ID A0A0K9PD64_ZOSMR Unreviewed; 769 AA.
AC A0A0K9PD64;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ZOSMA_2G01470 {ECO:0000313|EMBL:KMZ66135.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ66135.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(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:KMZ66135.1}.
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DR EMBL; LFYR01000981; KMZ66135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PD64; -.
DR STRING; 29655.A0A0K9PD64; -.
DR OMA; CFQGCKW; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000036987; 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; 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:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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:UP000036987};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 250..282
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 297..516
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 628..753
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 701
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-1"
FT BINDING 249..264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR028937-2"
SQ SEQUENCE 769 AA; 84434 MW; 1AD258D6936C4EBC CRC64;
MVSSSEEVEN VPFYADMTGN SLKGGQSRYP NIISKKEMLT ITALCETFLP SLDVSSSTTT
PKSIVDFYGT SAVMTRTDEE LGGLLSGRLK HRALGLIRLV LWLLSTWWGT LAICGTRCLS
DKFPYVQNFP AVGQEQRVKI VLSWSLSSFF LFRMLFKALK FTTMVLFFSQ ANENNQNPSW
KTMGYCGPDP NHINPDRKTT RDFVDEKDGP LRDFVVDAAH EEELLARAFK QMGFSTTAST
DSTCFTVNCD AVVVGSGTGG SVVAGKLAKA GHKVIVVEKG RYYSRRNLSL LEGPSLDQMY
EGNGFLCTDD LSMLILAGST VGGGSTINWS ASIRTPEHVL NEWCDEHELK LFGSNAFHHA
LDAVCDRMGV QGEVTDEGFN NAILRKGCEE LGYPVTTVGR NAPKDHNCGW CHLGCRDGRK
KSVQETWLSD MVNSGNGVIL QGCNVSRVLH RTKRGKSRNV AGGIVAEFGE KKKKQRIVIS
SIVTVVAGGA LNTPALLKRS GLNNANIGKN LHLHPVVMAW GHFPETTDDL SNNEDKRSNA
VIFPEKKSFE GGIITSMSTI DSSFKTSGYG AVIQTPALHP GVFSALMPWV SPLDFRHRMR
KFSRTAHLFA LARDRGSGSA PDYPNKLWYS LDPRDEEKLQ KGIERMLRVL VAAGATEIGT
HNCEGKIFNV KKGSKEELEE FVKEASGKRL RDLSTPLCSA HQMGSCRMGT EISTSVVSPR
CETWEVEGLF VADTSVFPTA LGVNPMITVQ AISFCTAQSI LEVLNRKKI
//
