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Q01738

- CDH_PHACH

UniProt

Q01738 - CDH_PHACH

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Protein

Cellobiose dehydrogenase

Gene

CDH-1

more
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Iron (heme axial ligand)
Metal bindingi181 – 1811Iron (heme axial ligand)
Active sitei707 – 7071By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi236 – 26530FADSequence AnalysisAdd
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-KW
Complete GO annotation...

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 acid1 Publication

Keywords - PTMi

Pyrrolidone carboxylic acid

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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.Curated

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

« 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
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: November 26, 2014
This is version 104 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