ID K4A658_SETIT Unreviewed; 761 AA.
AC K4A658;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=101767034 {ECO:0000313|EnsemblPlants:KQK88742};
GN ORFNames=SETIT_9G224200v2 {ECO:0000313|EMBL:RCV42530.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK88742, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV42530.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK88742,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV42530.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV42530.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV42530.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK88742}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK88742};
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; AGNK02005565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003536; RCV42530.1; -; Genomic_DNA.
DR RefSeq; XP_004982881.1; XM_004982824.2.
DR AlphaFoldDB; K4A658; -.
DR STRING; 4555.K4A658; -.
DR EnsemblPlants; KQK88742; KQK88742; SETIT_034362mg.
DR GeneID; 101767034; -.
DR Gramene; KQK88742; KQK88742; SETIT_034362mg.
DR KEGG; sita:101767034; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_1_1; -.
DR InParanoid; K4A658; -.
DR OMA; HERFYLA; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000004995; Chromosome IX.
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:SF2; OS10G0475100 PROTEIN; 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:UP000004995};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 154..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..522
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 612..746
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 761 AA; 82297 MW; D1001F5C33EF3AE9 CRC64;
MAVQGEEREK AAAAAAARGH PLLRGWRRDR YTHGMHPAQM EALRAMCGAL IPSLPADGAH
GRGDPPGGKD LERFYRASAA DSTIPDEVAE LMVTRCIREA VALAWVVLWV LSTRVGTLLL
CGRLCLAGGF PYVRKFADMT PERREAALQR WNRVRWLFPL RIAFAIVKIL CHYVFYAMVN
ENSENPYWKA IGYSVHEPRE DQTEAAPSPS RPLDVGVVET RLLDDNALLR SLVGRGLTVK
PVASDANHHV VQCDAVIVGS GCGGGVAAAV LASAGYKVVV VEKGDYFTAS DYSSIEGPSM
ERLFERGGIF CTSNVTTMIF TGATVGGGSA VNWSASIRTP KEVTQEWARE HGLPVFASPG
YAQAMDAVCA RLSVTDGCRE EGFQNKVVRR GCEALGLCAD AVPRNSSEGH FCGSCNFGCP
TGDKRGTDTT WLVDAVASGA VILTGCKAER FVFEKNSGGG RGRGKKCVGL VSTCASDGIT
KKLRIEAKVS IAACGALMTP PLLRNSGLKN RHIGRNLHLH PVSMAWGYFP ENRQDPQLTG
KSYEGGIITS MHRVTERTII ETPALGPGAF AAMVPWESGR DMKERMRRYS RTAHAFALVR
DRGAGFVDGE GRVRFTPSRE DVEELRNGLR RVLRILVAAG AAEVGTHRSD GLRLRCKGLR
DEDLEAFLDE VTIEKGPMHS TADKWALHCS AHQMGSCRMG SSPRDGAVDG RGESWEAEGL
YVCDGSLLPT AVGVNPMITI QSIAYCLSKG IAETLTQGEK Q
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