ID A0A0D2NAX8_GOSRA Unreviewed; 749 AA.
AC A0A0D2NAX8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=B456_001G179800 {ECO:0000313|EMBL:KJB10008.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB10008.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB10008.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001740; KJB10008.1; -; Genomic_DNA.
DR RefSeq; XP_012483683.1; XM_012628229.1.
DR AlphaFoldDB; A0A0D2NAX8; -.
DR STRING; 29730.A0A0D2NAX8; -.
DR EnsemblPlants; KJB10008; KJB10008; B456_001G179800.
DR GeneID; 105798235; -.
DR Gramene; KJB10008; KJB10008; B456_001G179800.
DR KEGG; gra:105798235; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000032304; Chromosome 1.
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:SF12; LONG-CHAIN-ALCOHOL OXIDASE FAO4B; 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:UP000032304};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..277
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 289..510
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 604..734
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 242..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ SEQUENCE 749 AA; 82136 MW; E63A3AF5657DBD7C CRC64;
MEIGNHETGD AHPLLRGGRR KTTYTHGFSS AQIQSLAAIC EALIPPLPLD SAHQASSLDA
FYKASGAEPP LPDEVAEMMV KRVVEPRVLS FVKVVLTVIS FRLGALLLCG WDCCDWKWPF
IHKFSELPVE RREKILMKWS SNGHHRLPLR AVFALIKTYC LFIFFSMLLK FVSQTDEKSE
NPSWKAIGYN VDKRQKRVSS PHGRKGIIET MHEDDSTFVQ SLTEKGLQVT EDPDHNVFNI
KCDVVIVGSG CGGGVAAAVL ASSGQKVVVI EKGNYFATTD YTSLEGPSMS ELYEYGGFLT
TTNGKFMIMA GSTVGGGSAI NWSASIKTPN NVLKEWSLDH KIPLFGSSEY ENAMDAVYQR
LGVTENCTEE GLQNQVLRKG CENLGLKVEA VPRNSPEDHY CGSCNLGCRT GDKKGTATTW
LVDAQGYGAV ILTACKADRL MLVNNNEDAR RRKKCLGVVA TSLNKNLTKK LQFEAKTTIS
ACGSLLTPPL MISSGLKNPN IGRNLHLHPA LVAWGYFPED ETGIKGKSYE GGIITSFNRI
VSEESNNVHA IIQAPALGPA SFAAISPWVS GRELKERMVR YPRLAHLFTL IRDQGSGEVM
EEGKIKYRLS EVDKENLKIG LRQVLRVLIA AGAVEVGTHR SDGQRIKCKG LTEESLQEFL
DNVPVVGGLS SKDEYWTLYL TAHQIGSCRM GATEEEGAVD ENGQSWEAEG LFVCDASVLP
TAIGVNPMIT IQSTSYCISN KIAQLLKKE
//
