ID   MBTG_MYCSS              Reviewed;         430 AA.
AC   Q1B6B3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=L-lysine N6-monooxygenase MbtG;
DE            EC=1.14.13.59;
DE   AltName: Full=Lysine 6-N-hydroxylase;
DE   AltName: Full=Lysine N6-hydroxylase;
DE   AltName: Full=Lysine-N-oxygenase;
DE   AltName: Full=Mycobactin synthase protein G;
DE   Flags: Precursor;
GN   Name=mbtG; OrderedLocusNames=Mmcs_3464;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Flavoprotein monooxygenase required for N-hydroxylation of
CC       the two acylated lysine residues during mycobactin assembly, thus
CC       producing the hydroxamate groups necessary for iron sequestration. Is
CC       also able, but less efficiently, to hydroxylate L-lysine (non acylated)
CC       in vitro (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000305}.
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DR   EMBL; CP000384; ABG09571.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1B6B3; -.
DR   SMR; Q1B6B3; -.
DR   KEGG; mmc:Mmcs_3464; -.
DR   HOGENOM; CLU_052650_0_0_11; -.
DR   OMA; QFAEWVD; -.
DR   BioCyc; MSP164756:G1G6O-3534-MON; -.
DR   UniPathway; UPA00011; -.
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; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   Pfam; PF13434; K_oxygenase; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..430
FT                   /note="L-lysine N6-monooxygenase MbtG"
FT                   /id="PRO_0000261311"
SQ   SEQUENCE   430 AA;  46622 MW;  2F943638F21DD3A2 CRC64;
     MTATLAVIGA GPKAVAVAAK AAELRNMGVD APDVVVVERA GVGANWTAAG GWTDGQHRLG
     TSPEKDIGFP YRSSLVPRRN AELDDRMTRH SWQAYLVATS QFAEWIDRGR PAPNHHRWAA
     YLRWVADAIG MNVVHGEVER ISIGGRGWEL HTPESTVAAD AVMITGPGQA ERTLLPGHPR
     VMSIADFWRR TAGHELIVAE RVAMIGGGET AASMLNELFR HRVSTITVIS PQVTLFTRGE
     GFFENTLFSD PTGWTSLTLA ERRDAMFRTD RGVFSARVQE ALLADDRIRH LRGRVAHAVP
     RDGRIRLTLH TDRAGERVET VHGFDLVIDG QGADALWFLP LLGQDARDLL ELGLGGPLTG
     ELLQESIGHD LAVGGVTPKL FLPGLAGLNQ GPGFPNLSCL GLMSDRILGA DLGANAAMTN
     RRSIEHQPIR