ID   FAO2_LOTJA              Reviewed;         750 AA.
AC   B5WWZ9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Long-chain-alcohol oxidase FAO2;
DE            EC=1.1.3.20;
DE   AltName: Full=Long-chain fatty alcohol oxidase 2;
GN   Name=FAO2;
OS   Lotus japonicus (Lotus corniculatus var. japonicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX   NCBI_TaxID=34305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhao S., Lin Z., Luo D., Ma W., Cheng Q.;
RT   "Cloning and characterization of long chain fatty alcohol oxidase LjFAO2 in
RT   Lotus japonicus.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AM900800; CAP15763.1; -; mRNA.
DR   PRIDE; B5WWZ9; -.
DR   GO; GO:0016021; C:integral component of 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; -; 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   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF028937; Lg_Ch_AO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..750
FT                   /note="Long-chain-alcohol oxidase FAO2"
FT                   /id="PRO_0000395508"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        683
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         239..254
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   750 AA;  82355 MW;  F36C985DADD053A0 CRC64;
     MEREESCETH PLLKGGRRKE KGYSHGLSSS QMHVIAAICE ALFPSQPLDS QNNQSSVDKA
     LSAFYTASGS QAPLPDEAAE LLFKFNRSFP EALSLVSWVL LILSFRLGTL LLCGTLCLDW
     RWPFIHKFSE IPLEKREEIL KRWSREKCWI PLRLVFVLTK LVCFYNLFSR ADVNGHNPIW
     KAIGYQVDTR EKLTQKKRPL QEGLIETMYE TDSTLIQSLT EKGLEVTEDL EQNMYKIKCD
     AVIVGSGCGG GVAAAVLANS GHKVIILEKG EYFVSHDYSS LEGPSMNELY ESGGILPSLD
     GKMMILAGST LGGXSAINWS ACIRTPDSVL REWSEKHKIP LFASPDYQSA MDTVCRRIGV
     TENCNKESFQ NQILRQGCAK IGFKVEPVAI NSSADHYCGS CCYGCRTGDK KGTESTWLVD
     AVGNGAVILT GCKAEKLNFT LKDGDNGTKR KTCSGVIASA TWRSKVTKKL QIESKVTISA
     CGSLSTPPLM ISSGLKNPNI GKNLHLHPCQ FAWGYFPEDM TNFSGNNYEG GIITSIHKVF
     EEDSTSTPRI IIEAPALGPG SFSALVPWVS GLDVKERMVK YARTANLFAL VRDHGSGEVK
     AEGRISYKLD KIDRESLQTG LRKALRILVA AGAVEVGTYR SDGQRIKCRG IKESDLEEFL
     DSVRVVGGPS SRNEVWTVFT SAHQMTSCRM SATEEEGAVD ENGESWEAKG LYVCDGSVLP
     SAVGVNPMIT IQSTAYCIAS NIAESLKKQN