ID   FAO1_LOTJA              Reviewed;         749 AA.
AC   B5WWZ8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Long-chain-alcohol oxidase FAO1;
DE            EC=1.1.3.20;
DE   AltName: Full=Long-chain fatty alcohol oxidase 1;
GN   Name=FAO1;
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], FUNCTION, MUTAGENESIS OF CYS-396, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY COLD
RP   STRESS, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18396913; DOI=10.1021/bp0703533;
RA   Zhao S., Lin Z., Ma W., Luo D., Cheng Q.;
RT   "Cloning and characterization of long-chain fatty alcohol oxidase LjFAO1 in
RT   lotus japonicus.";
RL   Biotechnol. Prog. 24:773-779(2008).
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation. {ECO:0000269|PubMed:18396913}.
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:0000269|PubMed:18396913};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=59.6 uM for 1-dodecanol {ECO:0000269|PubMed:18396913};
CC         KM=40.9 uM for 1-hexadecanol {ECO:0000269|PubMed:18396913};
CC         KM=19.4 uM for 1,16-hexadecandiol {ECO:0000269|PubMed:18396913};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in floral buds and apexes.
CC       Detected in roots, stems, leaves, flowers and siliques.
CC       {ECO:0000269|PubMed:18396913}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression in roots 4 days after
CC       germination, then in apexes 7 days after germination.
CC       {ECO:0000269|PubMed:18396913}.
CC   -!- INDUCTION: Down-regulated in leaves and apexes by cold stress, but no
CC       changes in roots and hypocotyls. {ECO:0000269|PubMed:18396913}.
CC   -!- DOMAIN: The C-terminal part (725-748) is necessary for enzyme activity.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AM900799; CAP15762.1; -; mRNA.
DR   AlphaFoldDB; B5WWZ8; -.
DR   SMR; B5WWZ8; -.
DR   PRIDE; B5WWZ8; -.
DR   KEGG; ag:CAP15762; -.
DR   SABIO-RK; B5WWZ8; -.
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; IDA:UniProtKB.
DR   GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..749
FT                   /note="Long-chain-alcohol oxidase FAO1"
FT                   /id="PRO_0000395507"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        681
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         237..252
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         396
FT                   /note="C->G: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:18396913"
SQ   SEQUENCE   749 AA;  82262 MW;  7BBB00D015B32D0B CRC64;
     MRKECHPLLR GGRKDNKFRQ GFSSSEMESL ASICEVILPP LPMDALKIKK HDDVSIEDVE
     FFWNTSASHY PIPHEVAEIL SKRSLIEAVI LIRVVLWLLA TRLGTFLLCG LLCFSEKWPF
     INNFSSMSLK KRERVMQWWL KNRFITPIRL AFAYLKVLCL FAYFTWVDEN GDNPAWKAIG
     YEVSADEKLP NSSNGRLLEK GIVETMHETN STLQQSLTEK GLNVTLDSRN NILKVKCDAI
     VVGSGCGGGV AASVLSGAGH KVVVLEKGNY FAPRDYSSLE GPSMDQLYET GGILASVDSR
     ILLLAGSTVG GGSAVNWSAC IKTPHEVLKE WSENHNLSLF STSEYLSAME TVCERIGVTE
     SCTHEGFQNQ VLRKGCQNLG LKVDYVPRNS SGNHFCGSCG YGCPKGEKQG TQDTWLVDAV
     ENGAVIITGC KAERFLLENN RNGSGRKKKC LGVLAKALSS RVTMKLQIEA KVTISAGGAL
     LTPPLMISSG LKNKNIGKNL HLHPVLMTWG YFPESTSELK GKIFEGGIIT SVHKVPSRDS
     NSYSDTRAII ETPSLGPGSF ASLCPWESGL DFKERMLNYP RTAHLITIIR DKACGQVTTE
     GRVSYKLSAF DKENMKCGLQ QALRILKAAG AVEVGTHRSD GQRVKCGEVS ENEMAEFIDS
     VCPMEGALSP GENWNIYTSA HQMGSCRMGM NEKEGAVDEN GESWEAQGLF VCDASLLPTA
     VGVNPMITIQ STAYCISNRV VDYLKRDQI