ID   A0A0Q5QWG7_9SPHN        Unreviewed;       531 AA.
AC   A0A0Q5QWG7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:KQS03660.1};
GN   ORFNames=ASG11_04885 {ECO:0000313|EMBL:KQS03660.1};
OS   Sphingomonas sp. Leaf357.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS03660.1, ECO:0000313|Proteomes:UP000051080};
RN   [1] {ECO:0000313|EMBL:KQS03660.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03660.1,
RC   ECO:0000313|Proteomes:UP000051080};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS03660.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03660.1,
RC   ECO:0000313|Proteomes:UP000051080};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00010139}.
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:KQS03660.1}.
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DR   EMBL; LMPM01000001; KQS03660.1; -; Genomic_DNA.
DR   RefSeq; WP_055775872.1; NZ_LMPM01000001.1.
DR   AlphaFoldDB; A0A0Q5QWG7; -.
DR   STRING; 1736350.ASG11_04885; -.
DR   OrthoDB; 312624at2; -.
DR   Proteomes; UP000051080; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:KQS03660.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051080}.
SQ   SEQUENCE   531 AA;  57969 MW;  7EDEC762031DEB70 CRC64;
     MDPREIDVVV VGAGFAGLYM IHKLRTLGFG VQGFEAGADV GGTWYFNRYP GARCDVESFD
     YSYSFDSEIE QEWNWTERFA TQPEILRYIR HVADRLDLRR DIRFSTRVAA ATWNEDQRRW
     QVTTDAGEMV AARYLILATG SLSAAKAPEI AGLDSFGGET LHTSSWPEEG VDFTGQRVGI
     IGTGSSAIQA IPLIAQQADH LTVFQRTPAF SLPARNAPLD DAAIAARKHE YRRHRARCRA
     TQAGVLFRGT DVPALSMGEE ERRAAYETAW ANGGQDFVRT FKDLILNRAA NDTASCFVRE
     KIAEVVADPA TAAALTPRDF PIGSKRVAVD TDYYETFNRP NVSLVNLRDT PIERIEASGV
     RTRAGVVPLD ALILATGFDA ITGSFLRIAI TNGDGATLAE KWAAGPQTYL GLGMAGFPNL
     FIVAGPGSPS VLVNMVLAGE QHVEWIADCL VSLRTRGLTR IEAQADAERK WVDRVNALAN
     KTLFMAGDSW YLGANVPGKP RVFMPFVGGF ASYAAICDDV AGKGYEGFTL S
//