ID CDH_PHACH Reviewed; 773 AA.
AC Q01738; O00047;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Cellobiose dehydrogenase;
DE Short=CDH;
DE EC=1.1.99.18;
DE AltName: Full=Cellobiose-quinone oxidoreductase;
DE Flags: Precursor;
GN Name=CDH-1;
GN and
GN Name=CDH-2;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=8919793; DOI=10.1128/aem.62.4.1329-1335.1996;
RA Li B., Nagalla S.R., Renganathan V.;
RT "Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme
RT from Phanerochaete chrysosporium.";
RL Appl. Environ. Microbiol. 62:1329-1335(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 201542 / OGC101;
RX PubMed=9023960; DOI=10.1128/aem.63.2.796-799.1997;
RA Li B., Nagalla S.R., Renganathan V.;
RT "Cellobiose dehydrogenase from Phanerochaete chrysosporium is encoded by
RT two allelic variants.";
RL Appl. Environ. Microbiol. 63:796-799(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-208, AND PYROGLUTAMATE
RP FORMATION AT GLN-19.
RX PubMed=10673428; DOI=10.1016/s0969-2126(00)00082-4;
RA Hallberg B.M., Bergfors T., Boeckbro K., Pettersson G., Henriksson G.,
RA Divne C.;
RT "A new scaffold for binding haem in the cytochrome domain of the
RT extracellular flavocytochrome cellobiose dehydrogenase.";
RL Structure 8:79-88(2000).
CC -!- FUNCTION: Degrades both lignin and cellulose. Oxidizes cellobiose to
CC cellobionolactone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + D-cellobiose = AH2 + D-cellobiono-1,5-lactone;
CC Xref=Rhea:RHEA:23484, ChEBI:CHEBI:13193, ChEBI:CHEBI:17057,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17863; EC=1.1.99.18;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: In the C-terminal section; belongs to the GMC
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U46081; AAC49277.1; -; mRNA.
DR EMBL; U65888; AAB61455.1; -; Genomic_DNA.
DR EMBL; U50409; AAB92262.1; -; Genomic_DNA.
DR PDB; 1D7B; X-ray; 1.90 A; A/B=20-204.
DR PDB; 1D7C; X-ray; 1.90 A; A/B=20-208.
DR PDB; 1D7D; X-ray; 1.90 A; A/B=20-204.
DR PDB; 1KDG; X-ray; 1.50 A; A/B=228-773.
DR PDB; 1NAA; X-ray; 1.80 A; A/B=233-773.
DR PDB; 1PL3; X-ray; 1.90 A; A/B=19-204.
DR PDBsum; 1D7B; -.
DR PDBsum; 1D7C; -.
DR PDBsum; 1D7D; -.
DR PDBsum; 1KDG; -.
DR PDBsum; 1NAA; -.
DR PDBsum; 1PL3; -.
DR AlphaFoldDB; Q01738; -.
DR SMR; Q01738; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR CAZy; AA8; Auxiliary Activities 8.
DR EnsemblFungi; AGR57_11438T0; AGR57_11438T0-p1; AGR57_11438.
DR VEuPathDB; FungiDB:AGR57_11438; -.
DR OMA; GPIFWEI; -.
DR BioCyc; MetaCyc:MONOMER-17578; -.
DR BRENDA; 1.1.99.18; 1380.
DR EvolutionaryTrace; Q01738; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047735; F:cellobiose dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd09630; CDH_like_cytochrome; 1.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation; FAD;
KW Flavoprotein; Heme; Iron; Metal-binding; Oxidoreductase;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..773
FT /note="Cellobiose dehydrogenase"
FT /id="PRO_0000012331"
FT REGION 19..208
FT /note="Heme domain"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..773
FT /note="Oxidoreductase"
FT ACT_SITE 707
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 83
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 181
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 236..265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10673428"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1D7B"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1D7B"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:1D7B"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 155..166
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:1D7B"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1D7B"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1D7B"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 471..482
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 485..495
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 554..558
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 562..571
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 596..606
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 621..628
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 636..640
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 657..670
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 681..685
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 691..697
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 700..703
FT /evidence="ECO:0007829|PDB:1KDG"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:1KDG"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:1KDG"
FT HELIX 752..768
FT /evidence="ECO:0007829|PDB:1KDG"
SQ SEQUENCE 773 AA; 82007 MW; 54F721E779AA4D7B CRC64;
MLGRSLLALL PFVGLAFSQS ASQFTDPTTG FQFTGITDPV HDVTYGFVFP PLATSGAQST
EFIGEVVAPI ASKWIGIALG GAMNNDLLLV AWANGNQIVS STRWATGYVQ PTAYTGTATL
TTLPETTINS THWKWVFRCQ GCTEWNNGGG IDVTSQGVLA WAFSNVAVDD PSDPQSTFSE
HTDFGFFGID YSTAHSANYQ NYLNGDSGNP TTTSTKPTST SSSVTTGPTV SATPYDYIIV
GAGPGGIIAA DRLSEAGKKV LLLERGGPST KQTGGTYVAP WATSSGLTKF DIPGLFESLF
TDSNPFWWCK DITVFAGCLV GGGTSVNGAL YWYPNDGDFS SSVGWPSSWT NHAPYTSKLS
SRLPSTDHPS TDGQRYLEQS FNVVSQLLKG QGYNQATIND NPNYKDHVFG YSAFDFLNGK
RAGPVATYLQ TALARPNFTF KTNVMVSNVV RNGSQILGVQ TNDPTLGPNG FIPVTPKGRV
ILSAGAFGTS RILFQSGIGP TDMIQTVQSN PTAAAALPPQ NQWINLPVGM NAQDNPSINL
VFTHPSIDAY ENWADVWSNP RPADAAQYLA NQSGVFAGAS PKLNFWRAYS GSDGFTRYAQ
GTVRPGAASV NSSLPYNASQ IFTITVYLST GIQSRGRIGI DAALRGTVLT PPWLVNPVDK
TVLLQALHDV VSNIGSIPGL TMITPDVTQT LEEYVDAYDP ATMNSNHWVS STTIGSSPQS
AVVDSNVKVF GTNNLFIVDA GIIPHLPTGN PQGTLMSAAE QAAAKILALA GGP
//
