ID A0A178EKU5_9PLEO Unreviewed; 743 AA.
AC A0A178EKU5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=IQ07DRAFT_6817 {ECO:0000313|EMBL:OAL56424.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL56424.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL56424.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL56424.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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; KV441636; OAL56424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EKU5; -.
DR STRING; 765867.A0A178EKU5; -.
DR InParanoid; A0A178EKU5; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000077535; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 272..497
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 579..726
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 674
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ SEQUENCE 743 AA; 81363 MW; BBD37DD0DCDAF10E CRC64;
MSLPTEPVSP KATPLPPLPS EDPLTPAQWK TLLAIADTVV PAIKPMSTAN TRTEIAIVDN
EYSTAVSKLR GLTPKDDPDV EAAVKDYLED YASKDPAFKL QLQRLFAMYM PHSQRKELIM
LLNILNTRAG SLAFTGYLTP ISEQPAHIRE QIIKGWGTAR LGALRQLHRS LTVILKQTWI
KITPSLRRVL GVPRVPTGMI PGKGYDYEFI QIPPGKKPEI IETDVVIVGS GCGGGVSAKN
LAEAGYRVLV TEKAYHWTPD HFPMSEADGW NHLFMNGAFI SSDDTSVSIV AGQAWGGGGT
VNWSASLQTQ GYVRREWASK GLPFFTSAEF QESLDRVCDR MGVSTESIKQ NRSNQLLMEG
ARKLGWAHKP VPQNTGGSQH YCGYCTFGCG SCEKQGPAVS YLPDAARAGA SFIEGFHAER
IIFSKRSGKK VATGVLGTWA SRDINGGIAG SPVTRRKVLI KAKRVIVSAG TMQSPLLLLR
SGLTNPQIGR NLYVHPVTMI GAIHEEEIKP WEGGILTSVI SEYENLDGKG HGAKLEATNM
IPSSWLIWLD WKGGLEYKLD AARLKHMVGY ISICRDRDTG RVYPDPVDGR VRFQYSTSKF
DKKHILEGIL ALAKVQYVSG AQEIFTVMPG MRPFIRDPST PPGDGINDEA FQTWLDEVRE
RGFRTPESAF VSAHQMGSNR MSAVEKDGVV DPHGRVWGTK GLFVADASVF PSASGVNPMV
TNMAISDYIS RGVVKGLQDK PKL
//
