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Q01738

- CDH_PHACH

UniProt

Q01738 - CDH_PHACH

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Protein

Cellobiose dehydrogenase

Gene
CDH-1
CDH-2
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - 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

Binds 1 FAD per subunit.
Binds 1 heme group per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Iron (heme axial ligand)
Metal bindingi181 – 1811Iron (heme axial ligand)
Active sitei707 – 7071 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi236 – 26530FAD Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. cellobiose dehydrogenase (acceptor) activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
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. 4722.

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 lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesCorticialesCorticiaceaePhanerochaete

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 773755Cellobiose dehydrogenasePRO_0000012331Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid

Keywords - PTMi

Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
773
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254
Turni27 – 293
Beta strandi32 – 387
Turni39 – 424
Beta strandi43 – 497
Beta strandi54 – 563
Beta strandi62 – 698
Beta strandi74 – 785
Beta strandi81 – 866
Beta strandi88 – 947
Beta strandi97 – 1048
Beta strandi106 – 1094
Beta strandi119 – 1224
Beta strandi130 – 14011
Turni141 – 1433
Beta strandi155 – 16612
Beta strandi182 – 1909
Helixi191 – 1933
Helixi199 – 2035
Beta strandi235 – 2406
Helixi244 – 25512
Beta strandi260 – 2634
Helixi271 – 2733
Helixi280 – 2856
Turni289 – 2913
Helixi293 – 3008
Beta strandi312 – 3143
Helixi322 – 3254
Helixi336 – 3394
Helixi341 – 3433
Helixi347 – 3493
Helixi353 – 36210
Helixi379 – 38911
Turni390 – 3923
Helixi398 – 4003
Beta strandi408 – 4114
Helixi423 – 4264
Helixi428 – 4336
Beta strandi438 – 4414
Beta strandi446 – 4527
Beta strandi455 – 4628
Helixi468 – 4703
Beta strandi471 – 48212
Helixi485 – 49511
Helixi501 – 5088
Helixi511 – 5166
Helixi520 – 5223
Turni528 – 5314
Beta strandi538 – 5436
Helixi550 – 5534
Turni554 – 5585
Helixi562 – 57110
Helixi575 – 5773
Beta strandi583 – 5908
Beta strandi596 – 60611
Helixi618 – 6203
Beta strandi621 – 6288
Beta strandi636 – 6405
Beta strandi646 – 6505
Helixi657 – 67014
Turni671 – 6733
Helixi674 – 6763
Beta strandi681 – 6855
Helixi691 – 6977
Helixi700 – 7034
Turni718 – 7203
Beta strandi733 – 7375
Helixi740 – 7423
Helixi752 – 76817

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 19-208, 228-773.

Miscellaneous databases

EvolutionaryTraceiQ01738.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 208190Heme domainAdd
BLAST
Regioni235 – 773539OxidoreductaseAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2303.
OMAiTPRILFQ.

Family and domain databases

Gene3Di2.60.40.1210. 1 hit.
InterProiIPR015920. Cellobiose_DH_cyt.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
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

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MLGRSLLALL PFVGLAFSQS ASQFTDPTTG FQFTGITDPV HDVTYGFVFP    50
PLATSGAQST EFIGEVVAPI ASKWIGIALG GAMNNDLLLV AWANGNQIVS 100
STRWATGYVQ PTAYTGTATL TTLPETTINS THWKWVFRCQ GCTEWNNGGG 150
IDVTSQGVLA WAFSNVAVDD PSDPQSTFSE HTDFGFFGID YSTAHSANYQ 200
NYLNGDSGNP TTTSTKPTST SSSVTTGPTV SATPYDYIIV GAGPGGIIAA 250
DRLSEAGKKV LLLERGGPST KQTGGTYVAP WATSSGLTKF DIPGLFESLF 300
TDSNPFWWCK DITVFAGCLV GGGTSVNGAL YWYPNDGDFS SSVGWPSSWT 350
NHAPYTSKLS SRLPSTDHPS TDGQRYLEQS FNVVSQLLKG QGYNQATIND 400
NPNYKDHVFG YSAFDFLNGK RAGPVATYLQ TALARPNFTF KTNVMVSNVV 450
RNGSQILGVQ TNDPTLGPNG FIPVTPKGRV ILSAGAFGTS RILFQSGIGP 500
TDMIQTVQSN PTAAAALPPQ NQWINLPVGM NAQDNPSINL VFTHPSIDAY 550
ENWADVWSNP RPADAAQYLA NQSGVFAGAS PKLNFWRAYS GSDGFTRYAQ 600
GTVRPGAASV NSSLPYNASQ IFTITVYLST GIQSRGRIGI DAALRGTVLT 650
PPWLVNPVDK TVLLQALHDV VSNIGSIPGL TMITPDVTQT LEEYVDAYDP 700
ATMNSNHWVS STTIGSSPQS AVVDSNVKVF GTNNLFIVDA GIIPHLPTGN 750
PQGTLMSAAE QAAAKILALA GGP 773
Length:773
Mass (Da):82,007
Last modified:November 1, 1996 - v1
Checksum:i54F721E779AA4D7B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D7B X-ray 1.90 A/B 20-204 [» ]
1D7C X-ray 1.90 A/B 20-208 [» ]
1D7D X-ray 1.90 A/B 20-204 [» ]
1KDG X-ray 1.50 A/B 228-773 [» ]
1NAA X-ray 1.80 A/B 233-773 [» ]
1PL3 X-ray 1.90 A/B 19-204 [» ]
ProteinModelPortali Q01738.
SMRi Q01738. Positions 19-208, 228-773.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2303.
OMAi TPRILFQ.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17578.
BRENDAi 1.1.99.18. 4722.

Miscellaneous databases

EvolutionaryTracei Q01738.

Family and domain databases

Gene3Di 2.60.40.1210. 1 hit.
InterProi IPR015920. Cellobiose_DH_cyt.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view ]
Pfami PF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view ]
PROSITEi PS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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: July 9, 2014
This is version 101 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

External Data

Dasty 3

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