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Database: UniProt
Entry: A0A3P1WKR2_9ACTN
LinkDB: A0A3P1WKR2_9ACTN
Original site: A0A3P1WKR2_9ACTN 
ID   A0A3P1WKR2_9ACTN        Unreviewed;       353 AA.
AC   A0A3P1WKR2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=L-lysine N6-monooxygenase MbtG {ECO:0000256|ARBA:ARBA00016406};
DE            EC=1.14.13.59 {ECO:0000256|ARBA:ARBA00013076};
DE   AltName: Full=Lysine 6-N-hydroxylase {ECO:0000256|ARBA:ARBA00032738};
DE   AltName: Full=Lysine N6-hydroxylase {ECO:0000256|ARBA:ARBA00032493};
DE   AltName: Full=Lysine-N-oxygenase {ECO:0000256|ARBA:ARBA00029939};
DE   AltName: Full=Mycobactin synthase protein G {ECO:0000256|ARBA:ARBA00031158};
GN   ORFNames=EII42_02980 {ECO:0000313|EMBL:RRD47239.1};
OS   Tessaracoccus sp. OH4464_COT-324.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=2491059 {ECO:0000313|EMBL:RRD47239.1, ECO:0000313|Proteomes:UP000274803};
RN   [1] {ECO:0000313|EMBL:RRD47239.1, ECO:0000313|Proteomes:UP000274803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OH4464_COT-324 {ECO:0000313|EMBL:RRD47239.1,
RC   ECO:0000313|Proteomes:UP000274803};
RA   Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA   Eisen J.A., Holcombe L.J., O'Flynn C.;
RT   "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT   for Automated Genome-Based Taxonomic Assignment.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+);
CC         Xref=Rhea:RHEA:23228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57783, ChEBI:CHEBI:57820,
CC         ChEBI:CHEBI:58349; EC=1.14.13.59;
CC         Evidence={ECO:0000256|ARBA:ARBA00000168};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
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:RRD47239.1}.
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DR   EMBL; RQYZ01000003; RRD47239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P1WKR2; -.
DR   OrthoDB; 5168853at2; -.
DR   Proteomes; UP000274803; Unassembled WGS sequence.
DR   GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274803}.
SQ   SEQUENCE   353 AA;  38809 MW;  7EDD293501363D6A CRC64;
     MNRGVVREAW QEHETIPCAV VGSGLFGIMA VRELTRRGLD VDWYSADSEP GGIWQGFPHG
     KARGSTELVN PGWCISRRFW RIRPVGAAEF LDELVRWADE RRDKQFRYFG SSVNMVEESS
     EGVLVTSDRG AKRYLFLVVA TGHYGKPMIP FPYSGKRVVH ASILSDLSSV GVGDRVLVVG
     GGQSGVEICE ELLATLPMIR PTWVTSRKVL LISRLSFLGI VGTCLSYRTA EEAPRGFVIT
     KDSGRVRSRC DIRPVRVERV EEETVYFSDG TTGCFEHVIA ATGYLPPEKL AFPASVRGKS
     KGMRVSIGGH IVSLNHFGDG CAGASVRCAR RQAREVGRLV TEVLAQHRLA GSP
//
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