ID   Q1K844_NEUCR            Unreviewed;      1365 AA.
AC   Q1K844;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 2.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Cholesterol oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NCU01193 {ECO:0000313|EMBL:EAA32323.3};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA32323.3, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA32323.3, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CM002240; EAA32323.3; -; Genomic_DNA.
DR   RefSeq; XP_961559.3; XM_956466.3.
DR   STRING; 367110.Q1K844; -.
DR   PaxDb; 5141-EFNCRP00000004278; -.
DR   EnsemblFungi; EAA32323; EAA32323; NCU01193.
DR   GeneID; 3877682; -.
DR   KEGG; ncr:NCU01193; -.
DR   VEuPathDB; FungiDB:NCU01193; -.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   InParanoid; Q1K844; -.
DR   OrthoDB; 1945480at2759; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
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   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805}.
FT   DOMAIN          185..438
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          615..683
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1365 AA;  151546 MW;  F535EBF4AE4B5B0F CRC64;
     MDRLSAHQSN GAPSPPPTPA CSGHQLGVKT DTAGLFVGST HTNGDSDASF TESPTSDFPP
     TPRRSPKQHP QDYPRSKQES HQIPTEGIHD HQPGGPRARA NTKVRSYVAD QDRQAFPRIS
     KPVELIQVAY DVVVIGSGYG GGVAASRMAR TGSSVCVLER GREKWPGEYP TGAADAFKEL
     HTSGTFAPGS LDGIPVETGD PTGMYHLIFG KGQNAVVANG LGGTSLMNAN VFMEADKGTL
     AMKAWPPEIR NKVDSLDKYY EKVEKVLEPA EYPDDWPELP KAKLLKRQAR YMGYGDKWRK
     VKQTTRFQNG PNSCGVEMSA SALTGQDATG VNDGSKTTTL VTYLADAWNW GAELFCECEV
     RYVEKAKDEN GNDDGYLVYF AWHGRNRGHF RANLHGDLMW VRARKAVFLG AGALATPEIL
     LRSKAMGLEM SNLVGQNMSG NGDILAFGYN TDETVNGIGR AHPSPYNPIG PCITSVIDCR
     HNLENPLDGF VIEEGSVPHA LAHFLQAMLD LMPGSEEPKN LTVLDKAHSA LARYGSRFLG
     PYFKKGAIER TQVYLIMSHD SNQAMLTLQD DKPVLEFLGV GRSDHVKKLN NLLAQATQAV
     GGTYVKSPFD AMMGNQQITV HPIGGACMAR DNTGRTGVTN HVGEVFTGLG SETHDGLIVT
     DAAVIPTALG TNPFATIAAL AERSVEAYCQ RQGLHISEEE NGILDLFGEP QHKPKQHLPV
     RTVSKIEAME EGHSLGYATR AIQMAKELCS SGMGFTEVMS GFIHHDPTMK TDERSTYELA
     YRTAKSRCES ARFFLSVQAF DTFRTLSHAQ HRAMLTGTFV CPAIPGSPFM VRRGEFNLFI
     IDDKAPGTRN LTYDFDMTGV DGRRLHFHGY KVVDSSVALD PLQFWRSTST LYVTVSEHVD
     GMCSNLDDEN AWRRGKVLAK GIMNIQPKHF LSEIMTMTPT GSNLLKKVAS AASFLTFFTR
     KSLSLFMAPL TPLEYPSMMP TGYVNNTAPT KSFAIYADDG VCTRLHMWEP THYPDNDKKN
     IKNLFMVPGA AVDHHIFALP TIRYNAVNYF RRAGYRVFIT VHRIGQLMVA EHNWTTYDAR
     LDIKACMQYI REHYGKEKIY TIAHCMGSVA LSTGMLDGTI PTDWFLGVSC SQVFMNPIWQ
     TMNLIKATTG PYDKIYKALA GNWFSCSTSR DDSYVQQALN QLLRLYPQPR KEICNNAACH
     RTSLVFGRCW NHSNLNEATH RQIDRFFGGV NMKLLHLLMK QGAEGHVMAN EPLCQRLDTP
     ENIRRLKGIP FLLFVGRDQA VLSPESTERT YEILCDTFGM DDTSYKRRVV PGYGHLDVWM
     GRNAWKDVYP FVREEVDRVC RGETYKFVEP QDEFKAMVDS GELLH
//