ID I1I4N2_BRADI Unreviewed; 786 AA.
AC I1I4N2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 Name=100822554 {ECO:0000313|EnsemblPlants:KQJ97074};
GN ORFNames=BRADI_3g28677v3 {ECO:0000313|EMBL:KQJ97074.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ97074.1};
RN [1] {ECO:0000313|EMBL:KQJ97074.1, ECO:0000313|EnsemblPlants:KQJ97074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ97074.1,
RC ECO:0000313|EnsemblPlants:KQJ97074};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ97074.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ97074.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ97074}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ97074};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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}.
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DR EMBL; CM000882; KQJ97074.1; -; Genomic_DNA.
DR EMBL; CM000882; PNT67535.1; -; Genomic_DNA.
DR RefSeq; XP_003571871.1; XM_003571823.3.
DR AlphaFoldDB; I1I4N2; -.
DR STRING; 15368.I1I4N2; -.
DR EnsemblPlants; KQJ97074; KQJ97074; BRADI_3g28677v3.
DR EnsemblPlants; PNT67535; PNT67535; BRADI_3g28677v3.
DR GeneID; 100822554; -.
DR Gramene; KQJ97074; KQJ97074; BRADI_3g28677v3.
DR Gramene; PNT67535; PNT67535; BRADI_3g28677v3.
DR KEGG; bdi:100822554; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_1_1; -.
DR InParanoid; I1I4N2; -.
DR OMA; HERFYLA; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
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:SF2; OS10G0475100 PROTEIN; 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 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR028937-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR028937};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR028937};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 270..303
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 316..543
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 637..771
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT BINDING 269..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ SEQUENCE 786 AA; 84768 MW; 96538AD33E2A8355 CRC64;
MAVQGEEGRK EEKAAAGRRA GPHPLLRGWR REGKYTHGMH PAQMEALRAI CGAFIPSMPA
EEAAGAGGRA DPPPGGKDLE RFYLASAADS TIPDEVAELM VTRCIREAVL LAWVVLWVLS
TRVGTLLLCG RLSLSFSGGA RDFSFPCVSR FADMPVARRE AALQRWNSTR WLLPLRIVFT
LVKILSHYVF YAMVNEKSEN PHWKAIGYRV DKRRTEQADD AAAKSPSPSR PLDSGVVETR
ALNDTTLLRS LADRGLAVSS DARHHTVQCD AVIVGSGCGG GVAAAMLASA GLKVVVLEKG
DYFTAEDYSS VEGPSMERLF EKGGIFCTSN VTTMVFTGST VGGGSAVNWS ASIRTPGTVL
QEWSQEHGLP VFGSDGYVQA MDAVCSRLAV TDACLEEGFQ NKVVRRGCEA LGLPVDAVPR
NSSAGHYCGS CNFGCPTGDK RGTDTTWLVD AVEHGAVILT GCKADRFILE SNTADTGGKD
NARRSKKCVG LVATCMSNGI TKKLRIEARV SISACGALMT PPLLRNSGLR NRHIGRNLHL
HPVSMAWGYF SDNKLPTSGQ TIITGKSYEG GIITSMHRIT DRTIVETPAL SPGAFAAMVP
WESGRDMKER MRRYARTAHA FALVRDRGAG FVDCEGRLRF TPSRDDTDEL RNGLRRVLRI
LVAAGAAEVG THRSDGLRLR CKGVRDEDLE AFLDEVTIEK GPMHSTTDKW ALFSSAHQMG
SCRMGSSPRE GAVDGSGESW EAEGLYVCDG SLLPTAVGVN PMITIQSVAY CLSKDIAQAL
AHGKKH
//
