ID A0A179HNN1_PURLI Unreviewed; 740 AA.
AC A0A179HNN1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=PCL_07868 {ECO:0000313|EMBL:PWI74554.1}, VFPFJ_05437
GN {ECO:0000313|EMBL:OAQ91278.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ91278.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:PWI74554.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=36-1 {ECO:0000313|EMBL:PWI74554.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWI74554.1, ECO:0000313|Proteomes:UP000245956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36-1 {ECO:0000313|EMBL:PWI74554.1,
RC ECO:0000313|Proteomes:UP000245956};
RX PubMed=27486440; DOI=10.3389/fmicb.2016.01084;
RA Xie J., Li S., Mo C., Xiao X., Peng D., Wang G., Xiao Y.;
RT "Genome and transcriptome sequences reveal the specific parasitism of the
RT nematophagous Purpureocillium lilacinum 36-1.";
RL Front. Microbiol. 7:1084-1084(2016).
RN [3] {ECO:0000313|EMBL:OAQ91278.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ91278.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-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 -!- 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:OAQ91278.1}.
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DR EMBL; LSBI01000004; OAQ91278.1; -; Genomic_DNA.
DR EMBL; LCWV01000003; PWI74554.1; -; Genomic_DNA.
DR RefSeq; XP_018179997.1; XM_018322517.1.
DR AlphaFoldDB; A0A179HNN1; -.
DR GeneID; 28887566; -.
DR KEGG; plj:VFPFJ_05437; -.
DR OMA; GCPTNAK; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR Proteomes; UP000245956; 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:UP000078340};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 218..250
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 265..491
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 572..728
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 676
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
SQ SEQUENCE 740 AA; 80878 MW; 08553F7D5DF835D2 CRC64;
MDLPAEHTPV ATPMPDPPSG DFMTVEQWET IFALLDGVIP AIAEASMFSE KAHLTLSTSE
YEKLLERGTK SLLEAPSRDS VKEFLRYRPS DDEAFRLDVL NTLAITPQRK QLAKIMNLLG
THYGSLLLTG YWSPVTQQPV KNREAIIKSW SQSRLPSLRM LAKALVTTAH KAHAMSSPYF
GSLSGYTDVP VNWKAGDGYD YKFIQVGSGD GVHEISTDVV IVGSGCGGGV SAKNLAEAGH
KVIVVDKGYY FPPSQLPMPQ SAGAKYLYDH GGVTMTDNTS AGIASGGAWG GGGTVNWSVC
FRLQDFVREE WAAKGLPLFK SSEFDDCQDR VWDFIGASKS GIRHNHRNQV LLNGSSKLGW
KADAVEQNTA SKEHYCGQCH LGCGSAEKRG PAVAWLPAAG EAGAEFMEGF EAKRIIFASD
GVTAIGVEGL WTSRDSEGQI HTPLSSRTQR TVRIKAKKVI ISGGSLWTPT ILQKSGVKNP
NVGKYLHLHP VNFVSATFQE DVRPWEGGII TSYCDEFENL DRKGHGVKLE PSCMVPYATF
AMQPWYGGQD AKLLALKYRH LNTWVALTRD RDSGRVYADP KTGEPRVDYT TSDFDRDHTL
EGVQALAKIC YVTGATEIRP HLGGLEPFVP DDGGERQRQH VAGKDPEFTD PKFAAWLKQL
RKVDNKPPFS IFVSAHQMGS CRMSSSPSSG AVDPNGKVWG HENLYVADAS VFPSASGVNP
MVTVMSIADW ISRGISRELK
//
