ID   H0E7B5_9ACTN            Unreviewed;       564 AA.
AC   H0E7B5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Putative cholesterol oxidase CHOD (Cholesterol-O2 oxidoreductase) {ECO:0000313|EMBL:EHN10440.1};
DE            EC=1.1.3.6 {ECO:0000313|EMBL:EHN10440.1};
GN   ORFNames=PAI11_27170 {ECO:0000313|EMBL:EHN10440.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10440.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN10440.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN10440.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
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:EHN10440.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGUD01000221; EHN10440.1; -; Genomic_DNA.
DR   RefSeq; WP_007576102.1; NZ_AGUD01000221.1.
DR   AlphaFoldDB; H0E7B5; -.
DR   PATRIC; fig|1097667.3.peg.2697; -.
DR   OrthoDB; 517968at2; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
DR   GO; GO:0016995; F:cholesterol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EHN10440.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143}.
FT   DOMAIN          11..304
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          466..526
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   564 AA;  61084 MW;  7850D3D4F5B5873A CRC64;
     MPQPDSTFDT DWLVIGSGFG GSVSAMRLAE KGHRVTVLER GEHFRDESEM PRSSWDLRKY
     LYMPRAGLRG LFKLTFFKDV FVMSGAGVGG GSLVYAMTLY VPPQAFFEDG QWAGIADWRS
     ELAPHYETAQ RMLGVTDVVE DDPADQLLKQ YAGELGVEHT YRKARVGTYL DTPGEEVADP
     YFGGEGPART GCSRIGRCML GCPQGSKNSL DKNYLWFAQR DGATVRAGRE VVALRPLNGT
     DGADGWEVHH ERTGRRRRKD RQVIRARGVV VSGGALGTNE LLARCKLQGD LPKVSDRLGH
     LVRTNSEAVL VVTVPEGRAE ALAKRVAITS SIYPDPHTHI ETVTYGAGGG AIRNLFTVLT
     GGGNRVTRPL KWLGQMVRHP GWVAELLIKP RWGERSIVVL VMQSLDNSMQ LVARLRRDGR
     VKLQTRQDPD HPNPTFIPAA NAFTEWLARK TGGAPGSAVP EALLSIPTTA HILGGAPIGA
     SPEHGVIDER HRVFGYENLL VCDGAAIPAN VGVNPSLTIT AMAERAIDHV PPKHAGATVH
     HRGRTAIAGK TAGGEPEPLA AAPA
//