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
//