Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01738

- CDH_PHACH

UniProt

Q01738 - CDH_PHACH

Protein

Cellobiose dehydrogenase

Gene

CDH-1

more
Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 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

    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 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 – 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.
    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

    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: October 1, 2014
    This is version 102 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