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Database: UniProt
Entry: M3DGL6_9ACTN
LinkDB: M3DGL6_9ACTN
Original site: M3DGL6_9ACTN 
ID   M3DGL6_9ACTN            Unreviewed;       428 AA.
AC   M3DGL6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=H114_10011 {ECO:0000313|EMBL:EMF29100.1};
OS   Streptomyces gancidicus BKS 13-15.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX   NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF29100.1, ECO:0000313|Proteomes:UP000011732};
RN   [1] {ECO:0000313|EMBL:EMF29100.1, ECO:0000313|Proteomes:UP000011732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF29100.1,
RC   ECO:0000313|Proteomes:UP000011732};
RX   PubMed=23599292;
RA   Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT   "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL   Genome Announc. 1:E00150-13(2013).
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:EMF29100.1}.
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DR   EMBL; AOHP01000052; EMF29100.1; -; Genomic_DNA.
DR   RefSeq; WP_006131547.1; NZ_AOHP01000052.1.
DR   AlphaFoldDB; M3DGL6; -.
DR   PATRIC; fig|1284664.3.peg.2006; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000011732; 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; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR   PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:EMF29100.1};
KW   Oxidoreductase {ECO:0000313|EMBL:EMF29100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011732}.
SQ   SEQUENCE   428 AA;  48300 MW;  880F267AA5486887 CRC64;
     MTALADTTVH DFVAIGLGPF NLGLACLTEP IDELDGVFLE SKPDFEWHAG MFLDGAHLQT
     PFMSDLVTLA DPTSPYSFLN YLKEKGRLYS FYIRENFYPL RVEYDDYCRW AAAQLGSVRF
     GTTVTEVTWD ETAEVYVVAT DTGATYRGRH LVLGTGTVPY VPEPCRGLEG GLFHNARYTR
     RKAELLTKKS VTIVGSGQSA AEIYYELLSE IDAHGYQLNW VTRSPRFFPL EYTKLTLEMT
     SPDYIDYFRA LPEDTRYRLE KQQKGLFKGI NSDLIDAIFD LLYQKNVESG GRGVPTRLLT
     NSSLTSARYE DGTYTLGFRQ DEQGKDFEIA TEGLVLATGY HYEQPAFLEP VRDRLRFDSH
     GRFDVARNYA IDVTGRGVFL QNAGVHTHSI TSPDLGMGAY RNASIIRELL GAEYYPVEKS
     IAFQEFAV
//
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