ID D8TGC3_SELML Unreviewed; 656 AA.
AC D8TGC3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125};
DE EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125};
DE Flags: Fragment;
GN ORFNames=SELMODRAFT_138935 {ECO:0000313|EMBL:EFJ04292.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ04292.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- FUNCTION: Long-chain fatty alcohol oxidase involved in the omega-
CC oxidation pathway of lipid degradation.
CC {ECO:0000256|ARBA:ARBA00003842}.
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; GL378008; EFJ04292.1; -; Genomic_DNA.
DR RefSeq; XP_002994642.1; XM_002994596.1.
DR AlphaFoldDB; D8TGC3; -.
DR EnsemblPlants; EFJ04292; EFJ04292; SELMODRAFT_138935.
DR Gramene; EFJ04292; EFJ04292; SELMODRAFT_138935.
DR KEGG; smo:SELMODRAFT_138935; -.
DR eggNOG; ENOG502QSD8; Eukaryota.
DR HOGENOM; CLU_008878_1_0_1; -.
DR InParanoid; D8TGC3; -.
DR OMA; ASEVWPE; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 194..410
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 507..642
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 589
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT BINDING 146..161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFJ04292.1"
SQ SEQUENCE 656 AA; 71588 MW; B37A88CA3104B78F CRC64;
LLLCGAESTD KAYPYDKKFS EVPLEEREKL MYQWANSDDD DSRLNFKIFK TFILNTFYSK
VDASGYNPTW EAIGYAGPDP NSMKATLPPK PSALKSAVFD VREHPDLRAV LKHTGYTLLD
DISHLKPALL PSNKLEDGED VIGIKCDVII VGAGSGGSVP AQVLSTAGLK VLLLEKGRYF
AREDLSLLEQ PTFSELYEEG GFLATDDFAY SLMSAAVVGG GTCINWAASF QTPPHVRQEW
AEECGLPMFT SEKYQQALDL ICKKIGVQPN ATVESFQNAV LRKGCVELGL HSANIPRNAS
PEHYCGCCNM GCRRGMKQAT TETWLVEAAA AGATILTGTK GLQVLFTDGT KKEKKAIGVL
ATTLGDQPKK LIIEAKATIV STGSIMTPPL LIRSGLTNPN IGKHFHIHPV LGVWGYFPEE
EKNPGASFEG GIMTAFSAVS ARWDTVGYGP VLMTPSFHPG QYASVVTWKS GAQHKEAMRR
FRRVSQVVLF TRDKGAGSIG VDKKTDEITI EYTLDPYDEE VCLEGAEKGL RVLKAAGAVE
VGTHHHDAES FTFGKSTSWK EEKKRFEEYL ASVRSKGLKP NRLPMVSYHL LGSCRMGSSP
ENSVIDAKGE TWDAEGLFLT DASVFPTPTG LNPMVTIQSI AYCTAQNIVE HVKSSK
//
