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Database: UniProt
Entry: M5C6I5_THACB
LinkDB: M5C6I5_THACB
Original site: M5C6I5_THACB 
ID   M5C6I5_THACB            Unreviewed;       612 AA.
AC   M5C6I5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Choline dehydrogenase Short=CDH {ECO:0000313|EMBL:CCO35021.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:CCO35021.1};
GN   ORFNames=BN14_09134 {ECO:0000313|EMBL:CCO35021.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO35021.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO35021.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCO35021.1}.
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DR   EMBL; CAOJ01013960; CCO35021.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5C6I5; -.
DR   HOGENOM; CLU_002865_6_0_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF218; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000313|EMBL:CCO35021.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        452..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..135
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          268..401
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          418..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  63897 MW;  2AD1ACC3C9B5D98A CRC64;
     MKKGDLASGD TNVAAITPST LNPSNFTRSN SLAGYITPAG PRKNLVILTG MQATGLVWGS
     KSNGGAVATG VNFAASAGTQ TYSVKASKEV ILCGGVIGSA QLLQVSGVGP KSLMDSLRIQ
     SVVDLPGVGQ NLQDHEATSV TWSVDGATWA DLAGNATLQE EQLAEYRESS TGLWTYINEA
     VAYPNIQDIM GTSAETWIST VSSQLSSALS SLSTAQSLDS TVLKGITEQF NVQLDMLRNG
     VGQLEIIMTM LAGAGNVGIQ VAQQHAWSRG ELRISSASVW DYPTINPNYL SNGWDVDIMN
     AGIKFVRRVG STAPMSSYLK TEGGGTSGAT TDVAINNYVA NAIATGYHPI GTCSMLPLDM
     GGVVDTTLRV YGTANVRVID ASVMPIHVTA HTTAPAYAIA EYGADIVKMA YWPVPPPSSS
     TTSKAGGATS TPGSSSEDDA VTGGLSQNQR TVAIAASIGG AAAVAALIAV LFFIRRRGQK
     AKAQEDAYSG AYATDQRRSD LPMQTLSQSD LHAPIIPFKD GGKSDYRMSA STMDTAQLHA
     ATPLQEHQHL HYDAPQSPGY AYNSQTYNPY TDVSAPGTPY MPPASGLAPG NAHEYQPVSG
     RASPGSNNGP RI
//
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