ID   A0A239DCI3_9ACTN        Unreviewed;       811 AA.
AC   A0A239DCI3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Cholesterol oxidase {ECO:0000313|EMBL:SNS29772.1};
GN   ORFNames=SAMN06265355_11489 {ECO:0000313|EMBL:SNS29772.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS29772.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNS29772.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS29772.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZNP01000014; SNS29772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239DCI3; -.
DR   OrthoDB; 517968at2; -.
DR   Proteomes; UP000198420; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          205..299
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          441..550
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          560..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   811 AA;  86804 MW;  FA57A27895854B33 CRC64;
     MTDTEHVDAV VVGSGFGGSV TAYRLAEAGQ RVVLLERGQP YPPGSFPRSP AEMGRAFWDP
     EAGLYGMYDV WGFKGCDSVV SAGLGGGSLI YANVLLRKDE RWFVHDRPVP GGGHEPWPIS
     RDDLDPHYDA VERMMGATPY PLDQVPYDDT PKTHALQDAA AELGLHSTLP PLAVSFASEP
     GGAPGVGLPI ADPAYGNLHG ARRRTCKLCG ECDIGCNEGS KNSLDHNYLS AAAHHGADIR
     TSHEVKAIRP RRGGGYEVDY VHHTDLTARK RRLPIRTITC DRLVLGAGTY GTTYLLLKSR
     KAFPGLSSAL GTRFCGNGDL LTFLMRAKDR NRVRPLNASR GPVITTAIRL PDDLDGVPGA
     GRGAYIQDGG YPGFTDWIVN GFDVRGEIER AAEFLWGRFR EFFKDAPDTN LSKELSDLIG
     GGALTVSSLP LLGMGRETAD GRLHLRDGRL AADWNARTSE ELFNRVRKTM QGIADVLGAD
     YADNPMWFRK RIITVHPLGG APMGGHPGEG VCDAFGEVFG FPGLYIADGA AMPGPVGPNP
     SLTIAAQADR LATRLLEETS ARRGAGGPTA PPATGAEPAG GAGSPGGAGN GSAYGPASGN
     HGGTRGPSTA AAGRTSLSFT EEMKGFVTYG ETDMRIGELA EGRRPLSFRL TITAADTERF
     LAEPDHEATA AGWVDATGHG GRRPVERGTF NLLVADAPED RRLMKYRLFY TDGEGRRRTL
     SGHKNVLHGP PTRIWPDTST LYVRLLDGHV AEDEEDGARV VAAGVLHIQL TDFARQLTTF
     RTTGPDGAGK LLDFGRFFAG ELWEVYGPDP A
//