ID M1WFI4_CLAP2 Unreviewed; 781 AA.
AC M1WFI4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CPUR_07614 {ECO:0000313|EMBL:CCE33688.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE33688.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE33688.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE33688.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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}.
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:CCE33688.1}.
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DR EMBL; CAGA01000064; CCE33688.1; -; Genomic_DNA.
DR AlphaFoldDB; M1WFI4; -.
DR STRING; 1111077.M1WFI4; -.
DR VEuPathDB; FungiDB:CPUR_07614; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_3_1_1; -.
DR OrthoDB; 601859at2759; -.
DR PhylomeDB; M1WFI4; -.
DR Proteomes; UP000016801; 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; IPR003953; FAD-binding_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; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF028937; Lg_Ch_AO; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR028937};
KW Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 257..289
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 304..529
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 613..768
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 79..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 716
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ SEQUENCE 781 AA; 84614 MW; 582057A6C78FCDF7 CRC64;
MASLVGPPPI PIPDVPPRDF MRPAQWETLF ALLDGVLPSV RSAASLDSTS EDQDQDKGGS
IVLPEEEFEA LVEECCGEGQ GLEGPLSVME DGKEKRGEMG EMDEEKMAEK ARRRECVRAF
LEDRPAGGEA FRGDCVRSLA GVPQRGKLAV VMDVLGSHVG SMLLTGHWTP ITSQPTPIRQ
AILQSWASSP LPALRTLAKS LVQMAQKANS LHSRFLHDIS GYSDIPSDWK NTESYPYTFI
QIPPGGKDLS PYELSTDVLI VGSGCGGGVS AKTLSEAGHK VLVVDKGYYF PPSQLPMTQE
SASHYLYEGG GVLTSDSAST GVVCGASWGG GGTVNWSVCF RLQDYVRDEW ASRGLPLFAS
AEFDACMDRV WEFIGASKAG LRHNARNQAL MDALETLRWK GGAVEQNTAG REHYCGRCHL
GCNSAEKRGP ATSWLPAAGE AGAEFMEGFA VERVVFGEDG RTAIGVEGLW TGRGEGGTLH
GKMEERTQRR VFVRAKRVIL AAGSMWSPVL LAKSGVKNPN VGRHLHLHPT NFVSGVFGKT
DMTSWEGGII TSYVNEFENL DGHGHGVKLE PTCNVPYTTF SLQSWRDGLD AKVLALKYRH
IGTYISLTRD RDTGRVYPDP VHGTPRIQYD MSDFDREHTL EGVIALAKIC YVARATEIRA
HLAGLAPFVA RDGGKRQAEH QSGTDPEFTD PDFAAWIKRL RRADNKPPTA MCVSAHQMGS
CRMSADEESG VVDMQGRVWG TSGLYVADAS VFPSASGVNP MVTAMALADW ISRGVAADLS
S
//
