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Database: UniProt
Entry: A0A445DZE0_ARAHY
LinkDB: A0A445DZE0_ARAHY
Original site: A0A445DZE0_ARAHY 
ID   A0A445DZE0_ARAHY        Unreviewed;       749 AA.
AC   A0A445DZE0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=Ahy_A03g015026 {ECO:0000313|EMBL:RYR68530.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR68530.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR68530.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR68530.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC       oxidation pathway of lipid degradation. {ECO:0000256|ARBA:ARBA00003842,
CC       ECO:0000256|PIRNR:PIRNR028937}.
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   -!- SUBCELLULAR LOCATION: Membrane {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:RYR68530.1}.
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DR   EMBL; SDMP01000003; RYR68530.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445DZE0; -.
DR   STRING; 3818.A0A445DZE0; -.
DR   OrthoDB; 601859at2759; -.
DR   Proteomes; UP000289738; Chromosome a03.
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; 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:SF7; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 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|PIRNR:PIRNR028937};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR028937};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          285..508
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          604..736
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        683
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT   BINDING         238..253
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ   SEQUENCE   749 AA;  82275 MW;  D24614DABD3B64F0 CRC64;
     MVRRECHPLL KGERGERKYR HGFFGYEMES LASICEVVIP PLPPLKDEED ELNNKDVTKS
     FSNISASQHP YPHEVAEILV KRGLIEAVIL IRVILWVLAT RLGTLLLCGS LSFGGKWPFI
     NNFSNMGLEK REKVVQKWLK HRFLTPIRLA FAYIKVLCVY CFFSSVDEKG DNPAWKAIGY
     EVAADEKQKN VSNNKRPLQK GIIETMQEQS DSTLQQSLAK KGLNVTMDTK TNTLKLKCDA
     VVVGSGCGGG VAASVLSSAG HKVVVLEKGN YFASQDYSSL EGPSMDQLYE TGGILASVDS
     RILVLAGSTV GGGSAVNWSA CIKTPQNVMK EWSEEHKLPL FSSLEYQSAM ETVCERIGVT
     EFCKQEGFQN QVLRKGCQNL GLKVDYVPRN SSGNHYCGSC GYGCPKGEKK GTQETWLVDA
     VESGAVIITG CKAEKFLLQT NTNGRRSERK NKCFGVLAKA LSSRITMKLQ IEAKVTVSAG
     GALLTPPLMI SSGLRNKNIG RNLHLHPVLM TWGYFPDSNS ELEGKVFEGG IITSVHKVPP
     RDSESSDTRA IIETPLLGPA SFASLCPWES GRDFKERMLK YPRTSHLITI IRDTACGVVT
     SEGRISYKLS EMDKENMRIG LQQALRILIA AGAVEVGTHR SDGQRIKCGD IGYGKIEEFL
     DSVWPMEGAL SPGEKWNIYC SAHQMGSCRM GATEKEGGVD ENGESWEAEG LFVCDASLLP
     SAVGVNPMIT IQSTAYCVSN RIVDYLKNL
//
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