ID   A0A446BPT0_9PEZI        Unreviewed;       761 AA.
AC   A0A446BPT0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
DE            EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125, ECO:0000256|PIRNR:PIRNR028937};
GN   ORFNames=TT172_LOCUS6926 {ECO:0000313|EMBL:SPQ24507.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ24507.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ24507.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation.
CC       {ECO:0000256|ARBA:ARBA00003842}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain primary fatty alcohol + O2 = a long-chain fatty
CC         aldehyde + H2O2; Xref=Rhea:RHEA:22756, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17176, ChEBI:CHEBI:77396; EC=1.1.3.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00000920,
CC         ECO:0000256|PIRNR:PIRNR028937};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|PIRNR:PIRNR028937}.
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DR   EMBL; OUUZ01000013; SPQ24507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A446BPT0; -.
DR   Proteomes; UP000289323; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR012400; Long_Oxdase.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF028937; Lg_Ch_AO; 3.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR028937};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          285..499
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          583..741
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          642..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        689
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ   SEQUENCE   761 AA;  82315 MW;  19C0DCA98D617DED CRC64;
     MSTTTEVAPL TAPVPVDLPD AVEFLSESQW KVLMAVMDAV IPAIRMEDAS QPSKPNHDPS
     VFYLPSGQYS EAAIKLRNAV SPLDHPSDTL EAYLAERPSD NPLFTQVLKC VLSNLPPSKQ
     RDMRVLLSIL NTRPGSLLLT SHAKPLPALP ITDRLKILRS WSTSPLWALR SLFKSLSTVG
     KLVYIRSSAA FPVLTGFPAV PTAWAATSTS HPFTFLQFHP SSNSRKTPVE VTTDVAIVGS
     GCGAGVVAHR LAREFGPALS VLVLEKGRHV DARHFPLSQA AGLATLFEAG GVIETDDGSM
     TVTAGACFGG GGTINWSASL QTQDFVRAEW ARERGLPFFE SDEFQACLDR VCHVMGVAEV
     PPNHANRVLL EGARKLGYQA KAVPQNCGGK EHDDGYCALG CWRGEKMGPV NGWFPEAARQ
     GVKFAEGMKV EKVLFEQKKG AKVATGVKGV WTSREGEKVE VIVRAKKVVI SCGTLWSPVV
     LLNSGLKNPH IGKNLHLHPT NFVSGIFDED VRPWEGGSLT SVVTSFENLD SKGHGVKLEA
     MTMMPSFCLP FLPWTTGIEY KLRAAHYRHL NTFIAICRDR DSGSVHRDPS TGAPRVAYTP
     SDFDRAHNLR GVLELCRILH AHGAREIHPS IAGCPPFIRS AARRRSGEGS TPENADGEQG
     EEAKEFERWL AGVRALGNKP PVTPFASAHQ MGSCRMSARA KDGVVDSRGR VWGTKGLYVA
     DASVFPSASG VNPMVTTMAI ADWIAMGLCE DLRGEGVAAR L
//