ID   MBTG_MYCTU              Reviewed;         431 AA.
AC   P9WKF7; L0TCC4; O05820; Q7D793;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=L-lysine N6-monooxygenase MbtG;
DE            EC=1.14.13.59 {ECO:0000269|PubMed:16461464};
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=Rv2378c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16461464; DOI=10.1073/pnas.0507924103;
RA   Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.;
RT   "A genetic locus required for iron acquisition in Mycobacterium
RT   tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. Shows 5-fold preference for using acetylated lysine over
CC       lysine. {ECO:0000269|PubMed:16461464}.
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:0000269|PubMed:16461464};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:16461464};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000305|PubMed:16461464}.
CC   -!- INDUCTION: Induced by iron starvation conditions and during infection
CC       of human THP-1 macrophages. Transcriptionally repressed by ideR and
CC       iron (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP45166.1; -; Genomic_DNA.
DR   PIR; A70588; A70588.
DR   RefSeq; NP_216894.1; NC_000962.3.
DR   RefSeq; WP_003899296.1; NZ_NVQJ01000029.1.
DR   AlphaFoldDB; P9WKF7; -.
DR   SMR; P9WKF7; -.
DR   STRING; 83332.Rv2378c; -.
DR   PaxDb; P9WKF7; -.
DR   DNASU; 885648; -.
DR   GeneID; 885648; -.
DR   KEGG; mtu:Rv2378c; -.
DR   TubercuList; Rv2378c; -.
DR   eggNOG; COG3486; Bacteria.
DR   OMA; QFAEWVD; -.
DR   BioCyc; MetaCyc:G185E-6604-MON; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0047091; F:L-lysine 6-monooxygenase (NADPH) activity; IDA:MTBBASE.
DR   GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; IDA:MTBBASE.
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; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..431
FT                   /note="L-lysine N6-monooxygenase MbtG"
FT                   /id="PRO_0000261312"
SQ   SEQUENCE   431 AA;  46944 MW;  8D200693CB6D4EB0 CRC64;
     MNPTLAVLGA GAKAVAVAAK ASVLRDMGVD VPDVIAVERI GVGANWQASG GWTDGAHRLG
     TSPEKDVGFP YRSALVPRRN AELDERMTRY SWQSYLIATA SFAEWIDRGR PAPTHRRWSQ
     YLAWVADHIG LKVIHGEVER LAVTGDRWAL CTHETTVQAD ALMITGPGQA EKSLLPGNPR
     VLSIAQFWDR AAGHDRINAE RVAVIGGGET AASMLNELFR HRVSTITVIS PQVTLFTRGE
     GFFENSLFSD PTDWAALTFD ERRDALARTD RGVFSATVQE ALLADDRIHH LRGRVAHAVG
     RQGQIRLTLS TNRGSENFET VHGFDLVIDG SGADPLWFTS LFSQHTLDLL ELGLGGPLTA
     DRLQEAIGYD LAVTDVTPKL FLPTLSGLTQ GPGFPNLSCL GLLSDRVLGA GIFTPTKHND
     TRRSGEHQSF R