
IPR005018. DOMON_domain.
IPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF16010. CDH-cyt. 1 hit.
PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i54F721E779AA4D7B
GO

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.

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:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliQ01738.
SMRiQ01738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5306.JGI74422.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.
AA8. Auxiliary Activities 8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IUIF. Eukaryota.
COG2303. LUCA.
OMAiSGRWGGT.

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.
Gene3Di2.60.40.1210. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR015920. Cellobiose_DH_cyt.
IPR005018. DOMON_domain.
IPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF16010. CDH-cyt. 1 hit.
PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDH_PHACH
AccessioniPrimary (citable) accession number: Q01738
Secondary accession number(s): O00047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.