ID A0A0Q8UYA9_9ACTN Unreviewed; 646 AA.
AC A0A0Q8UYA9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=long-chain-alcohol oxidase {ECO:0000256|ARBA:ARBA00013125};
DE EC=1.1.3.20 {ECO:0000256|ARBA:ARBA00013125};
GN ORFNames=ASE19_15785 {ECO:0000313|EMBL:KRC50079.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC50079.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC50079.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC50079.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC50079.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC50079.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRC50079.1}.
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DR EMBL; LMIP01000013; KRC50079.1; -; Genomic_DNA.
DR RefSeq; WP_056893547.1; NZ_LMIP01000013.1.
DR AlphaFoldDB; A0A0Q8UYA9; -.
DR OrthoDB; 9798604at2; -.
DR Proteomes; UP000051414; 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; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000051414};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 204..414
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 499..635
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 646 AA; 67836 MW; 045DB6BF572D8533 CRC64;
MVFTPRQVRA MGLIADTFAT GGDGVPSPTQ VGSHELALRI AEANPRAGEL RQLKALLDLW
DTRALGLALT GRPRRFSQLD QAGREQVLLS LSDAKVGAKR ALFQGLKTAS LFPYYMTGGD
ALWDGIGYPG PLGTADTPPP AVLTPEQVTR DSDLSCDVVV VGSGAGGGTA AGVLAASGLD
VVVLEAGGFH DERDFDGGEE TGFLQLYALA PQSTAEGQVQ LVAGRGLGGG TVVNYTTSFR
TPDHVREEWA SHGATQFSGE EYAASMDAVC ARLGVNTDHD KAAPRDAILE RGARALGWDV
DAMPRNVQGC DQDVECGRCG MGCRIGAKQS TAKTWLADAA AAGARILTGV DVRTVSTSFG
RATGVVATTA EGHRVRVRAR AVVVAAGAVQ TPALLQRSGL SNPNIGRYLR LHPATAVWGR
MDEPVDGWVG SMQSRYVDAH TDLDGTGYGV LYETAPLTPG FGTGFVNWRG SDDFRRRMVE
LKHTLGVAVI VRDRDPGGTV RIGRDGEPVV RYQLSPRDTD HLVQGLVGGA RIAEAAGANW
IATTHHRTVS YEPGRRGSID TFESDIRTAG AAPATMALAA LHIMGTARMG GSALSSAVDP
DGQTWDVPGL YVADASCFPT ASGVNPMISI ESIAHMTATR LAARLA
//
