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Database: UniProt
Entry: A0A103XFL1_CYNCS
LinkDB: A0A103XFL1_CYNCS
Original site: A0A103XFL1_CYNCS 
ID   A0A103XFL1_CYNCS        Unreviewed;       765 AA.
AC   A0A103XFL1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=Ccrd_008188 {ECO:0000313|EMBL:KVH89826.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH89826.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVH89826.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVH89826.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
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:KVH89826.1}.
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DR   EMBL; LEKV01005137; KVH89826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103XFL1; -.
DR   STRING; 59895.A0A103XFL1; -.
DR   EnsemblPlants; KVH89826; KVH89826; Ccrd_008188.
DR   Gramene; KVH89826; KVH89826; Ccrd_008188.
DR   OMA; CFQGCKW; -.
DR   Proteomes; UP000243975; Unassembled WGS sequence.
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: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|PIRNR:PIRNR028937};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR028937};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          300..521
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          618..745
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        692
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT   BINDING         253..268
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ   SEQUENCE   765 AA;  84484 MW;  F64FDD34BDA96CB4 CRC64;
     MEEQRCVDEK SWIKNDDTEK EEYTILQIDT PLQEDNQRDS EHTHSFSSRQ MEVIVALCDT
     LLPSINISND RLLDDSLLNL YHTSASMIGI PLQVAMMMST KTEHPKQFLV QLSLWLLSTA
     MGTLILCGRG SLSNQFPYVQ KFSRVSSKER EAILVSWSVS YFFLLRMLFR ALKFVNEKNE
     NPSWKAIDYC GPDPDFVPQI SHAFNTDDIL GPLYTAVVCL NKPRQMVAEA LQRSRLAISI
     PRHPKLTSMV IKCDVVVVGS GSGGGVVAGV LAKSGYKVLV LEKGNYRARS NLSLLEGPSM
     DEMYLGKGLL ATSNMEAVIL AGSTVGGGSA INWSASIRTP QHVLKEWSEC YELELFQSGL
     YEEAMDVICE RMGVQSEIED EGFNNTILRK GCEELGYPVN NIPRNSPPDH YCGWCCLGCK
     DGRKKGTSET WLVDVVESGN GAILPGCEAV KVVHDRKKGR ERSTARGVMF EFRHQDGSKE
     VCLVESKVTI VSCGAMCTPQ LLKRSGLKNP SIGKNLHIHP VAMAWGHFPL ERWPEVEKKS
     YKGGIMTAMS TVVADFKGSG YGAIIQTPAL HPGMFSALMP WVSGSDFKNR MTKFSRTAHI
     FALARDKGSG ELGQKSSISY QMDIIDEENL KRGLEKSLRI LAAAGAEEIG THNNKGRTIN
     VKKVSYRELE KFVREESSRA LRDLSTPICS AHQMGSCRMG VTGKGSAVNP MGETWEVEGL
     YVADASVFPT ALGVNPMVTV QAIAYCTAQS VLESLKRMKD TGYGI
//
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