LCAO_UNCAR
ID LCAO_UNCAR Reviewed; 479 AA.
AC A0A075HNX4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Long-chain alcohol oxidase {ECO:0000303|PubMed:34709726};
DE Short=LCAO {ECO:0000303|PubMed:34709726};
DE EC=1.1.3.20 {ECO:0000269|PubMed:34709726};
OS Uncultured marine euryarchaeote.
OC Archaea; Euryarchaeota; environmental samples.
OX NCBI_TaxID=257466;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KM3_72_H01 / Group II/III;
RX PubMed=24923324; DOI=10.1093/gbe/evu127;
RA Deschamps P., Zivanovic Y., Moreira D., Rodriguez-Valera F.,
RA Lopez-Garcia P.;
RT "Pangenome evidence for extensive interdomain horizontal transfer affecting
RT lineage core and shell genes in uncultured planktonic thaumarchaeota and
RT euryarchaeota.";
RL Genome Biol. Evol. 6:1549-1563(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=34709726; DOI=10.1002/cbic.202100510;
RA Rembeza E., Boverio A., Fraaije M.W., Engqvist M.;
RT "Discovery of two novel oxidases using a high-throughput activity screen.";
RL ChemBioChem 0:0-0(2021).
CC -!- FUNCTION: In vitro catalyzes the oxidation of a range of fatty alcohols
CC having a carbon chain length of six and above, with a reduction of O2
CC to H2O2. Shows the highest activity with 1-dodecanol. Is likely
CC involved in lipid metabolism. {ECO:0000269|PubMed:34709726}.
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:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecan-1-ol + O2 = dodecanal + H2O2; Xref=Rhea:RHEA:69484,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:27836,
CC ChEBI:CHEBI:28878; EC=1.1.3.20;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + tetradecan-1-ol = H2O2 + tetradecanal;
CC Xref=Rhea:RHEA:69488, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:77417, ChEBI:CHEBI:84067;
CC Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + octan-1-ol = H2O2 + octanal; Xref=Rhea:RHEA:69492,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16188, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17935; Evidence={ECO:0000269|PubMed:34709726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decan-1-ol + O2 = decanal + H2O2; Xref=Rhea:RHEA:69496,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28903,
CC ChEBI:CHEBI:31457; Evidence={ECO:0000269|PubMed:34709726};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9ZBU1};
CC Note=Binds 1 FAD covalently per subunit.
CC {ECO:0000250|UniProtKB:Q9ZBU1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.7 uM for 1-dodecanol {ECO:0000269|PubMed:34709726};
CC pH dependence:
CC Optimum pH is 8-9. Shows almost no activity at pH 5.
CC {ECO:0000269|PubMed:34709726};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:34709726}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; KF901047; AIF16132.1; -; Genomic_DNA.
DR UniPathway; UPA00199; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050105; F:L-gulonolactone oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046577; F:long-chain-alcohol oxidase activity; IEA:RHEA.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43762; PTHR43762; 2.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cell membrane; FAD; Flavoprotein; Membrane; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="Long-chain alcohol oxidase"
FT /id="PRO_0000455050"
FT TRANSMEM 241..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 14..183
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 120..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT BINDING 425
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
FT MOD_RES 49
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZBU1"
SQ SEQUENCE 479 AA; 54379 MW; 176E64C8EAB988FC CRC64;
MAQGAQRKNF GHNQILRPSA AYTPVDEQEV LQILDRHRGQ RIRAVGRLHS WSEAVTGDGV
LLDLQRLNDV RLQSDGDQLV ATVGAGCQIK RLLKELNREG ATLHSLGLIT AQTIAGAIST
GTHGSGRNSM SHYVVGVRLA CYDASTGQAI IEELSAGEPL QAARCSLGSL GIILAVRIRC
REQYNVQEHF TESRRLLDVM DAEAPFPLQQ FYLLPWRWSY FIQHRREDDR PRSRLARLYR
LYWLGTMDYG LILQILFLER VARSRRLIRL AFRRIIPAFL IRNWRVTDRS SSMLVMRHDA
FRHIEIELFV RRDQLADALG FTQEVIKIAG GRESALSADN QRRIEELGMQ EALAGLHDQY
CHHFPICVRR VLPDDTLISM ASGAGEDWYA LSFISYAKPA RRAGFSLFAS FMARSMSRLF
HARPHWGKVC PLEADELTSL YPRFDAFRTV CNTLDPQGVF QNDWTTALLE ADGQVGDFP
