ID   A0A0Q5R0B2_9SPHN        Unreviewed;       553 AA.
AC   A0A0Q5R0B2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Cyclohexanone monooxygenase {ECO:0000313|EMBL:KQS03600.1};
GN   ORFNames=ASG11_04495 {ECO:0000313|EMBL:KQS03600.1};
OS   Sphingomonas sp. Leaf357.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736350 {ECO:0000313|EMBL:KQS03600.1, ECO:0000313|Proteomes:UP000051080};
RN   [1] {ECO:0000313|EMBL:KQS03600.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03600.1,
RC   ECO:0000313|Proteomes:UP000051080};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS03600.1, ECO:0000313|Proteomes:UP000051080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf357 {ECO:0000313|EMBL:KQS03600.1,
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:KQS03600.1}.
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DR   EMBL; LMPM01000001; KQS03600.1; -; Genomic_DNA.
DR   RefSeq; WP_055775696.1; NZ_LMPM01000001.1.
DR   AlphaFoldDB; A0A0Q5R0B2; -.
DR   STRING; 1736350.ASG11_04495; -.
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:KQS03600.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051080}.
SQ   SEQUENCE   553 AA;  61171 MW;  4B7596318BB142BE CRC64;
     MVQTATIETG RQHPARRRLD ALVVGMGFGG MCMLHTAREA GLDVHAIEAG DDVGGTWYWN
     RYPGARCDVM SIDYSYSFLN ELQQEWTWSE KFAAQPEILA YASFVAEKLD LRRDTSFSTR
     ATSVVFDDAH NMWVVETDQG QIYEATYCIM ATGPLSIPKG IDVPGQEKFG GEIYLTGRWP
     HGTVDFTGKR VGIIGTGSSG IQAIPVVAEQ AEHLTVFQRT PSFTIPMRNS KLTPEYMAQV
     KEHYPRLRTI AKATHTGGMR PVSTRPMFSV TTEEAQQLLE DGWNAGGQTI FGLFSDLLYD
     QQTNDVVAAF VRGKIREAVN DPHTAEVLTP HGYPIFSRRP CLDTNYYETF NRDNVLLVDC
     INEPIEEIIE TGIRTGKRDI PLDIIIGATG YDGLTGAMLA VDIKGRGGRS LREKWAGGAH
     SYLGLMMEGF PNLFMIAGAN GPSALANFVI LNEQNADWIT RCILNMRASG QATIEPTIEA
     EDRYMDLLIE IAGRSLIPKA KSWYVGANIP GKANFFPIFA GGFARYIDMC NAAASDNYAG
     FVFKDQRSLV NQD
//