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Database: UniProt
Entry: A0A1U8B338_NELNU
LinkDB: A0A1U8B338_NELNU
Original site: A0A1U8B338_NELNU 
ID   A0A1U8B338_NELNU        Unreviewed;       807 AA.
AC   A0A1U8B338;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125};
DE            EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125};
GN   Name=LOC104610302 {ECO:0000313|RefSeq:XP_010275157.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010275157.1};
RN   [1] {ECO:0000313|RefSeq:XP_010275157.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_010275157.1; XM_010276855.2.
DR   AlphaFoldDB; A0A1U8B338; -.
DR   STRING; 4432.A0A1U8B338; -.
DR   GeneID; 104610302; -.
DR   KEGG; nnu:104610302; -.
DR   eggNOG; ENOG502QSD8; Eukaryota.
DR   InParanoid; A0A1U8B338; -.
DR   OrthoDB; 601859at2759; -.
DR   Proteomes; UP000189703; Unplaced.
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; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR028937-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR028937-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        123..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          337..557
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          658..785
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          29..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        732
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT   BINDING         290..305
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ   SEQUENCE   807 AA;  89235 MW;  C8E0151052848C73 CRC64;
     MNGNGAGKFS NFPTNGGVRH TVIDLGSIRT DPESKSTKAP NELHSPSLLP GERKPYVNSL
     SPRQMEVLTA FSDTLLPSVF PDINCSGQLE DSLFKFYRTS ASMAGTPELV GGFLSGKIEH
     PMLGVLLLAL WLLSTWFGTF ILCGIPSLST QFPYFQRFSQ VSQKKREKIL LSWSSSSFNI
     YRMLFKTLKY LVFFIFFTQV DENNENPTWR GIDYCGPDPD FINNRTRETK TPQGHEHEEL
     FEPLYRGIVN MRQPREALAE TLRQSGFHVR LHPHRRYNPS PSHPSLTIRC DAVVVGSGSG
     GGVAAGILAK AGYKVAVLEK GNYFGRKNLS LLEGPSMDEM YLSGGLMVTD DMGVIMLAGS
     TVGGGSTINW SASIRTPQHV IREWCNEYEL ELFGSKLYKE AMDVVCKRMG VQPDVEEESL
     SNTVLRKGCS ELGYPVITAP RNSPPNHYCG WCCFGCKDGR KKGTSETWLV DLVDSGNGVI
     LPGCEALKIL HERKKGRKRN TATGVVFEFN NGWGKDFCVL ESKVTIVAGG ALCTPTLLKR
     SGLRNSNIGK NLHLHPVVMA WGHFPSRPAD SGWPEKDKKS YKGGIITAMS TVVANSEGSG
     YGAVIQTPML HPGMFSVITP WISSVDMRER MSKFSRTAYI FALARDKGSG QVNSPSSISY
     RMDAMDEEHL KQGLEKILRI LAAAGAEEIG TSHCLGRKVN VKKVSSNEFE RFVKKESRRA
     LRDLRTPIPS AHQMGSCRMG VDPKSSVVNH RGETWEVEGL FLADSSVFPT ALGVNPMVTI
     QSIAYCTAQS VLEVLRRKKD DLISFQF
//
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