ID A0A166PPS3_9PEZI Unreviewed; 804 AA.
AC A0A166PPS3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125};
DE EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125};
DE Flags: Fragment;
GN ORFNames=CI238_04727 {ECO:0000313|EMBL:KZL67014.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL67014.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL67014.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL67014.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:KZL67014.1}.
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DR EMBL; LFIW01002552; KZL67014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166PPS3; -.
DR STRING; 1573173.A0A166PPS3; -.
DR Proteomes; UP000076584; 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; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 262..293
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 309..538
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 632..788
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 676..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 736
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL67014.1"
SQ SEQUENCE 804 AA; 87167 MW; 0E14FD2D611CE2CF CRC64;
LLLPYCLLTV PSTLYVHVSP HVSSFVRLVA STLIVCFAMA TLPKTVPGTA VQLQLPALPT
SDFWNETQWA VLISLLEAVL PSISRPATLS DTTNQVRVSE AEYAAALQLV QNTMKKPPSE
EKFQEYLAHN PAKEPRFVES ITRTLAALPA GAQRQLGGAM GALATRTGTL FLTGYWTPVH
LQPVEVREKI LKAWQTSRIP TIRVLSKSIC LLAQKSAVQT SPLFRELTDY TDMPEFQKHG
EGFDFKFMQF EASGTPAVVE TDVVIVGSGC GGAVAAKVLA EQGHKVLVVD KSYYYPPTQL
PMTQDTGCQF LYENGGFITS DDNSLNMVAG SCWGGGGTVN WSVSLQTQGF VREEWSEQRG
LPFFTSPQFQ NCLDKVCDFM GVSADGVRHN HRNKVLLDGA RKLGWHAATA PQNTGGSEHY
CGQCHLGCGS TEKQGPTVSW LPAAAASGAK FMEGFEVEKV MFDESSGSRR ATGVVGKWVS
RDANGSTSAP LDQRTTREVI VKAKKVILSA GSVSSPLVLL RSGLTNRHIG CNLYVHPCNF
VGGYWKEDCK PWEGGIITSY CSSFEDLDKA GHGVKLEPTC MIPYAILSSM PWHSGFQAKL
SELRFRHFGA FISLTRDRDT GRVYPDPISG RPRVDYVVSD FDRANTLEGV IALCKICYVE
GATEIHAGIP GLEPFVREDH AEPPEKTASA ASGSLGSESG DEAILDGVND PRFVAWLDKL
RKVGNAPPVA IFSSAHQMGT CRMAPNEDEG VVGPKGHVWG TEGLFVADAS VFPSASGVNP
MITNMAIADW IAMNVGKEIK AEFE
//
