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 27-MAR-2024, entry version 36.
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 GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF12; LONG-CHAIN-ALCOHOL OXIDASE FAO4B; 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; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//
